Patent Publication Number: US-2004043928-A1

Title: Therapeutic polypeptides, nucleic acids encoding same, and methods of use

Description:
RELATED APPLICATIONS  
     [0001] This application claims priority to patent applications U.S. Ser. No. 60/193,664, filed Mar. 31, 2000; U.S. Ser. No. 60/239,613, filed Oct. 11, 2000; U.S. Ser. No. 60/263,604, filed Jan. 23, 2001; U.S. Ser. No. 60/309,501, filed Aug. 2, 2001; U.S. Ser. No. 60/310,291, filed Aug. 3, 2001; U.S. Ser. No. 60/310,544, filed Aug. 7, 2001; U.S. Ser. No. 60/310,951, filed Aug. 8, 2001; U.S. Ser. No. 60/311,292, filed Aug. 9, 2001; U.S. Ser. No. 60/311,979, filed Aug. 13, 2001; U.S. Ser. No. 60/312,892, filed Aug. 16, 2001; U.S. Ser. No. 60/313,201, filed Aug. 17, 2001; U.S. Ser. No. 60/313,415, filed Aug. 17, 2001; U.S. Ser. No. 60/313,702, filed Aug. 20, 2001; U.S. Ser. No. 60/313,643, filed Aug. 20, 2001; U.S. Ser. No. 60/314,031, filed Aug. 21, 2001; U.S. Ser. No. 60/314,466, filed Aug. 23, 2001; U.S. Ser. No. 60/315,403, filed Aug. 28, 2001; U.S. Ser. No. 60/315,853, filed Aug. 29, 2001; U.S. Ser. No. 60/322,716, filed Sep. 17, 2001; U.S. Ser. No. 60/323,994, filed Sep. 21, 2001; U.S. Ser. No. 60/340,233, filed Dec. 14, 2001; U.S. Ser. No. 60/365,478, filed Mar. 19, 2002; U.S. Ser. No. 60/373,814, filed Apr. 19, 2002; U.S. Ser. No. 60/373,825, filed April 19, 2002; U.S. Ser. No. 60/373,989, filed Apr. 19, 2002; and U.S. Ser. No. 60/374,632, filed Apr. 23, 2002; U.S. Ser. No. 60/354,591, filed Feb. 5, 2002; U.S. Ser. No. not yet assigned, filed Jun. 7, 2002 (Docket 15966-748U-C PRO), each of which is incorporated herein by reference in its entirety. 
    
    
     
       FIELD OF THE INVENTION  
       [0002] The present invention relates to novel polypeptides, and the nucleic acids encoding them, having properties related to stimulation of biochemical or physiological responses in a cell, a tissue, an organ or an organism. More particularly, the novel polypeptides are gene products of novel genes, or are specified biologically active fragments or derivatives thereof. Methods of use encompass diagnostic and prognostic assay procedures as well as methods of treating diverse pathological conditions.  
       BACKGROUND OF THE INVENTION  
       [0003] Eukaryotic cells are characterized by biochemical and physiological processes which under normal conditions are exquisitely balanced to achieve the preservation and propagation of the cells. When such cells are components of multicellular organisms such as vertebrates, or more particularly organisms such as mammals, the regulation of the biochemical and physiological processes involves intricate signaling pathways. Frequently, such signaling pathways involve extracellular signaling proteins, cellular receptors that bind the signaling proteins, and signal transducing components located within the cells.  
       [0004] Signaling proteins may be classified as endocrine effectors, paracrine effectors or autocrine effectors. Endocrine effectors are signaling molecules secreted by a given organ into the circulatory system, which are then transported to a distant target organ or tissue. The target cells include the receptors for the endocrine effector, and when the endocrine effector binds, a signaling cascade is induced. Paracrine effectors involve secreting cells and receptor cells in close proximity to each other, for example two different classes of cells in the same tissue or organ. One class of cells secretes the paracrine effector, which then reaches the second class of cells, for example by diffusion through the extracellular fluid. The second class of cells contains the receptors for the paracrine effector; binding of the effector results in induction of the signaling cascade that elicits the corresponding biochemical or physiological effect. Autocrine effectors are highly analogous to paracrine effectors, except that the same cell type that secretes the autocrine effector also contains the receptor. Thus the autocrine effector binds to receptors on the same cell, or on identical neighboring cells. The binding process then elicits the characteristic biochemical or physiological effect.  
       [0005] Signaling processes may elicit a variety of effects on cells and tissues including by way of nonlimiting example induction of cell or tissue proliferation, suppression of growth or proliferation, induction of differentiation or maturation of a cell or tissue, and suppression of differentiation or maturation of a cell or tissue.  
       [0006] Many pathological conditions involve dysregulation of expression of important effector proteins. In certain classes of pathologies the dysregulation is manifested as diminished or suppressed level of synthesis and secretion of protein effectors. In other classes of pathologies the dysregulation is manifested as increased or up-regulated level of synthesis and secretion of protein effectors. In a clinical setting a subject may be suspected of suffering from a condition brought on by altered or mis-regulated levels of a protein effector of interest. Therefore there is a need to assay for the level of the protein effector of interest in a biological sample from such a subject, and to compare the level with that characteristic of a nonpathological condition. There also is a need to provide the protein effector as a product of manufacture. Administration of the effector to a subject in need thereof is useful in treatment of the pathological condition. Accordingly, there is a need for a method of treatment of a pathological condition brought on by a diminished or suppressed levels of the protein effector of interest. In addition, there is a need for a method of treatment of a pathological condition brought on by a increased or up-regulated levels of the protein effector of interest.  
       [0007] Antibodies are multichain proteins that bind specifically to a given antigen, and bind poorly, or not at all, to substances deemed not to be cognate antigens. Antibodies are comprised of two short chains termed light chains and two long chains termed heavy chains. These chains are constituted of immunoglobulin domains, of which generally there are two classes: one variable domain per chain, one constant domain in light chains, and three or more constant domains in heavy chains. The antigen-specific portion of the immunoglobulin molecules resides in the variable domains; the variable domains of one light chain and one heavy chain associate with each other to generate the antigen-binding moiety. Antibodies that bind immunospecifically to a cognate or target antigen bind with high affinities. Accordingly, they are useful in assaying specifically for the presence of the antigen in a sample. In addition, they have the potential of inactivating the activity of the antigen.  
       [0008] Therefore there is a need to assay for the level of a protein effector of interest in a biological sample from such a subject, and to compare this level with that characteristic of a nonpathological condition. In particular, there is a need for such an assay based on the use of an antibody that binds immunospecifically to the antigen. There further is a need to inhibit the activity of the protein effector in cases where a pathological condition arises from elevated or excessive levels of the effector based on the use of an antibody that binds immunospecifically to the effector. Thus, there is a need for the antibody as a product of manufacture. There further is a need for a method of treatment of a pathological condition brought on by an elevated or excessive level of the protein effector of interest based on administering the antibody to the subject.  
       SUMMARY OF THE INVENTION  
       [0009] The invention is based in part upon the discovery of isolated polypeptides including amino acid sequences selected from mature forms of the amino acid sequences selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. The novel nucleic acids and polypeptides are referred to herein as NOVX, or NOV1, NOV2, NOV3, etc., nucleic acids and polypeptides. These nucleic acids and polypeptides, as well as derivatives, homologs, analogs and fragments thereof, will hereinafter be collectively designated as “NOVX” nucleic acid or polypeptide sequences.  
       [0010] The invention also is based in part upon variants of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, wherein any amino acid in the mature form is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed. In another embodiment, the invention includes the amino acid sequences selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. In another embodiment, the invention also comprises variants of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 wherein any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed. The invention also involves fragments of any of the mature forms of the amino acid sequences selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, or any other amino acid sequence selected from this group. The invention also comprises fragments from these groups in which up to 15% of the residues are changed.  
       [0011] In another embodiment, the invention encompasses polypeptides that are naturally occurring allelic variants of the sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. These allelic variants include amino acid sequences that are the translations of nucleic acid sequences differing by a single nucleotide from nucleic acid sequences selected from the group consisting of SEQ ID NOS: 2n−1, wherein n is an integer between 1 and 102. The variant polypeptide where any amino acid changed in the chosen sequence is changed to provide a conservative substitution.  
       [0012] In another embodiment, the invention comprises a pharmaceutical composition involving a polypeptide with an amino acid sequence selected from the group consisting of  
       [0013] SEQ ID NO: 2n, wherein n is an integer between 1 and 102 and a pharmaceutically acceptable carrier. In another embodiment, the invention involves a kit, including, in one or more containers, this pharmaceutical composition.  
       [0014] In another embodiment, the invention includes the use of a therapeutic in the manufacture of a medicament for treating a syndrome associated with a human disease, the disease being selected from a pathology associated with a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 wherein said therapeutic is the polypeptide selected from this group.  
       [0015] In another embodiment, the invention comprises a method for determining the presence or amount of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 in a sample, the method involving providing the sample; introducing the sample to an antibody that binds immunospecifically to the polypeptide; and determining the presence or amount of antibody bound to the polypeptide, thereby determining the presence or amount of polypeptide in the sample.  
       [0016] In another embodiment, the invention includes a method for determining the presence of or predisposition to a disease associated with altered levels of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 in a first mammalian subject, the method involving measuring the level of expression of the polypeptide in a sample from the first mammalian subject; and comparing the amount of the polypeptide in this sample to the amount of the polypeptide present in a control sample from a second mammalian subject known not to have, or not to be predisposed to, the disease, wherein an alteration in the expression level of the polypeptide in the first subject as compared to the control sample indicates the presence of or predisposition to the disease.  
       [0017] In another embodiment, the invention involves a method of identifying an agent that binds to a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, the method including introducing the polypeptide to the agent; and determining whether the agent binds to the polypeptide. The agent could be a cellular receptor or a downstream effector.  
       [0018] In another embodiment, the invention involves a method for identifying a potential therapeutic agent for use in treatment of a pathology, wherein the pathology is related to aberrant expression or aberrant physiological interactions of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, the method including providing a cell expressing the polypeptide of the invention and having a property or function ascribable to the polypeptide; contacting the cell with a composition comprising a candidate substance; and determining whether the substance alters the property or function ascribable to the polypeptide; whereby, if an alteration observed in the presence of the substance is not observed when the cell is contacted with a composition devoid of the substance, the substance is identified as a potential therapeutic agent.  
       [0019] In another embodiment, the invention involves a method for screening for a modulator of activity or of latency or predisposition to a pathology associated with a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, the method including administering a test compound to a test animal at increased risk for a pathology associated with the polypeptide of the invention, wherein the test animal recombinantly expresses the polypeptide of the invention; measuring the activity of the polypeptide in the test animal after administering the test compound; and comparing the activity of the protein in the test animal with the activity of the polypeptide in a control animal not administered the polypeptide, wherein a change in the activity of the polypeptide in the test animal relative to the control animal indicates the test compound is a modulator of latency of, or predisposition to, a pathology associated with the polypeptide of the invention. The recombinant test animal could express a test protein transgene or express the transgene under the control of a promoter at an increased level relative to a wild-type test animal. The promoter may or may not b the native gene promoter of the transgene.  
       [0020] In another embodiment, the invention involves a method for modulating the activity of a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, the method including introducing a cell sample expressing the polypeptide with a compound that binds to the polypeptide in an amount sufficient to modulate the activity of the polypeptide.  
       [0021] In another embodiment, the invention involves a method of treating or preventing a pathology associated with a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, the method including administering the polypeptide to a subject in which such treatment or prevention is desired in an amount sufficient to treat or prevent the pathology in the subject. The subject could be human.  
       [0022] In another embodiment, the invention involves a method of treating a pathological state in a mammal, the method including administering to the mammal a polypeptide in an amount that is sufficient to alleviate the pathological state, wherein the polypeptide is a polypeptide having an amino acid sequence at least 95% identical to a polypeptide having the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 or a biologically active fragment thereof.  
       [0023] In another embodiment, the invention involves an isolated nucleic acid molecule comprising a nucleic acid sequence encoding a polypeptide having an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102; a variant of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 wherein any amino acid in the mature form of the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed; the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102; a variant of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, in which any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed; a nucleic acid fragment encoding at least a portion of a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 or any variant of the polypeptide wherein any amino acid of the chosen sequence is changed to a different amino acid, provided that no more than 10% of the amino acid residues in the sequence are so changed; and the complement of any of the nucleic acid molecules.  
       [0024] In another embodiment, the invention comprises an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102, wherein the nucleic acid molecule comprises the nucleotide sequence of a naturally occurring allelic nucleic acid variant.  
       [0025] In another embodiment, the invention involves an isolated nucleic acid molecule including a nucleic acid sequence encoding a polypeptide having an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102 that encodes a variant polypeptide, wherein the variant polypeptide has the polypeptide sequence of a naturally occurring polypeptide variant.  
       [0026] In another embodiment, the invention comprises an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102, wherein the nucleic acid molecule differs by a single nucleotide from a nucleic acid sequence selected from the group consisting of SEQ ID NOS: 2n−1, wherein n is an integer between 1 and 102.  
       [0027] In another embodiment, the invention includes an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102, wherein the nucleic acid molecule comprises a nucleotide sequence selected from the group consisting of the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102; a nucleotide sequence wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed; a nucleic acid fragment of the sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102; and a nucleic acid fragment wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed.  
       [0028] In another embodiment, the invention includes an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102, wherein the nucleic acid molecule hybridizes under stringent conditions to the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or a complement of the nucleotide sequence.  
       [0029] In another embodiment, the invention includes an isolated nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102, wherein the nucleic acid molecule has a nucleotide sequence in which any nucleotide specified in the coding sequence of the chosen nucleotide sequence is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides in the chosen coding sequence are so changed, an isolated second polynucleotide that is a complement of the first polynucleotide, or a fragment of any of them.  
       [0030] In another embodiment, the invention includes a vector involving the nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102. This vector can have a promoter operably linked to the nucleic acid molecule. This vector can be located within a cell.  
       [0031] In another embodiment, the invention involves a method for determining the presence or amount of a nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102 in a sample, the method including providing the sample; introducing the sample to a probe that binds to the nucleic acid molecule; and determining the presence or amount of the probe bound to the nucleic acid molecule, thereby determining the presence or amount of the nucleic acid molecule in the sample. The presence or amount of the nucleic acid molecule is used as a marker for cell or tissue type. The cell type can be cancerous.  
       [0032] In another embodiment, the invention involves a method for determining the presence of or predisposition for a disease associated with altered levels of a nucleic acid molecule having a nucleic acid sequence encoding a polypeptide including an amino acid sequence selected from the group consisting of a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102 in a first mammalian subject, the method including measuring the amount of the nucleic acid in a sample from the first mammalian subject; and comparing the amount of the nucleic acid in the sample of step (a) to the amount of the nucleic acid present in a control sample from a second mammalian subject known not to have or not be predisposed to, the disease; wherein an alteration in the level of the nucleic acid in the first subject as compared to the control sample indicates the presence of or predisposition to the disease.  
       [0033] The invention further provides an antibody that binds immunospecifically to a NOVX polypeptide. The NOVX antibody may be monoclonal, humanized, or a fully human antibody. Preferably, the antibody has a dissociation constant for the binding of the NOVX polypeptide to the antibody less than 1×10 −9  M. More preferably, the NOVX antibody neutralizes the activity of the NOVX polypeptide.  
       [0034] In a further aspect, the invention provides for the use of a therapeutic in the manufacture of a medicament for treating a syndrome associated with a human disease, associated with a NOVX polypeptide. Preferably the therapeutic is a NOVX antibody.  
       [0035] In yet a further aspect, the invention provides a method of treating or preventing a NOVX-associated disorder, a method of treating a pathological state in a mammal, and a method of treating or preventing a pathology associated with a polypeptide by administering a NOVX antibody to a subject in an amount sufficient to treat or prevent the disorder.  
       [0036] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs Although methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, suitable methods and materials are described below. All publications, patent applications, patents, and other references mentioned herein are incorporated by reference in their entirety. In the case of conflict, the present specification, including definitions, will control. In addition, the materials, methods, and examples are illustrative only and are not intended to be limiting.  
       [0037] Other features and advantages of the invention will be apparent from the following detailed description and claims.  
       DETAILED DESCRIPTION OF THE INVENTION  
       [0038] The present invention provides novel nucleotides and polypeptides encoded thereby. Included in the invention are the novel nucleic acid sequences, their encoded polypeptides, antibodies, and other related compounds. The sequences are collectively referred to herein as “NOVX nucleic acids” or “NOVX polynucleotides” and the corresponding encoded polypeptides arc referred to as “NOVX polypeptides” or “NOVX proteins.” Unless indicated otherwise, “NOVX” is meant to refer to any of the novel sequences disclosed herein. Table A provides a summary of the NOVX nucleic acids and their encoded polypeptides.  
               TABLE A                          Sequences and Corresponding SEQ ID Numbers                                         SEQ ID NO   SEQ ID NO           NOVX   Internal   (nucleic   (amino       Assignment   Identification   acid)   acid)   Homology                                          1a   CG113254-01   1   2   Fibrillin like                         homo sapiens          1b   CG113254-02   3   4   Fibrillin like                         homo sapiens          1c   211648303   5   6   Fibulin        1d   212170920   7   8   Fibulin        2a   CG122729-01   9   10   FAN like  homo                           sapiens          3a   CG122777-01   11   12   P-type trefoil                       domain containing                       protein like  homo                           sapiens          4a   CG124229-01   13   14   Insulin-like                       growth factor binding                       protien 3                       like  homo sapiens          5a   CG124445-02   15   16   transmembrane                       kuzbanian like  homo                           sapiens          6a   CG124590-02   17   18   Integrin Beta 4                       like  homo sapiens          7a   CG124916-01   19   20   Selenoprotein P                       like  homo sapiens          8a   CG126224-01   21   22   Type II Membrane                       Protein with C2                       domains like  homo                           sapiens          9a   CG126233-01   23   24   CTL2 PROTEIN like                         homo sapiens         1Oa   CG126600-01   25   26   Fibronectin type                       III Domain-Membrane                       Protein like  homo                           sapiens         11a   CG127888-01   27   28   Secretory Protein                       like  homo sapiens         12a   CG128249-02   29   30   EPHRIN-A4 like                         homo sapiens         13a   CG128785-01   31   32   Alternatively                       spliced SPUF like                         homo sapiens         14a   CG129005-01   33   34   54TM like  homo                           sapiens         15a   CG132086-01   35   36   Membrane Protein                       containing Alanine                       dehydrogenase and                       pyridine nucleotide                       transhydrogenase                       domain like  homo                           sapiens         16a   CG132297-01   37   38   Elastin like  homo                           sapiens         16b   CG132297-02   39   40   Elastin like  homo                           sapiens         17a   CG132343-01   41   42   transmembrane protein                       like  homo sapiens         18a   CG132423-01   43   44   PREGNANCY-SPECIFIC                       BETA-1-GLYCOPROTEIN                       2 like  homo sapiens         18b   225029377   45   46   Pregnancy Specific                       Beta-1 Glycoprotein 2                       Precursor       19a   CG132541-01   47   48   Cadherin like                         homo sapiens         19b   CG132541-02   49   50   Cadherin       20a   CG132888-02   51   52   M130 Antigen like                         homo sapiens         21a   CG133159-01   53   54   EGF like domain                       and Vacuolar sorting                       protein 9 (VPS9)                       domain containing like                         homo sapiens         22a   CG133508-01   55   56   SYNAPTOTAGMIN VI                       like  homo sapiens         22b   225171562   57   58   SYNAPTOTAGMIN VI       23a   CG133548-01   59   60   300003P13RIK                       Homolog (TmMP) like                         homo sapiens         23b   CG133548-02   61   62   300003P13RIK                       Homolog (TmMP) like                         homo sapiens         24a   CG133569-01   63   64   Type I membrane                       protein with SH3                       domain like  homo                           sapiens         24b   CG133569-02   65   66   Type I membrane                       protein       25a   CG133858-01   67   68   Granulocyte Peptide                       Zgpal like                         homo sapiens         26a   CG134100-01   69   70   Amidase_2 Domain                       like  homo sapiens         26b   CG134100-02   71   72   Amidase_2 Domain                       like  homo sapiens         27a   CG134403-01   73   74   2510042P03RIK                       Homolog (TmSP) like                         homo sapiens         28a   CG135049-01   75   76   Fetuin-B like                         homo sapiens         28b   CG135049-02   77   78   Fetuin-B like                         homo sapiens         28c   CG135049-03   79   80   Fetuin-B like                         homo sapiens         28d   CG135049-04   81   82   Fetuin-B like                         homo sapiens         28e   CG135049-05   83   84   Fetuin-B like                         homo sapiens         28f   CG135049-06   85   86   Fetuin-B like                         homo sapiens         29a   CG54912-02   87   88       29b   207601301   89   90       29c   207601309   91   92       29d   207601313   93   94       29e   207601331   95   96       29f   207639332   97   98       30a   CG56315-03   99   100   Bioactive Peptide                       Connexin       30b   CG56315-04   101   102   Bioactive Peptide                       Connexin       30c   CC56315-05   103   104   Bioactive Peptide                       Connexin       30d   CG56315-06   105   106   Bioactive Peptide                       Connexin       30e   CG56315-07   107   108   Bioactive Peptide                       Connexin       30f   CG56315-08   109   110   Bioactive Peptide                       Connexin       30g   CG56315-01   111   112   Gap Junction                       Beta-5 Connexin -                       isoform 1       30h   CG56315-02   113   114   Connexin       31a   CG56326-01   115   116       31b   175070268   117   118       32a   CG56711-01   119   120       32b   166280659   121   122       32c   166280667   123   124       32d   166280670   125   126       32e   166280673   127   128       32f   166280680   129   130       32g   166280703   131   132       32h   166280730   133   134       33a   CG57658-02   135   136   Bioactive Peptide                       Connexin       33b   CG57658-03   137   138   Bioactive Peptide                       Connexin       33c   CG57658-04   139   140   Bioactive Peptide                       Connexin       33d   CG57658-05   141   142   Bioactive Peptide                       Connexin       33e   CG57658-06   143   144   Bioactive Peptide                       Connexin       33f   CG57658-07   145   146   Bioactive Peptide                       Connexin       33g   CG57658-01   147   148   Connexin - isoform I       34a   CG57664-02   149   150   Bioactive Peptide                       MHC Class I       34b   CG57664-01   151   152   MHC Class I                       antigen - isoform I       35a   CG57668-02   153   154   Bioactive Peptide                       MHC Class I       35b   CG57668-01   155   156   HLA Class I                       Histocompatibiliy                       antigen - isoform I       36a   CG59256-02   157   158   Bioactive Peptide                       MHC Class I       36b   CG59256-01   159   160   MHC Class I                       antigen - isoform I       37a   CG59437-01   161   162       37b   170108827   163   164       37c   170108863   165   166       38a   CG59739-01   167   168       38b   169679148   169   170       39a   CG94630-02   171   172   Bioactive Peptide                       MHC Class I       39b   CG94630-01   173   174   MHC Class I                       antigen - isoform I       40a   CG95205-02   175   176   TEM-1 like  homo                           sapiens                    
 
       [0039]               TABLE B                          Sequences and Corresponding SEQ ID Numbers                                         SEQ ID   SEQ ID                   NO   NO       NOVX   Internal   (nucleic   (amino       Assignment   Identification   acid)   acid)   Homology               41a   CG55676-01   177   178   GPCR like       41b   CG55676-02   179   180   GPCR like       41c   CG55676-03   181   182   GPCR like       41d   CG55676-04   183   184   GPCR like       41e   CG55676-05   185   186   GPCR like       41f   CG55676-06   187   188   GPCR like       41g   CG55676-07   189   190   GPCR like       41h   248209538   191   192   GPCR like       41i   248209591   193   194   GPCR like       41j   248209663   195   196   GPCR like       41k   248209745   197   198   GPCR like       42a   CG53677-01   199   200   GPCR like       42b   CG53677-02   201   202   GPCR like       42c   116781634   203   204   GPCR like                    
       [0040] Table A and B indicate the homology of NOVX polypeptides to known protein families. Thus, the nucleic acids and polypeptides, antibodies and related compounds according to the invention corresponding to a NOVX as identified in column 1 of Table A will be useful in therapeutic and diagnostic applications implicated in, for example, pathologies and disorders associated with the known protein families identified in column 5 of Table A.  
       [0041] Pathologies, diseases, disorders and condition and the like that are associated with NOVX sequences include, but are not limited to: e.g., cardiomyopathy, atherosclerosis, hypertension, congenital heart defects, aortic stenosis, atrial septal defect (ASD), atrioventricular (A-V) canal defect, ductus arteriosus, pulmonary stenosis, subaortic stenosis, ventricular septal defect (VSD), valve diseases, tuberous sclerosis, scleroderma, obesity, metabolic disturbances associated with obesity, transplantation, adrenoleukodystrophy, congenital adrenal hyperplasia, prostate cancer, diabetes, metabolic disorders, neoplasm; adenocarcinoma, lymphoma, uterus cancer, fertility, hemophilia, hypercoagulation, idiopathic thrombocytopenic purpura, immunodeficiencies, graft versus host disease, AIDS, bronchial asthma, Crohn&#39;s disease; multiple sclerosis, treatment of Albright Hereditary Ostoeodystrophy, infectious disease, anorexia, cancer-associated cachexia, cancer, neurodegenerative disorders, Alzheimer&#39;s Disease, Parkinson&#39;s Disorder, immune disorders, hematopoietic disorders, and the various dyslipidemias, the metabolic syndrome X and wasting disorders associated with chronic diseases and various cancers, as well as conditions such as transplantation, neuroprotection, fertility, or regeneration.  
       [0042] NOVX nucleic acids and their encoded polypeptides are useful in a variety of applications and contexts. The various NOVX nucleic acids and polypeptides according to the invention are useful as novel members of the protein families according to the presence of domains and sequence relatedness to previously described proteins. Additionally, NOVX nucleic acids and polypeptides can also be used to identify proteins that are members of the family to which the NOVX polypeptides belong.  
       [0043] Consistent with other known members of the family of proteins, identified in column 5 of Table A, the NOVX polypeptides of the present invention show homology to, and contain domains that are characteristic of, other members of such protein families. Details of the sequence relatedness and domain analysis for each NOVX are presented in Example A.  
       [0044] The NOVX nucleic acids and polypeptides can also be used to screen for molecules, which inhibit or enhance NOVX activity or function. Specifically, the nucleic acids and polypeptides according to the invention may be used as targets for the identification of small molecules that modulate or inhibit diseases associated with the protein families listed in Table A.  
       [0045] The NOVX nucleic acids and polypeptides are also useful for detecting specific cell types. Details of the expression analysis for each NOVX are presented in Example C. Accordingly, the NOVX nucleic acids, polypeptides, antibodies and related compounds according to the invention will have diagnostic and therapeutic applications in the detection of a variety of diseases with differential expression in normal vs. diseased tissues, e g detection of a variety of cancers.  
       [0046] Additional utilities for NOVX nucleic acids and polypeptides according to the invention are disclosed herein.  
       [0047] NOVX Clones  
       [0048] NOVX nucleic acids and their encoded polypeptides are useful in a variety of applications and contexts. The various NOVX nucleic acids and polypeptides according to the invention are useful as novel members of the protein families according to the presence of domains and sequence relatedness to previously described proteins. Additionally, NOVX nucleic acids and polypeptides can also be used to identify proteins that are members of the family to which the NOVX polypeptides belong.  
       [0049] The NOVX genes and their corresponding encoded proteins are useful for preventing, treating or ameliorating medical conditions, e g., by protein or gene therapy. Pathological conditions can be diagnosed by determining the amount of the new protein in a sample or by determining the presence of mutations in the new genes. Specific uses are described for each of the NOVX genes, based on the tissues in which they are most highly expressed. Uses include developing products for the diagnosis or treatment of a variety of diseases and disorders.  
       [0050] The NOVX nucleic acids and proteins of the invention are useful in potential diagnostic and therapeutic applications and as a research tool. These include serving as a specific or selective nucleic acid or protein diagnostic and/or prognostic marker, wherein the presence or amount of the nucleic acid or the protein are to be assessed, as well as potential therapeutic applications such as the following: (i) a protein therapeutic, (ii) a small molecule drug target, (iii) an antibody target (therapeutic, diagnostic, drug targeting/cytotoxic antibody), (iv) a nucleic acid useful in gene therapy (gene delivery/gene ablation), and (v) a composition promoting tissue regeneration in vitro and in vivo (vi) a biological defense weapon.  
       [0051] In one specific embodiment, the invention includes an isolated polypeptide comprising an amino acid sequence selected from the group consisting of: (a) a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102; (b) a variant of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, wherein any amino acid in the mature form is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed; (c) an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102; (d) a variant of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 wherein any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed; and (e) a fragment of any of (a) through (d).  
       [0052] In another specific embodiment, the invention includes an isolated nucleic acid molecule comprising a nucleic acid sequence encoding a polypeptide comprising an amino acid sequence selected from the group consisting of: (a) a mature form of the amino acid sequence given SEQ ID NO: 2n, wherein n is an integer between 1 and 102; (b) a variant of a mature form of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 wherein any amino acid in the mature form of the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence of the mature form are so changed; (c) the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102; (d) a variant of the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, in which any amino acid specified in the chosen sequence is changed to a different amino acid, provided that no more than 15% of the amino acid residues in the sequence are so changed; (e) a nucleic acid fragment encoding at least a portion of a polypeptide comprising the amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 102 or any variant of said polypeptide wherein any amino acid of the chosen sequence is changed to a different amino acid, provided that no more than 10% of the amino acid residues in the sequence are so changed; and (f) the complement of any of said nucleic acid molecules.  
       [0053] In yet another specific embodiment, the invention includes an isolated nucleic acid molecule, wherein said nucleic acid molecule comprises a nucleotide sequence selected from the group consisting of (a) the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102; (b) a nucleotide sequence wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed; (c) a nucleic acid fragment of the sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102; and (d) a nucleic acid fragment wherein one or more nucleotides in the nucleotide sequence selected from the group consisting of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102 is changed from that selected from the group consisting of the chosen sequence to a different nucleotide provided that no more than 15% of the nucleotides are so changed.  
       [0054] NOVX Nucleic Acids and Polypeptides  
       [0055] One aspect of the invention pertains to isolated nucleic acid molecules that encode NOVX polypeptides or biologically active portions thereof. Also included in the invention are nucleic acid fragments sufficient for use as hybridization probes to identify NOVX-encoding nucleic acids (e.g. NOVX mRNAs) and fragments for use as PCR primers for the amplification and/or mutation of NOVX nucleic acid molecules. As used herein, the term “nucleic acid molecule” is intended to include DNA molecules (e g., cDNA or genomic DNA), RNA molecules (e.g, mRNA), analogs of the DNA or RNA generated using nucleotide analogs, and derivatives, fragments and homologs thereof. The nucleic acid molecule may be single-stranded or double-stranded, but preferably is comprised double-stranded DNA.  
       [0056] A NOVX nucleic acid can encode a mature NOVX polypeptide. As used herein, a “mature” form of a polypeptide or protein disclosed in the present invention is the product of a naturally occurring polypeptide or precursor form or proprotein. The naturally occurring polypeptide, precursor or proprotein includes, by way of nonlimiting example, the full-length gene product encoded by the corresponding gene. Alternatively, it may be defined as the polypeptide, precursor or proprotein encoded by an ORF described herein. The product “mature” form arises, by way of nonlimiting example, as a result of one or more naturally occurring processing steps that may take place within the cell (e.g., host cell) in which the gene product arises. Examples of such processing steps leading to a “mature” form of a polypeptide or protein include the cleavage of the N-terminal methionine residue encoded by the initiation codon of an ORF, or the proteolytic cleavage of a signal peptide or leader sequence. Thus a mature form arising from a precursor polypeptide or protein that has residues 1 to N, where residue 1 is the N-terminal methionine, would have residues 2 through N remaining after removal of the N-terminal methionine. Alternatively, a mature form arising from a precursor polypeptide or protein having residues 1 to N, in which an N-terminal signal sequence from residue 1 to residue M is cleaved, would have the residues from residue M+1 to residue N remaining. Further as used herein, a “mature” form of a polypeptide or protein may arise from a step of post-translational modification other than a proteolytic cleavage event. Such additional processes include, by way of non-limiting example, glycosylation, myristylation or phosphorylation. In general, a mature polypeptide or protein may result from the operation of only one of these processes, or a combination of any of them.  
       [0057] The term “probe”, as utilized herein, refers to nucleic acid sequences of variable length, preferably between at least about 10 nucleotides (nt), about 100 nt, or as many as approximately, e g., 6,000 nt, depending upon the specific use. Probes are used in the detection of identical, similar, or complementary nucleic acid sequences. Longer length probes are generally obtained from a natural or recombinant source, are highly specific, and much slower to hybridize than shorter-length oligomer probes. Probes may be single-stranded or double-stranded and designed to have specificity in PCR, membrane-based hybridization technologies, or ELISA-like technologies.  
       [0058] The term “isolated” nucleic acid molecule, as used herein, is a nucleic acid that is separated from other nucleic acid molecules which are present in the natural source of the nucleic acid. Preferably, an “isolated” nucleic acid is free of sequences which naturally flank the nucleic acid (i.e., sequences located at the 5′- and 3′-termini of the nucleic acid) in the genomic DNA of the organism from which the nucleic acid is derived. For example, in various embodiments, the isolated NOVX nucleic acid molecules can contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb or 0.1 kb of nucleotide sequences which naturally flank the nucleic acid molecule in genomic DNA of the cell/tissue from which the nucleic acid is derived (e.g., brain, heart, liver, spleen, etc.). Moreover, an “isolated” nucleic acid molecule, such as a cDNA molecule, can be substantially free of other cellular material, or culture medium, or of chemical precursors or other chemicals.  
       [0059] A nucleic acid molecule of the invention, e g., a nucleic acid molecule having the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or a complement of this nucleotide sequence, can be isolated using standard molecular biology techniques and the sequence information provided herein. Using all or a portion of the nucleic acid sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, as a hybridization probe, NOVX molecules can be isolated using standard hybridization and cloning techniques (e.g., as described in Sambrook, et al., (eds.), MOLECULAR CLONING: A LABORATORY MANUAL 2 nd  Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989; and Ausubel, et al., (eds.), CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley &amp; Sons, New York, N.Y., 1993.)  
       [0060] A nucleic acid of the invention can be amplified using cDNA, mRNA or alternatively, genomic DNA, as a template with appropriate oligonucleotide primers according to standard PCR amplification techniques. The nucleic acid so amplified can be cloned into an appropriate vector and characterized by DNA sequence analysis. Furthermore, oligonucleotides corresponding to NOVX nucleotide sequences can be prepared by standard synthetic techniques, e.g., using an automated DNA synthesizer.  
       [0061] As used herein, the term “oligonucleotide” refers to a series of linked nucleotide residues. A short oligonucleotide sequence may be based on, or designed from, a genomic or cDNA sequence and is used to amplify, confirm, or reveal the presence of an identical, similar or complementary DNA or RNA in a particular cell or tissue. Oligonucleotides comprise a nucleic acid sequence having about 10 nt, 50 nt, or 100 nt in length, preferably about 15 nt to 30 nt in length. In one embodiment of the invention, an oligonucleotide comprising a nucleic acid molecule less than 100 nt in length would further comprise at least 6 contiguous nucleotides of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or a complement thereof. Oligonucleotides may be chemically synthesized and may also be used as probes.  
       [0062] In another embodiment, an isolated nucleic acid molecule of the invention comprises a nucleic acid molecule that is a complement of the nucleotide sequence shown in SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or a portion of this nucleotide sequence (e.g., a fragment that can be used as a probe or primer or a fragment encoding a biologically-active portion of a NOVX polypeptide). A nucleic acid molecule that is complementary to the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, is one that is sufficiently complementary to the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, that it can hydrogen bond with few or no mismatches to the nucleotide sequence shown in SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, thereby forming a stable duplex.  
       [0063] As used herein, the term “complementary” refers to Watson-Crick or Hoogsteen base pairing between nucleotides units of a nucleic acid molecule, and the term “binding” means the physical or chemical interaction between two polypeptides or compounds or associated polypeptides or compounds or combinations thereof. Binding includes ionic, non-ionic, van der Waals, hydrophobic interactions, and the like. A physical interaction can be either direct or indirect. Indirect interactions may be through or due to the effects of another polypeptide or compound. Direct binding refers to interactions that do not take place through, or due to, the effect of another polypeptide or compound, but instead are without other substantial chemical intermediates.  
       [0064] A “fragment” provided herein is defined as a sequence of at least 6 (contiguous) nucleic acids or at least 4 (contiguous) amino acids, a length sufficient to allow for specific hybridization in the case of nucleic acids or for specific recognition of an epitope in the case of amino acids, and is at most some portion less than a full length sequence. Fragments may be derived from any Contiguous portion of a nucleic acid or amino acid sequence of choice.  
       [0065] A full-length NOVX clone is identified as containing an ATG translation start codon and an in-frame stop codon. Any disclosed NOVX nucleotide sequence lacking an ATG start codon therefore encodes a truncated C-terminal fragment of the respective NOVX polypeptide, and requires that the corresponding full-length cDNA extend in the 5′ direction of the disclosed sequence. Any disclosed NOVX nucleotide sequence lacking an in-frame stop codon similarly encodes a truncated N-terminal fragment of the respective NOVX polypeptide, and requires that the corresponding full-length cDNA extend in the 3′ direction of the disclosed sequence.  
       [0066] A “derivative” is a nucleic acid sequence or amino acid sequence formed from the native compounds either directly, by modification or partial substitution. An “analog” is a nucleic acid sequence or amino acid sequence that has a structure similar to, but not identical to, the native compound, e.g. they differs from it in respect to certain components or side chains. Analogs may be synthetic or derived from a different evolutionary origin and may have a similar or opposite metabolic activity compared to wild type. A “homolog” is a nucleic acid sequence or amino acid sequence of a particular gene that is derived from different species.  
       [0067] Derivatives and analogs may be full length or other than full length. Derivatives or analogs of the nucleic acids or proteins of the invention include, but are not limited to, molecules comprising regions that are substantially homologous to the nucleic acids or proteins of the invention, in various embodiments, by at least about 70%, 80%, or 95% identity (with a preferred identity of 80-95%) over a nucleic acid or amino acid sequence of identical size or when compared to an aligned sequence in which the alignment is done by a computer homology program known in the art, or whose encoding nucleic acid is capable of hybridizing to the complement of a sequence encoding the proteins under stringent, moderately stringent, or low stringent conditions. See e.g Ausubel, et al., CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley &amp; Sons, New York, N.Y., 1993, and below.  
       [0068] A “homologous nucleic acid sequence” or “homologous amino acid sequence,” or variations thereof, refer to sequences characterized by a homology at the nucleotide level or amino acid level as discussed above. Homologous nucleotide sequences include those sequences coding for isoforms of NOVX polypeptides. Isoforms can be expressed in different tissues of the same organism as a result of, for example, alternative splicing of RNA. Alternatively, isoforms can be encoded by different genes. In the invention, homologous nucleotide sequences include nucleotide sequences encoding for a NOVX polypeptide of species other than humans, including, but not limited to: vertebrates, and thus can include, e.g., frog, mouse, rat, rabbit, dog, cat cow, horse, and other organisms. Homologous nucleotide sequences also include, but are not limited to, naturally occurring allelic variations and mutations of the nucleotide sequences set forth herein. A homologous nucleotide sequence does not, however, include the exact nucleotide sequence encoding human NOVX protein. Homologous nucleic acid sequences include those nucleic acid sequences that encode conservative amino acid substitutions (see below) in SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, as well as a polypeptide possessing NOVX biological activity. Various biological activities of the NOVX proteins are described below.  
       [0069] A NOVX polypeptide is encoded by the open reading frame (“ORF”) of a NOVX nucleic acid. An ORF corresponds to a nucleotide sequence that could potentially be translated into a polypeptide. A stretch of nucleic acids comprising an ORF is uninterrupted by a stop codon. An ORF that represents the coding sequence for a full protein begins with an ATG “start” codon and terminates with one of the three “stop” codons, namely, TAA, TAG, or TGA. For the purposes of this invention, an ORF may be any part of a coding sequence, with or without a start codon, a stop codon, or both. For an ORF to be considered as a good candidate for coding for a bona fide cellular protein, a minimum size requirement is often set, e.g., a stretch of DNA that would encode a protein of 50 amino acids or more.  
       [0070] The nucleotide sequences determined from the cloning of the human NOVX genes allows for the generation of probes and primers designed for use in identifying and/or cloning NOVX homologues in other cell types, e.g. from other tissues, as well as NOVX homologues from other vertebrates. The probe/primer typically comprises substantially purified oligonucleotide. The oligonucleotide typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least about 12, 25, 50, 100, 150, 200, 250, 300, 350 or 400 consecutive sense strand nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102; or an anti-sense strand nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102; or of a naturally occurring mutant of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102.  
       [0071] Probes based on the human NOVX nucleotide sequences can be used to detect transcripts or genomic sequences encoding the same or homologous proteins. In various embodiments, the probe has a detectable label attached, e g. the label can be a radioisotope, a fluorescent compound, an enzyme, or an enzyme co-factor. Such probes can be used as a part of a diagnostic test kit for identifying cells or tissues which mis-express a NOVX protein, such as by measuring a level of a NOVX-encoding nucleic acid in a sample of cells from a subject e g, detecting NOVX mRNA levels or determining whether a genomic NOVX gene has been mutated or deleted.  
       [0072] “A polypeptide having a biologically-active portion of a NOVX polypeptide” refers to polypeptides exhibiting activity similar, but not necessarily identical to, an activity of a polypeptide of the invention, including mature forms, as measured in a particular biological assay, with or without dose dependency. A nucleic acid fragment encoding a “biologically-active portion of NOVX” can be prepared by isolating a portion of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, that encodes a polypeptide having a NOVX biological activity (the biological activities of the NOVX proteins are described below), expressing the encoded portion of NOVX protein (e.g., by recombinant expression in vitro) and assessing the activity of the encoded portion of NOVX.  
       [0073] NOVX Nucleic Acid and Polypeptide Variants  
       [0074] The invention further encompasses nucleic acid molecules that differ from the nucleotide sequences of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, due to degeneracy of the genetic code and thus encode the same NOVX proteins as that encoded by the nucleotide sequences of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102. In another embodiment, an isolated nucleic acid molecule of the invention has a nucleotide sequence encoding a protein having an amino acid sequence of SEQ ID NO: 2n, wherein n is an integer between 1 and 102.  
       [0075] In addition to the human NOVX nucleotide sequences of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, it will be appreciated by those skilled in the art that DNA sequence polymorphisms that lead to changes in the amino acid sequences of the NOVX polypeptides may exist within a population (e.g., the human population). Such genetic polymorphism in the NOVX genes may exist among individuals within a population due to natural allelic variation. As used herein, the terms “gene” and “recombinant gene” refer to nucleic acid molecules comprising an open reading frame (ORF) encoding a NOVX protein, preferably a vertebrate NOVX protein. Such natural allelic variations can typically result in 1-5% variance in the nucleotide sequence of the NOVX genes. Any and all such nucleotide variations and resulting amino acid polymorphisms in the NOVX polypeptides, which are the result of natural allelic variation and that do not alter the functional activity of the NOVX polypeptides, are intended to be within the scope of the invention.  
       [0076] Moreover, nucleic acid molecules encoding NOVX proteins from other species, and thus that have a nucleotide sequence that differs from a human SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, are intended to be within the scope of the invention. Nucleic acid molecules corresponding to natural allelic variants and homologues of the NOVX cDNAs of the invention can be isolated based on their homology to the human NOVX nucleic acids disclosed herein using the human cDNAs, or a portion thereof, as a hybridization probe according to standard hybridization techniques under stringent hybridization conditions.  
       [0077] Accordingly, in another embodiment, an isolated nucleic acid molecule of the invention is at least 6 nucleotides in length and hybridizes under stringent conditions to the nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102. In another embodiment, the nucleic acid is at least 10, 25, 50, 100, 250, 500, 750, 1000, 1500, or 2000 or more nucleotides in length. In yet another embodiment, an isolated nucleic acid molecule of the invention hybridizes to the coding region. As used herein, the term “hybridizes under stringent conditions” is intended to describe conditions for hybridization and washing under which nucleotide sequences at least about 65% homologous to each other typically remain hybridized to each other.  
       [0078] Homologs (i.e., nucleic acids encoding NOVX proteins derived from species other than human) or other related sequences (e g., paralogs) can be obtained by low, moderate or high stringency hybridization with all or a portion of the particular human sequence as a probe using methods well known in the art for nucleic acid hybridization and cloning.  
       [0079] As used herein, the phrase “stringent hybridization conditions” refers to conditions under which a probe, primer or oligonucleotide will hybridize to its target sequence, but to no other sequences. Stringent conditions are sequence-dependent and will be different in different circumstances. Longer sequences hybridize specifically at higher temperatures than shorter sequences. Generally, stringent conditions are selected to be about 5° C. lower than the thermal melting point (Tm) for the specific sequence at a defined ionic strength and pH. The Tm is the temperature (under defined ionic strength, pH and nucleic acid concentration) at which 50% of the probes complementary to the target sequence hybridize to the target sequence at equilibrium. Since the target sequences are generally present at excess, at Tm, 50% oifthe probes are occupied at equilibrium. Typically, stringent conditions will be those in which the salt concentration is less than about 1.0 M sodium ion, typically about 0.01 to 1.0 M sodium ion (or other salts) at pH 7.0 to 8.3 and the temperature is at least about 30° C. for short probes, primers or oligonucleotides (e.g , 10 nt to 50 nt) and at least about 60° C. for longer probes, primers and oligonucleotides. Stringent conditions may also be achieved with the addition of destabilizing agents, such as formamide.  
       [0080] Stringent conditions are known to those skilled in the art and can be found in Ausubel, et al., (eds.), CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley &amp; Sons, N.Y. (1989), 6.3.1-6.3.6. Preferably, the conditions are such that sequences at least about 65%, 70%, 75%, 85%, 90%, 95%, 98%, or 99% homologous to each other typically remain hybridized to each other. A non-limiting example of stringent hybridization conditions are hybridization in a high salt buffer comprising 6×SSC, 50 mM Tris-HCl (pH 7.5), 1 mM EDTA, 0.02% PVP, 0.02% Ficoll, 0.02% BSA, and 500 mg/ml denatured salmon sperm DNA at 65° C., followed by one or more washes in 0.2×SSC, 0.01% BSA at 50° C. An isolated nucleic acid molecule of the invention that hybridizes under stringent conditions to a sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, corresponds to a naturally-occurring nucleic acid molecule. As used herein, a “naturally-occurring” nucleic acid molecule refers to an RNA or DNA molecule having a nucleotide sequence that occurs in nature (e.g., encodes a natural protein).  
       [0081] In a second embodiment, a nucleic acid sequence that is hybridizable to the nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or fragments, analogs or derivatives thereof, under conditions of moderate stringency is provided. A non-limiting example of moderate stringency hybridization conditions are hybridization in 6×SSC, 5× Reinhardt&#39;s solution, 0.5% SDS and 100 mg/ml denatured salmon sperm DNA at 55° C., followed by one or more washes in 1×SSC, 0.1% SDS at 37° C. Other conditions of moderate stringency that may be used are well-known within the art. See, e.g., Ausubel, et al (eds.), 1993, CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley &amp; Sons, NY, and Krieger, 1990; GENE TRANSFER AND EXPRESSION, A LABORATORY MANUAL, Stockton Press, NY.  
       [0082] In a third embodiment, a nucleic acid that is hybridizable to the nucleic acid molecule comprising the nucleotide sequences of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or fragments, analogs or derivatives thereof, under conditions of low stringency, is provided. A non-limiting, example of low stringency hybridization conditions are hybridization in 35% formamide, 5×SSC, 50 mM Tris-HCl (pH 7.5), 5 mM EDTA, 0.02% PVP, 0.02% Ficoll, 0.2% BSA, 100 mg/ml denatured salmon sperm DNA, 10% (wt/vol) dextran sulfate at 40° C., followed by one or more washes in 2×SSC, 25 mM Tris-HCl (pH 7.4), 5 mM EDTA, and 0.1% SDS at 50° C. Other conditions of low stringency that may be used are well known in the art (e g., as employed for cross-species hybridizations). See, e.g, Ausubel, et al. (eds.), 1993, CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley &amp; Sons, NY, and Kiegler, 1990, GENE TRANSFER AND EXPRESSION, A LABORATORY MANUAL, Stockton Press, NY; Shilo and Weinberg, 1981.  Proc Natl Acad Sci USA  78: 6789-6792.  
       [0083] Conservative Mutations  
       [0084] In addition to naturally-occurring allelic variants of NOVX sequences that may exist in the population, the skilled artisan will further appreciate that changes can be introduced by mutation into the nucleotide sequences of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, thereby leading to changes in the amino acid sequences of the encoded NOVX protein, without altering the functional ability of that NOVX protein. For example, nucleotide substitutions leading to amino acid substitutions at “non-essential” amino acid residues can be made in the sequence of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. A “non-essential” amino acid residue is a residue that can be altered from the wild-type sequences of the NOVX proteins without altering their biological activity, whereas an “essential” amino acid residue is required for such biological activity. For example, amino acid residues that are conserved among the NOVX proteins of the invention are predicted to be particularly non-amenable to alteration. Amino acids for which conservative substitutions can be made are well-known within the art.  
       [0085] Another aspect of the invention pertains to nucleic acid molecules encoding NOVX proteins that contain changes in amino acid residues that are not essential for activity. Such NOVX proteins differ in amino acid sequence from SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, yet retain biological activity. In one embodiment, the isolated nucleic acid molecule comprises a nucleotide sequence encoding a protein, wherein the protein comprises an amino acid sequence at least about 40% homologous to the amino acid sequences of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. Preferably, the protein encoded by the nucleic acid molecule is at least about 60% homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102; more preferably at least about 70% homologous to SEQ ID NO: 2n, wherein is an integer between 1 and 102; still more preferably at least about 80% homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102; even more preferably at least about 90% homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102; and most preferably at least about 95% homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102.  
       [0086] An isolated nucleic acid molecule encoding a NOVX protein homologous to the protein of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, can be created by introducing one or more nucleotide substitutions, additions or deletions into the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, such that one or more amino acid substitutions, additions or deletions are introduced into the encoded protein.  
       [0087] Mutations can be introduced any one of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, by standard techniques, such as site-directed mutagenesis and PCR-mediated mutagenesis. Preferably, conservative amino acid substitutions are made at one or more predicted, non-essential amino acid residues. A “conservative amino acid substitution” is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined within the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e g, threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). Thus, a predicted non-essential amino acid residue in the NOVX protein is replaced with another amino acid residue from the same side chain family. Alternatively, in another embodiment, mutations can be introduced randomly along all or part of a NOVX coding sequence, such as by saturation mutagenesis, and the resultant mutants can be screened for NOVX biological activity to identify mutants that retain activity. Following mutagenesis of a nucleic acid of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, the encoded protein can be expressed by any recombinant technology known in the art and the activity of the protein can be determined.  
       [0088] The relatedness of amino acid families may also be determined based on side chain interactions. Substituted amino acids may be fully conserved “strong” residues or fully conserved “weak” residues. The “strong” group of conserved amino acid residues may be any one of the following groups: STA, NEQK, NHQK, NDEQ, QHRK, MILV, MILF, HY, FYW, wherein the single letter amino acid codes are grouped by those amino acids that may be substituted for each other. Likewise, the “weak” group of conserved residues may be any one of the following: CSA, ATV, SAG, STNK, STPA, SGND, SNDEQK, NDEQHK, NEQHRK, HFY, wherein the letters within each group represent the single letter amino acid code.  
       [0089] In one embodiment, a mutant NOVX protein can be assayed for (i) the ability to form protein:protein interactions with other NOVX proteins, other cell-surface proteins, or biologically-active portions thereof, (ii) complex formation between a mutant NOVX protein and a NOVX ligand; or (iii) the ability of a mutant NOVX protein to bind to an intracellular target protein or biologically-active portion thereof; (e.g. avidin proteins).  
       [0090] In yet another embodiment, a mutant NOVX protein can be assayed for the ability to regulate a specific biological function (e.g., regulation of insulin release).  
       [0091] Antisense Nucleic Acids  
       [0092] Another aspect of the invention pertains to isolated antisense nucleic acid molecules that are hybridizable to or complementary to the nucleic acid molecule comprising the nucleotide sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or fragments, analogs or derivatives thereof. An “antisense” nucleic acid comprises a nucleotide sequence that is complementary to a “sense” nucleic acid encoding a protein (e.g., complementary to the coding strand of a double-stranded cDNA molecule or complementary to an mRNA sequence). In specific aspects, antisense nucleic acid molecules are provided that comprise a sequence complementary to at least about 10, 25, 50, 100, 250 or 500 nucleotides or an entire NOVX coding strand, or to only a portion thereof. Nucleic acid molecules encoding fragments, homologs, derivatives and analogs of a NOVX protein of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, or antisense nucleic acids complementary to a NOVX nucleic acid sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, are additionally provided.  
       [0093] In one embodiment, an antisense nucleic acid molecule is antisense to a “coding region” of the coding strand of a nucleotide sequence encoding a NOVX protein. The term “coding region” refers to the region of the nucleotide sequence comprising codons which are translated into amino acid residues. In another embodiment, the antisense nucleic acid molecule is antisense to a “noncoding region” of the coding strand of a nucleotide sequence encoding the NOVX protein. The term “noncoding region” refers to 5′ and 3′ sequences which flank the coding region that are not translated into amino acids (i.e , also referred to as 5′ and 3′ untranslated regions).  
       [0094] Given the coding strand sequences encoding the NOVX protein disclosed herein, antisense nucleic acids of the invention can be designed according to the rules of Watson and Crick or Hoogsteen base pairing. The antisense nucleic acid molecule can be complementary to the entire coding region of NOVX mRNA, but more preferably is an oligonucleotide that is antisense to only a portion of the coding or noncoding region of NOVX mRNA. For example, the antisense oligonucleotide can be complementary to the region surrounding the translation start site of NOVX mRNA. An antisense oligonucleotide can be, for example, about 5, 10, 15, 20, 25, 30, 35, 40, 45 or 50 nucleotides in length. An antisense nucleic acid of the invention can be constructed using chemical synthesis or enzymatic ligation reactions using procedures known in the art. For example, an antisense nucleic acid (e.g., an antisense oligonucleotide) can be chemically synthesized using naturally-occurring nucleotides or variously modified nucleotides designed to increase the biological stability of the molecules or to increase the physical stability of the duplex formed between the antisense and sense nucleic acids (e.g., phosphorothioate derivatives and acridine substituted nucleotides can be used).  
       [0095] Examples of modified nucleotides that can be used to generate the antisense nucleic acid include: 5-fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil, hypoxanthine, xanthine, 4-acetylcytosine, 5-carboxymethylaminomethyl-2-thiouridine, 5-(carboxyhydroxylmethyl)uracil, 5-carboxymethylaminomethyluracil, dihydrouracil, beta-D-galactosylqueosine, inosine, N6-isopentenyladenine, 1-methylguanine, 1-methylinosine, 2,2-dimethylguanine, 2-methyladenine, 2-methylguanine, 5-methoxyuracil, 3-methylcytosine, 5-methylcytosine, N6-adenine, 7-methylguanine, 5-methylaminomethyluracil, 5-methoxyaminomethyl-2-thiouracil, 2-thiouracil, 4-thiouracil, beta-D-manniosylqueosine, 5′-methoxycarboxymethyluracil, 2-methylthio-N6-isopentenyladenine, uracil-5-oxyacetic acid (v), wybutoxosine, pseudouracil, queosine, 2-thiocytosine, 5-methyl-2-thiouracil, 5-methyluracil, uracil-5-oxyacetic acid methylester, uracil-5-oxyacetic acid (v), 5-methyl-2-thiouracil, 3-(3 -amino-3-N-2-carboxypropyl) uracil, (acp3 )w, and 2,6-diaminopurine. Alternatively, the antisense nucleic acid can be produced biologically using an expression vector into which a nucleic acid has been subcloned in an antisense orientation (i e, RNA transcribed from the inserted nucleic acid will be of an antisense orientation to a target nucleic acid of interest, described further in the following subsection).  
       [0096] The antisense nucleic acid molecules of the invention are typically administered to a subject or generated in situ such that they hybridize with or bind to cellular mRNA and/or genomic DNA encoding a NOVX protein to thereby inhibit expression of the protein (e g., by inhibiting transcription and/or translation). The hybridization can be by conventional nucleotide complementarity to form a stable duplex, or, for example, in the case of an antisense nucleic acid molecule that binds to DNA duplexes, through specific interactions in the major groove of the double helix. An example of a route of administration of antisense nucleic acid molecules of the invention includes direct injection at a tissue site. Alternatively, antisense nucleic acid molecules can be modified to target selected cells and then administered systemically. For example, for systemic administration, antisense molecules can be modified such that they specifically bind to receptors or antigens expressed on a selected cell surface (e.g., by linking the antisense nucleic acid molecules to peptides or antibodies that bind to cell surface receptors or antigens). The antisense nucleic acid molecules can also be delivered to cells using the vectors described herein. To achieve sufficient nucleic acid molecules, vector constructs in which the antisense nucleic acid molecule is placed under the control of a strong pol II or pol III promoter are preferred.  
       [0097] In yet another embodiment, the antisense nucleic acid molecule of the invention is an α-anomeric nucleic acid molecule. An α-anomeric nucleic acid molecule forms specific double-stranded hybrids with complementary RNA in which, contrary to the usual β-units, the strands run parallel to each other. See, e.g., Gaultier, et al., 1987.  Nucl. Acids Res.  15: 6625-6641. The antisense nucleic acid molecule can also comprise a 2′-o-methylribonucleotide (See, e.g., Inoue, et al. 1987.  Nucl. Acids Res  15: 6131-6148) or a chimeric RNA-DNA analogue (See, e.g., Inoue, et al., 1987.  FEBS Lett.  215: 327-330.  
       [0098] Ribozymes and PNA Moieties  
       [0099] Nucleic acid modifications include, by way of non-limiting example, modified bases, and nucleic acids whose sugar phosphate backbones are modified or derivatized. These modifications are carried out at least in part to enhance the chemical stability of the modified nucleic acid, such that they may be used, for example, as antisense binding nucleic acids in therapeutic applications in a subject.  
       [0100] In one embodiment, an antisense nucleic acid of the invention is a ribozyme. Ribozymes arc catalytic RNA molecules with ribonuclease activity that are capable of cleaving a single-stranded nucleic acid, such as an mRNA, to which they have a complementary region. Thus, ribozymes (e g., hammerhead ribozymes as described in Haselhoff and Gerlach 1988.  Nature  334: 585-591) can be used to catalytically cleave NOVX mRNA transcripts to thereby inhibit translation of NOVX mRNA. A ribozyme having specificity for a NOVX-encoding nucleic acid can be designed based upon the nucleotide sequence of a NOVX cDNA disclosed herein (i.e., SEQ ID NO: 2n−1 , wherein n is an integer between 1 and 102). For example, a derivative of a Tetrahymena L-19 IVS RNA can be constructed in which the nucleotide sequence of the active site is complementary to the nucleotide sequence to be cleaved in a NOVX-encoding mRNA. See, e.g., U.S. Pat. No. 4,987,071 to Cech, et al. and U.S. Pat. No. 5,116,742 to Cech, et al. NOVX mRNA can also be used to select a catalytic RNA having a specific ribonuclease activity from a pool of RNA molecules. See, e.g., Bartel et al., (1993)  Science  261:1411-1418.  
       [0101] Alternatively, NOVX gene expression can be inhibited by targeting nucleotide sequences complementary to the regulatory region of the NOVX nucleic acid (e.g., the NOVX promoter and/or enhancers) to form triple helical structures that prevent transcription of the NOVX gene in target cells. See, e.g., Helene, 1991.  Anticancer Drug Des.  6: 569-84; Helene, et al. 1992.  Ann. N.Y. Acad. Sci.  660: 27-36; Maher, 1992.  Bioassays  14: 807-15.  
       [0102] In various embodiments, the NOVX nucleic acids can be modified at the base moiety, sugar moiety or phosphate backbone to improve, e.g., the stability, hybridization, or solubility of the molecule. For example, the deoxyribose phosphate backbone of the nucleic acids can be modified to generate peptide nucleic acids. See, e.g., Hyrup, et al., 1996.  Bioorg Med Chem  4: 5-23. As used herein, the terms “peptide nucleic acids” or “PNAs” refer to nucleic acid mimics (e.g., DNA mimics) in which the deoxyribose phosphate backbone is replaced by a pseudopeptide backbone and only the four natural nucleotide bases are retained. The neutral backbone of PNAs has been shown to allow for specific hybridization to DNA and RNA under conditions of low ionic strength. The synthesis of PNA oligomer can be performed using standard solid phase peptide synthesis protocols as described in Hyrup, et al., 1996. supra; Perry-O&#39;Keefe, et al., 1996.  Proc Natl Acad. Sci. USA  93: 14670-14675.  
       [0103] PNAs of NOVX can be used in therapeutic and diagnostic applications. For example, PNAs can be used as antisense or antigens agents for sequence-specific modulation of gene expression by, e.g., inducing transcription or translation arrest or inhibiting replication. PNAs of NOVX can also be used, for example, in the analysis of single base pair mutations in a gene (e g., PNA directed PCR clamping; as artificial restriction enzymes when used in combination with other enzymes, e g , S 1  nucleases (See, Hyrup, et al., 1996.supra); or as probes or primers for DNA sequence and hybridization (See, Hyrup, et al., 1996, supra; Perry-O&#39;Keefe, et al., 1996. supra).  
       [0104] In another embodiment, PNAs of NOVX can be modified, e.g., to enhance their stability or cellular uptake, by attaching, lipophilic or other helper groups to PNA, by the formation of PNA-DNA chimeras, or by the use of liposomes or other techniques of drug delivery known in the art. For example, PNA-DNA chimeras of NOVX can be generated that may combine the advantageous properties of PNA and DNA. Such chimeras allow DNA recognition enzymes (e.g., RNase H and DNA polymerases) to interact with the DNA portion while the PNA portion would provide high binding affinity and specificity. PNA-DNA chimeras can be linked using linkers of appropriate lengths selected in terms of base stacking, number of bonds between the nucleotide bases, and orientation (see, Hyrup, et al., 1996. supra). The synthesis of PNA-DNA chimeras can be performed as described in Hyrup, et al, 1996. supra and Finn, et al., 1996.  Nucl Acids Res  24: 3357-3363. For example, a DNA chain can be synthesized on a solid support using standard phosphoramidite coupling chemistry, and modified nucleoside analogs, e.g, 5′-(4-methoxytrityl)amino-5′-deoxy-thymidine phosphoramidite, can be used between the PNA and the 5′ end of DNA. See, e.g, Mag, et al., 1989.  Nucl Acid Res  17: 5973-5988. PNA monomers are then coupled in a stepwise manner to produce a chimeric molecule with a 5′ PNA segment and a 3′ DNA segment. See, e.g., Finn, et al., 1996. supra. Alternatively, chimeric molecules can be synthesized with a 5′ DNA segment and a 3′ PNA segment. See, e.g., Petersen, et al., 1975.  Bioorg. Med. Chem. Lett.  5: 1119-11124.  
       [0105] In other embodiments, the oligonucleotide may include other appended groups such as peptides (e.g, for targeting host cell receptors in vivo), or agents facilitating transport across the cell membrane (see, e.g., Letsinger, et al., 1989.  Proc. Natl. Acad. Sci. U.S.A  86: 6553-6556; Lemaitre, et al., 1987.  Proc. Natl. Acad. Sci.  84: 648-652; PCT Publication No. WO88/09810) or the blood-brain barrier (see, e.g., PCT Publication No. WO 89/10134). In addition, oligonucleotides can be modified with hybridization triggered cleavage agents (see, e.g., Krol, et al., 1988.  BioTechniques  6:958-976) or intercalating agents (see, e g, Zon, 1988.  Pharm Res.  5: 539-549). To this end, the oligonucleotide may be conjugated to another molecule, e.g., a peptide, a hybridization triggered cross-linking agent, a transport agent, a hybridization-triggered cleavage agent, and the like.  
       [0106] NOVX Polypeptides  
       [0107] A polypeptide according to the invention includes a polypeptide including the amino acid sequence of NOVX polypeptides whose sequences are provided in any one of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. The invention also includes a mutant or variant protein any of whose residues may be changed from the corresponding residues shown in any one of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, while still encoding a protein that maintains its NOVX activities and physiological functions, or a functional fragment thereof.  
       [0108] In general, a NOVX variant that preserves NOVX-like function includes any variant in which residues at a particular position in the sequence have been substituted by other amino acids, and further include the possibility of inserting an additional residue or residues between two residues of the parent protein as well as the possibility of deleting one or more residues from the parent sequence. Any amino acid substitution, insertion, or deletion is encompassed by the invention. In favorable circumstances, the substitution is a conservative substitution as defined above.  
       [0109] One aspect of the invention pertains to isolated NOVX proteins, and biologically-active portions thereof, or derivatives, fragments, analogs or homologs thereof. Also provided are polypeptide fragments suitable for use as immunogens to raise anti-NOVX antibodies. In one embodiment, native NOVX proteins can be isolated from cells or tissue sources by an appropriate purification scheme using standard protein purification techniques. In another embodiment, NOVX proteins are produced by recombinant DNA techniques. Alternative to recombinant expression, a NOVX protein or polypeptide can be synthesized chemically using standard peptide synthesis techniques.  
       [0110] An “isolated” or “purified” polypeptide or protein or biologically-active portion thereof is substantially free of cellular material or other contaminating proteins from the cell or tissue source from which the NOVX protein is derived, or substantially free from chemical precursors or other chemicals when chemically synthesized. The language “substantially free of cellular material” includes preparations of NOVX proteins in which the protein is separated from cellular components of the cells from which it is isolated or recombinantly-produced. In one embodiment, the language “substantially free of cellular material” includes preparations of NOVX proteins having less than about 30% (by dry weight) of non-NOVX proteins (also referred to herein as a “contaminating protein”), more preferably less than about 20% of non-NOVX proteins, still more preferably less than about 10% of non-NOVX proteins, and most preferably less than about 5% of non-NOVX proteins. When the NOVX protein or biologically-active portion thereof is recombinantly-produced, it is also preferably substantially free of culture medium, i.e , culture medium represents less than about 20%, more preferaibly less than about 10%, and most preferably less than about 5% of the volume of the NOVX protein preparation.  
       [0111] The language “substantially free of chemical precursors or other chemicals” includes preparations of NOVX proteins in which the protein is separated from chemical precursors or other chemicals that are involved in the synthesis of the protein. In one embodiment, the language “substantially free of chemical precursors or other chemicals” includes preparations of NOVX proteins having less than about 30% (by dry weight) of chemical precursors or non-NOVX chemicals, more preferably less than about 20% chemical precursors or non-NOVX chemicals, still more preferably less than about 10% chemical precursors or non-NOVX chemicals, and most preferably less than about 5% chemical precursors or non-NOVX chemicals.  
       [0112] Biologically-active portions of NOVX proteins include peptides comprising amino acid sequences sufficiently homologous to or derived from the amino acid sequences of the NOVX proteins (e.g., the amino acid sequence of SEQ ID NO: 2n, wherein n is an integer between 1 and 102) that include fewer amino acids than the full-length NOVX proteins, and exhibit at least one activity of a NOVX protein. Typically, biologically-active portions comprise a domain or motif with at least one activity of the NOVX protein. A biologically-active portion of a NOVX protein can be a polypeptide which is, for example, 10, 25, 50, 100 or more amino acid residues in length.  
       [0113] Moreover, other biologically-active portions, in which other regions of the protein are deleted, can be prepared by recombinant techniques and evaluated for one or more of the functional activities of a native NOVX protein.  
       [0114] In an embodiment, the NOVX protein has an amino acid sequence of SEQ ID NO: 2n, wherein n is an integer between 1 and 102. In other embodiments, the NOVX protein is substantially homologous to SEQ ID NO: 2n, wherein n is an integer between 1 and 102, and retains the functional activity of the protein of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, yet differs in amino acid sequence due to natural allelic variation or mutagenesis, as described in detail, below. Accordingly, in another embodiment, the NOVX protein is a protein that comprises an amino acid sequence at least about 45% homologous to the amino acid sequence of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, and retains the functional activity of the NOVX proteins of SEQ ID NO: 2n, wherein n is an integer between 1 and 102.  
       [0115] Determining Homology Between Two or More Sequences  
       [0116] To determine the percent homology of two amino acid sequences or of two nucleic acids, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in the sequence of a first amino acid or nucleic acid sequence for optimal alignment with a second amino or nucleic acid sequence). The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are homologous at that position (i.e., as used herein amino acid or nucleic acid “homology” is equivalent to amino acid or nucleic acid “identity”).  
       [0117] The nucleic acid sequence homology may be determined as the degree of identity between two sequences. The homology may be determined using computer programs known in the art, such as GAP software provided in the GCG program package. See, Needleman and Wunsch, 1970.  J Mol Biol  48: 443-453. Using GCG GAP software with the following settings for nucleic acid sequence comparison: GAP creation penalty of 5.0 and GAP extension penalty of 0.3, the coding region of the analogous nucleic acid sequences referred to above exhibits a degree of identity preferably of at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99%, with the CDS (encoding) part of the DNA sequence of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102.  
       [0118] The term “sequence identity” refers to the degree to which two polynucleotide or polypeptide sequences are identical on a residue-by-residue basis over a particular region of comparison. The term “percentage of sequence identity” is calculated by comparing, two optimally aligned sequences over that region of comparison, determining the number of positions at which the identical nucleic acid base (e.g., A, T, C, G,. U, or I, in the case of nucleic acids) occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the region of comparison (i.e., the window size), and multiplying the result by 100 to yield the percentage of sequence identity. The term “substantial identity” as used herein denotes a characteristic of a polynucleotide sequence, wherein the polynucleotide comprises a sequence that has at least 80 percent sequence identity, preferably at least 85 percent identity and often 90 to 95 percent sequence identity, more usually at least 99 percent sequence identity as compared to a reference sequence over a comparison region.  
       [0119] Chimeric and Fusion Proteins  
       [0120] The invention also provides NOVX chimeric or fusion proteins. As used herein, a NOVX “chimeric protein” or “fusion protein” comprises a NOVX polypeptide operatively-linked to a non-NOVX polypeptide. An “NOVX polypeptide” refers to a polypeptide having an amino acid sequence corresponding to a NOVX protein of SEQ ID NO: 2n, wherein n is an integer between 1 and 102, whereas a “non-NOVX polypeptide” refers to a polypeptide having an amino acid sequence corresponding to a protein that is not substantially homologous to the NOVX protein, e.g., a protein that is different from the NOVX protein and that is derived from the same or a different organism. Within a NOVX fusion protein the NOVX polypeptide can correspond to all or a portion of a NOVX protein. In one embodiment, a NOVX fusion protein comprises at least one biologically-active portion of a NOVX protein. In another embodiment, a NOVX fusion protein comprises at least two biologically-active portions of a NOVX protein. In yet another embodiment, a NOVX fusion protein comprises at least three biologically-active portions of a NOVX protein. Within the fusion protein, the term “operatively-linked” is intended to indicate that the NOVX polypeptide and the non-NOVX polypeptide are fused in-frame with one another. The non-NOVX polypeptide can be fused to the N-terminus or C-terminus of the NOVX polypeptide.  
       [0121] In one embodiment, the fusion protein is a GST-NOVX fusion protein in which the NOVX sequences are fused to the C-terminus of the GST (glutathione S-transferase) sequences. Such fusion proteins can facilitate the purification of recombinant NOVX polypeptides.  
       [0122] In another embodiment, the fusion protein is a NOVX protein containing a heterologous signal sequence at its N-terminus. In certain host cells (e.g., mammalian host cells), expression and/or secretion of NOVX can be increased through use of a heterologous signal sequence.  
       [0123] In yet another embodiment, the fusion protein is a NOVX-immunoglobulin fusion protein in which the NOVX sequences are fused to sequences derived from a member of the immunoglobulin protein family. The NOVX-immunoglobulin fusion proteins of the invention can be incorporated into pharmaceutical compositions and administered to a subject to inhibit an interaction between a NOVX ligand and a NOVX protein on the surface of a cell, to thereby suppress NOVX-mediated signal transduction in vivo. The NOVX-immunoglobulin fusion proteins can be used to affect the bioavailability of a NOVX cognate ligand. Inhibition of the NOVX ligand/NOVX interaction may be useful therapeutically for both the treatment of proliferative and differentiative disorders, as well as modulating (e.g. promoting or inhibiting) cell survival. Moreover, the NOVX-immunoglobulin fusion proteins of the invention can be used as immunogens to produce anti-NOVX antibodies in a subject, to purify NOVX ligands, and in screening assays to identify molecules that inhibit the interaction of NOVX with a NOVX ligand.  
       [0124] A NOVX chimeric or fusion protein of the invention can be produced by standard recombinant DNA techniques. For example, DNA fragments coding for the different polypeptide sequences are ligated together in-frame in accordance with conventional techniques, e.g., by employing blunt-ended or stagger-ended termini for ligation, restriction enzyme digestion to provide for appropriate termini, filling-in of cohesive ends as appropriate, alkaline phosphatase treatment to avoid undesirable joining, and enzymatic ligation. In another embodiment, the fusion gene can be synthesized by conventional techniques including automated DNA synthesizers. Alternatively, PCR amplification of gene fragments can be carried out using anchor primers that give rise to complementary overhangs between two consecutive gene fragments that can subsequently be annealed and reamplified to generate a chimeric gene sequence (see, e.g., Ausubel, et al. (eds.) CURRENT PROTOCOLS IN MOLECULAR BIOLOGY, John Wiley &amp; Sons, 1992). Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST polypeptide). A NOVX-encoding nucleic acid can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the NOVX protein.  
       [0125] NOVX Agonists and Antagonists  
       [0126] The invention also pertains to variants of the NOVX proteins that function as either NOVX agonists (i.e., mimetics) or as NOVX antagonists. Variants of the NOVX protein can be generated by mutagenesis (e.g., discrete point mutation or truncation of the NOVX protein). An agonist of the NOVX protein can retain substantially the same, or a subset of, the biological activities of the naturally occurring form of the NOVX protein. An antagonist of the NOVX protein can inhibit one or more of the activities of the naturally occurring form of the NOVX protein by, for example, competitively binding to a downstream or upstream member of a cellular signaling cascade which includes the NOVX protein. Thus, specific biological effects can be elicited by treatment with a variant of limited function. In one embodiment, treatment of a subject with a variant having a subset of the biological activities of the naturally occurring form of the protein has fewer side effects in a subject relative to treatment with the naturally occurring form of the NOVX proteins.  
       [0127] Variants of the NOVX proteins that function as either NOVX agonists (i.e mimetics) or as NOVX antagonists can be identified by screening combinatorial libraries of mutants (e.g., truncation mutants) of the NOVX proteins for NOVX protein agonist or antagonist activity. In one embodiment, a variegated library of NOVX variants is generated by combinatorial mutagenesis at the nucleic acid level and is encoded by a variegated gene library. A variegated library of NOVX variants can be produced by, for example, enzymatically ligating a mixture of synthetic oligonucleotides into gene sequences such that a degenerate set of potential NOVX sequences is expressible as individual polypeptides, or alternatively, as a set of larger fusion proteins (e.g., for phage display) containing the set of NOVX sequences therein. There are a variety of methods which can be used to produce libraries of potential NOVX variants from a degenerate oligonucleotide sequence. Chemical synthesis of a degenerate gene sequence can be performed in an automatic DNA synthesizer, and the synthetic gene then ligated into an appropriate expression vector. Use of a degenerate set of genes allows for the provision, in one mixture, of all of the sequences encoding the desired set of potential NOVX sequences. Methods for synthesizing degenerate oligonucleotides are well-known within the art. See, e.g., Narang, 1983.  Tetrahedron  39: 3; Itakura, et al., 1984.  Annu Rev Biochem.  53: 323; Itakura, et al., 1984.  Science  198: 1056; Ike, et al., 1983.  Nucl. Acids Res.  11: 477.  
       [0128] Polypeptide Libraries  
       [0129] In addition, libraries of fragments of the NOVX protein coding sequences can be used to generate a variegated population of NOVX fragments for screening and subsequent selection of variants of a NOVX protein. In one embodiment, a library of coding sequence fragments can be generated by treating a double stranded PCR fragment of a NOVX coding sequence with a nuclease under conditions wherein nicking occurs only about once per molecule, denaturing the double stranded DNA, renaturing the DNA to form double-stranded DNA that can include sense/antisense pairs from different nicked products, removing single stranded portions from reformed duplexes by treatment with S 1  nuclease, and ligating the resulting fragment library into an expression vector. By this method, expression libraries can be derived which encodes N-terminal and internal fragments of various sizes of the NOVX proteins.  
       [0130] Various techniques are known in the art for screening gene products of combinatorial libraries made by point mutations or truncation, and for screening cDNA libraries for gene products having a selected property. Such techniques are adaptable for rapid screening of the gene libraries generated by the combinatorial mutagenesis of NOVX proteins. The most widely used techniques, which are amenable to high throughput analysis, for screening large gene libraries typically include cloning the gene library into replicable expression vectors, transforming appropriate cells with the resulting library of vectors, and expressing the combinatorial genes under conditions in which detection of a desired activity facilitates isolation of the vector encoding the gene whose product was detected. Recursive ensemble mutagenesis (REM), a new technique that enhances the frequency of functional mutants in the libraries, can be used in combination with the screening assays to identify NOVX variants. See, e.g., Arkin and Yourvan, 1992.  Proc. Natl. Acad. Sci USA  89: 7811-7815; Delgrave, et al., 1993.  Protein Engineering  6:327-331.  
       [0131] Anti-NOVX Antibodies  
       [0132] Included in the invention are antibodies to NOVX proteins, or fragments of NOVX proteins. The term “antibody” as used herein refers to immunoglobulin molecules and immunologically active portions of immunoglobulin (Ig) molecules, i.e., molecules that contain an antigen binding site that specifically binds (immunoreacts with) an antigen. Such antibodies include, but are not limited to, polyclonal, monoclonal, chimeric, single chain, F ab , F ab′  and F (ab′)2  fragments, and an F ab  expression library. In general, antibody molecules obtained from humans relates to any of the classes IgG, IgM, IgA, IgE and IgD, which differ from one another by the nature of the heavy chain present in the molecule. Certain classes have subclasses as well, such as IgG 1 , IgG 2 , and others. Furthermore, in humans, the light chain may be a kappa chain or a lambda chain. Reference herein to antibodies includes a reference to all such classes, subclasses and types of human antibody species.  
       [0133] An isolated protein of the invention intended to serve as an antigen, or a portion or fragment thereof, can be used as an immunogen to generate antibodies that immunospecifically bind the antigen, using standard techniques for polyclonal and monoclonal antibody preparation. The full-length protein can be used or, alternatively, the invention provides antigenic peptide fragments of the antigen for use as immunogens. An antigenic peptide fragment comprises at least 6 amino acid residues of the amino acid sequence of the full length protein, such as an amino acid sequence or SEQ ID NO: 2n, wherein n is an integer between 1 and 102, and encompasses an epitope thereof such that an antibody raised against the peptide forms a specific immune complex with the full length protein or with any fragment that contains the epitope. Preferably, the antigenic peptide comprises at least 10 amino acid residues, or at least 15 amino acid residues, or at least 20 amino acid residues, or at least 30 amino acid residues. Preferred epitopes encompassed by the antigenic peptide are regions of the protein that are located on its surface; commonly these are hydrophilic regions.  
       [0134] In certain embodiments of the invention, at least one epitope encompassed by the antigenic peptide is a region of NOVX that is located on the surface of the protein, e.g, a hydrophilic region. A hydrophobicity analysis of the human NOVX protein sequence will indicate which regions of a NOVX polypeptide arc particularly hydrophilic and, therefore, are likely to encode surface residues useful for targeting antibody production. As a means for targeting antibody production, hydropathy plots showing regions of hydrophilicity and hydrophobicity may be generated by any method well known in the art, including, for example, the Kyte Doolittle or the Hopp Woods methods, either with or without Fourier transformation. See, e g., Hopp and Woods, 1981,  Proc. Nat. Acad Sci USA  78: 3824-3828; Kyte and Doolittle 1982,  J. Mol. Biol.  157: 105-142, each incorporated herein by reference in their entirety. Antibodies that are specific for one or more domains within an antigenic protein, or derivatives, fragments, analogs or homologs thereof, are also provided herein.  
       [0135] The term “epitope” includes any protein determinant capable of specific binding to an immunoglobulin or T-cell receptor. Epitopic determinants usually consist of chemically active surface groupings of molecules such as amino acids or sugar side chains and usually have specific three dimensional structural characteristics, as well as specific charge characteristics. A NOVX polypeptide or a fragment thereof comprises at least one antigenic epitope. An anti-NOVX antibody of the present invention is said to specifically bind to antigen NOVX when the equilibrium binding constant (K D ) is ≦1 μM, preferably ≦100 nM, more preferably ≦10 nM, and most preferably ≦100 pM to about 1 pM, as measured by assays such as radioligand binding assays or similar assays known to those skilled in the art.  
       [0136] A protein of the invention, or a derivative, fragment, analog, homolog or ortholog thereof may be utilized as an immunogen in the generation of antibodies that immunospecifically bind these protein components.  
       [0137] Various procedures known within the art may be used for the production of polyclonal or monoclonal antibodies directed against a protein of the invention, or against derivatives, fragments, analogs homologs or orthologs thereof (see, for example, Antibodies: A Laboratory Manual, Harlow E, and Lane D, 1988, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., incorporated herein by reference). Some of these antibodies are discussed below.  
       [0138] Polyclonal Antibodies  
       [0139] For the production of polyclonal antibodies, various suitable host animals (e.g., rabbit, goat, mouse or other mammal) may be immunized by one or more injections with the native protein, a synthetic variant thereof, or a derivative of the foregoing. An appropriate immunogenic preparation can contain, for example, the naturally occurring immunogenic protein, a chemically synthesized polypeptide representing the immunogenic protein, or a recombinantly expressed immunogenic protein. Furthermore, the protein may be conjugated to a second protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic proteins include but are not limited to keyhole limpet hemocyanin, serum albumin, bovine thyroglobulin, and soybean trypsin inhibitor. The preparation can further include an adjuvant. Various adjuvants used to increase the immunological response include, but are not limited to, Freund&#39;s (complete and incomplete), mineral gels (e.g., aluminum hydroxide), surface active substances (e.g., lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, dinitrophenol, etc), adjuvants usable in humans such as Bacille Calmette-Guerin and Corynebacterium parvum, or similar immunostimulatory agents. Additional examples of adjuvants which can be employed include MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate).  
       [0140] The polyclonal antibody molecules directed against the immunogenic protein can be isolated from the mammal (e.g, from the blood) and further purifed by well known techniques, such as affinity chromatography using protein A or protein G, which provide primarily the IgG fraction of immune serum. Subsequently, or alternatively, the specific antigen which is the target of the immunoglobulin sought, or an epitope thereof, may be immobilized on a column to purify the immune specific antibody by immunoaffinity chromatography. Purification of immunoglobulins is discussed, for example, by D. Wilkinson (The Scientist, published by The Scientist, Inc., Philadelphia Pa., Vol. 14, No. 8 (Apr. 17, 2000), pp. 25-28).  
       [0141] Monoclonal Antibodies  
       [0142] The term “monoclonal antibody” (MAb) or “monoclonal antibody composition”, as used herein, refers to a population of antibody molecules that contain only one molecular species of antibody molecule consisting of a unique light chain gene product and a unique heavy chain gene product. In particular, the complementarity determining regions (CDRs) of the monoclonal antibody are identical in all the molecules of the population. MAbs thus contain an antigen binding site capable of immunoreacting with a particular epitope of the antigen characterized by a unique binding affinity for it.  
       [0143] Monoclonal antibodies can be prepared using hybridoma methods, such as those described by Kohler and Milstein, Nature, 256:495 (1975). In a hybridoma method, a mouse, hamster, or other appropriate host animal, is typically immunized with an immunizing agent to elicit lymphocytes that produce or are capable of producing antibodies that will specifically bind to the immunizing agent. Alternatively, the lymphocytes can be immunized in vitro.  
       [0144] The immunizing agent will typically include the protein antigen, a fragment thereof or a fusion protein thereof. Generally, either peripheral blood lymphocytes are used if cells of human origin are desired, or spleen cells or lymph node cells are used if non-human mammalian sources are desired. The lymphocytes are then fused with an immortalized cell line using a suitable fusing agent, such as polyethylene glycol, to form a hybridoma cell (Goding,  Monoclonal Antibodies: Principles and Practice,  Academic Press, (1986) pp. 59-103). Immortalized cell lines are usually transformed mammalian cells, particularly myeloma cells of rodent, bovine and human origin. Usually, rat or mouse myeloma cell lines are employed. The hybridoma cells can be cultured in a suitable culture medium that preferably contains one or more substances that inhibit the growth or survival of the unfused, immortalized cells. For example, if the parental cells lack the enzyme hypoxanthine guanine phosphoribosyl transferase (HGPRT or HPRT), the culture medium for the hybridomas typically will include hypoxanthine, aminopterin, and thymidine (“HAT medium”), which substances prevent the growth of HGPRT-deficient cells.  
       [0145] Preferred immortalized cell lines are those that fuse efficiently, support stable high level expression of antibody by the selected antibody-producing cells and are sensitive to a medium such as HAT medium. More preferred immortalized cell lines are murine myeloma lines, which can be obtained, for instance, from the Salk Institute Cell Distribution Center, San Diego, Calif. and the American Type Culture Collection, Manassas, Va. Human myeloma and mouse-human heteromyeloma cell lines also have been described for the production of human monoclonal antibodies (Kozbor, J. Immunol., 133:3001 (1984); Brodeur et al., Monoclonal Antibody Production Techniques and Applications, Marcel Dekker, Inc., New York, (1987) pp. 51-63).  
       [0146] The culture medium in which the hybridoma cells are cultured can then be assayed for the presence of monoclonal antibodies directed against the antigen. Preferably, the binding specificity of monoclonal antibodies produced by the hybridoma cells is determined by immunoprecipitation or by an in vitro binding assay, such as radioimmunoassay (RIA) or enzyme-linked immunoabsorbent assay (ELISA). Such techniques and assays are known in the art. The binding affinity of the monoclonal antibody can, for example, be determined by the Scatchard analysis of Munson and Pollard, Anal. Biochem., 107:220 (1980). It is an objective, especially important in therapeutic applications of monoclonal antibodies, to identify antibodies having a high degree of specificity and a high binding affinity for the target antigen.  
       [0147] After the desired hybridoma cells are identified, the clones can be subcloned by limiting dilution procedures and grown by standard methods (Goding,1986). Suitable culture media for this purpose include, for example, Dulbecco&#39;s Modified Eagle&#39;s Medium and RPMI-1640 medium. Alternatively, the hybridoma cells can be grown in vivo as ascites in a mammal.  
       [0148] The monoclonal antibodies secreted by the subclones can be isolated or purified from the culture medium or ascites fluid by conventional immunoglobulin purification procedures such as, for example, protein A-Sepharose, hydroxylapatite chromatography, gel electrophoresis, dialysis, or affinity chromatography.  
       [0149] The monoclonal antibodies can also be made by recombinant DNA methods, such as those described in U.S. Pat. No. 4,816,567. DNA encoding the monoclonal antibodies of the invention can be readily isolated and sequenced using conventional procedures (e g, by using oligonucleotide probes that are capable of binding specifically to genes encoding the heavy and light chains of murine antibodies). The hybridoma cells of the invention serve as a preferred source of such DNA. One isolated, the DNA can be placed into expression vectors, which are then transfected into host cells such as simian COS cells, Chinese hamster ovary (CHO) cells, or myeloma cells that do not otherwise produce immunoglobulin protein, to obtain the synthesis of monoclonal antibodies in the recombinant host cells. The DNA also can be modified, for example, by substituting the coding sequence for human heavy and light chain constant domains in place of the homologous murine sequences (U.S. Pat. No. 4,816,567; Morrison, Nature 368, 812-13 (1994)) or by covalently joining to the immunoglobulin coding sequence all or part of the coding sequence for a non-immunoglobulin polypeptide. Such a non-immunoglobulin polypeptide can be substituted for the constant domains of an antibody of the invention, or can be substituted for the variable domains of one antigen-combining site of an antibody of the invention to create a chimeric bivalent antibody.  
       [0150] Humanized Antibodies  
       [0151] The antibodies directed against the protein antigens of the invention can further comprise humanized antibodies or human antibodies. These antibodies are suitable for administration to humans without engendering an immune response by the human against the administered immunoglobulin. Humanized forms of antibodies are chimeric immunoglobulins, immunoglobulin chains or fragments thereof (such as Fv, Fab, Fab′, F(ab′) 2  or other antigen-binding subsequences of antibodies) that are principally comprised of the sequence of a human immunoglobulin, and contain minimal sequence derived from a non-human immunoglobulin. Humanization can be performed following the method of Winter and co-workers (Jones et al., Nature, 321:522-525 (1986); Riechmann et al., Nature, 332:323-327 (1988); Verhoeyen et al., Science, 239:1534-1536 (1988)), by substituting rodent CDRs or CDR sequences for the corresponding sequences of a human antibody. (See also U.S. Pat. No. 5,225,539.) In some instances, Fv framework residues of the human immunoglobulin are replaced by corresponding non-human residues. Humanized antibodies can also comprise residues which are found neither in the recipient antibody nor in the imported CDR or framework sequences. In general, the humanized antibody will comprise substantially all of at least one, and typically two, variable domains, in which all or substantially all of the CDR regions correspond to those of a non-human immunoglobulin and all or substantially all of the framework regions are those of a human immunoglobulin consensus sequence. The humanized antibody optimally also will comprise at least a portion of an immunoglobulin constant region (Fc), typically that of a human immunoglobulin (Jones et al., 1986; Riechmann et al., 1988; and Presta, Curr. Op. Struct. Biol., 2:593-596 (1992)).  
       [0152] Human Antibodies  
       [0153] Fully human antibodies essentially relate to antibody molecules in which the entire sequence of both the light chain and the heavy chain, including the CDRs, arise from human genes. Such antibodies are termed “human antibodies”, or “fully human antibodies” herein. Human monoclonal antibodies can be prepared by the trioma technique; the human B-cell hybridoma technique (see Kozbor, et al., 1983 Immunol Today 4: 72) and the EBV hybridoma technique to produce human monoclonal antibodies (see Cole, et al., 1985 In: MONOCLONAL ANTIBODIES AND CANCER THERAPY, Alan R. Liss, Inc., pp. 77-96). Human monoclonal antibodies may be utilized in the practice of the present invention and may be produced by using human hybridomas (see Cote, et al., 1983. Proc Natl Acad Sci USA 80: 2026-2030) or by transforming human B-cells with Epstein Barr Virus in vitro (see Cole, et al., 1985 In: MONOCLONAL ANTIBODIES AND CANCER THERAPY, Alan R. Liss, Inc., pp. 77-96).  
       [0154] In addition, human antibodies can also be produced using additional techniques, including phage display libraries (Hoogenboom and Winter, J. Mol. Biol., 227:381 (1991); Marks et al., J. Mol. Biol., 222:581 (1991)). Similarly, human antibodies can be made by introducing human immunoglobulin loci into transgenic animals, e.g, mice in which the endogenous immunoglobulin genes have been partially or completely inactivated. Upon challenge, human antibody production is observed, which closely resembles that seen in humans in all respects, including gene rearrangement, assembly, and antibody repertoire. This approach is described, for example, in U.S. Pat. Nos. 5,545,807; 5,545,806; 5,569,825; 5,625,126; 5,633,425; 5,661,016, and in Marks et al. (Bio/Technology 10, 779-783 (1992)); Lonberg et al. (Nature 368 856-859 (1994)); Morrison ( Nature 368, 812-13 (1994)); Fishwild et al, (Nature Biotechnology 14, 845-51 (1996)); Neuberger (Nature, Biotechnology 14, 826 (1996)); and Lonberg and Huszar (Intern. Rev. Immunol. 13 65-93 (1995)).  
       [0155] Human antibodies may additionally be produced using transgenic nonhuman animals which are modified so as to produce fully human antibodies rather than the animal&#39;s endogenous antibodies in response to challenge by an antigen. (See PCT publication WO94/02602). The endogenous genes encoding the heavy and light immunoglobulin chains in the nonhuman host have been incapacitated, and active loci encoding human heavy and light chain immunoglobulins are inserted into the host&#39;s genome. The human genes are incorporated, for example, using yeast artificial chromosomes containing the requisite human DNA segments. An animal which provides all the desired modifications is then obtained as progeny by crossbreeding intermediate transgenic animals containing fewer than the full complement of the modifications. The preferred embodiment of such a nonhuman animal is a mouse, and is termed the Xenomouse™ as disclosed in PCT publications WO 96/33735 and WO 96/34096. This animal produces B cells which secrete fully human immunoglobulins. The antibodies can be obtained directly from the animal after immunization with an immunogen of interest, as, for example, a preparation of a polyclonal antibody, or alternatively from immortalized B cells derived from the animal, such as hybridomas producing monoclonal antibodies. Additionally, the genes encoding the immunoglobulins with human variable regions can be recovered and expressed to obtain the antibodies directly, or can be further modified to obtain analogs of antibodies such as, for example, single chain Fv molecules.  
       [0156] An example of a method of producing a nonhuman host, exemplified as a mouse, lacking expression of an endogenous immunoglobulin heavy chain is disclosed in U.S. Pat. No. 5,939,598. It can be obtained by a method including deleting the J segment genes from at least one endogenous heavy chain locus in an embryonic stem cell to prevent rearrangement of the locus and to prevent formation of a transcript of a rearranged immunoglobulin heavy chain locus, the deletion being effected by a targeting vector containing a gene encoding a selectable marker; and producing from the embryonic stem cell a transgenic mouse whose somatic and germ cells contain the gene encoding the selectable marker.  
       [0157] A method for producing an antibody of interest, such as a human antibody, is disclosed in U.S. Pat. No. 5,916,771. It includes introducing an expression vector that contains a nucleotide sequence encoding a heavy chain into one mammalian host cell in culture, introducing an expression vector containing a nucleotide sequence encoding a light chain into another mammalian host cell, and fusing the two cells to form a hybrid cell. The hybrid cell expresses an antibody containing the heavy chain and the light chain.  
       [0158] In a further improvement on this procedure, a method for identifying a clinically relevant epitope on an immunogen, and a correlative method for selecting an antibody that binds immunospecifically to the relevant epitope with high affinity, are disclosed in PCT publication WO 99/53049.  
       [0159] F ab  Fragments and Single Chain Antibodies  
       [0160] According to the invention, techniques can be adapted for the production of single-chain antibodies specific to an antigenic protein of the invention (see e g, U.S. Pat. No. 4,946,778). In addition, methods can be adapted for the construction of F ab  expression libraries (see e g., Huse, et al., 1989 Science 246: 1275-1281) to allow rapid and effective identification of monoclonal F ab  fragments with the desired specificity for a protein or derivatives, fragments, analogs or homologs thereof. Antibody fragments that contain the idiotypes to a protein antigen may be produced by techniques known in the art including, but not limited to: (i) an F (ab′)2  fragment produced by pepsin digestion of an antibody molecule; (ii) an F ab  fragment generated by reducing the disulfide bridges of an F (ab′)2  fragment; (iii) an F ab  fragment generated by the treatment of the antibody molecule with papain and a reducing agent and (iv) F v  fragments.  
       [0161] Bispecific Antibodies  
       [0162] Bispecific antibodies are monoclonal, preferably human or humanized, antibodies that have binding specificities for at least two different antigens. In the present case, one of the binding specificities is for an antigenic protein of the invention. The second binding target is any other antigen, and advantageously is a cell-surface protein or receptor or receptor subunit.  
       [0163] Methods for making bispecific antibodies are known in the art. Traditionally, the recombinant production of bispecific antibodies is based on the co-expression of two immunoglobulin heavy-chain/light-chain pairs, where the two heavy chains have different specificities (Milstein and Cuello, Nature, 305:537-539 (1983)). Because of the random assortment of immunoglobulin heavy and light chains, these hybridomas (quadromas) produce a potential mixture of ten different antibody molecules, of which only one has the correct bispecific structure. The purification of the correct molecule is usually accomplished by affinity chromatography steps. Similar procedures are disclosed in WO 93/08829, published May 13, 1993, and in Traunecker et al., EMBO J., 10:3655-3659 (1991).  
       [0164] Antibody variable domains with the desired binding specificities (antibody-antigen combining sites) can be fused to immunoglobulin constant domain sequences. The fusion preferably is with an immunoglobulin heavy-chain constant domain, comprising at least part of the hinge, CH2, and CH3 regions. It is preferred to have the first heavy-chain constant region (CH1) containing the site necessary for light-chain binding present in at least one of the fusions. DNAs encoding the immunoglobulin heavy-chain fusions and, if desired, the immunoglobulin light chain, are inserted into separate expression vectors, and are co-transfected into a suitable host organism. For further details of generating bispecific antibodies see, for example, Suresh et al., Methods in Enzymology, 121:210 (1986).  
       [0165] According to another approach described in WO 96/27011, the interface between a pair of antibody molecules can be engineered to maximize the percentage of heterodimers which are recovered from recombinant cell culture. The preferred interface comprises it least a part of the CH3 region of an antibody constant domain. In this method, one or more small amino acid side chains from the interface of the first antibody molecule are replaced with larger side chains (e g tyrosine or tryptophan). Compensatory “cavities” of identical or similar size to the large side chain(s) are created on the interface of the second antibody molecule by replacing large amino acid side chains with smaller ones (e.g. alanine or threonine). This provides a mechanism for increasing the yield of the heterodimer over other unwanted end-products such as homodimers.  
       [0166] Bispecific antibodies can be prepared as full length antibodies or antibody fragments (e.g. F(ab′) 2  bispecific antibodies). Techniques for generating bispecific antibodies from antibody fragments have been described in the literature. For example, bispecific antibodies can be prepared using chemical linkage. Brennan et al., Science 229:81 (1985) describe a procedure wherein intact antibodies are proteolytically cleaved to generate F(ab′) 2  fragments. These fragments are reduced in the presence of the dithiol complexing agent sodium arsenite to stabilize vicinal dithiols and prevent intermolecular disulfide formation. The Fab′ fragments generated are then converted to thionitrobenzoate (TNB) derivatives. One of the Fab′-TNB derivatives is then reconverted to the Fab′-thiol by reduction with mercaptoethylamine and is mixed with an equimolar amount of the other Fab′-TNB derivative to form the bispecific antibody. The bispecific antibodies produced can be used as agents for the selective immobilization of enzymes.  
       [0167] Additionally, Fab′ fragments can be directly recovered from  E. coli  and chemically coupled to form bispecific antibodies. Shalaby et al., J. Exp. Med. 175:217-225 (1992) describe the production of a fully humanized bispecific antibody F(ab′) 2  molecule. Each Fab′ fragment was separately secreted from  E. coli  and subjected to directed chemical coupling in vitro to form the bispecific antibody. The bispecific antibody thus formed was able to bind to cells overexpressing the ErbB2 receptor and normal human T cells, as well as trigger the lytic activity of human cytotoxic lymphocytes against human breast tumor targets.  
       [0168] Various techniques for making, and isolating bispecific antibody fragments directly from recombinant cell culture have also been described. For example, bispecific antibodies have been produced using leucine zippers. Kostelny et al., J. Immunol. 148(5):1547-1553 (1992). The leucine zipper peptides from the Fos and Jun proteins were linked to the Fab′ portions of two different antibodies by gene fusion. The antibody homodimers were reduced at the hinge region to form monomers and then re-oxidized to form the antibody heterodimers. This method can also be utilized for the production of antibody homodimers. The “diabody” technology described by Hollinger et al., Proc. Natl. Acad. Sci. USA 90:6444-6448 (1993) has provided an alternative mechanism for making bispecific antibody fragments. The fragments comprise a heavy-chain variable domain (V H ) connected to a light-chain variable domain (V L ) by a linker which is too short to allow pairing between the two domains on the same chain. Accordingly, the V L  and V H  domains of one fragment are forced to pair with the complementary V L  and V H  domains of another fragment, thereby forming two antigen-binding sites. Another strategy for making bispecific antibody fragments by the use of single-chain Fv (sFv) dimers has also been reported. See, Gruber et al., J. Immunol. 152:5368 (1994).  
       [0169] Antibodies with more than two valencies are contemplated. For example, trispecific antibodies can be prepared. Tutt et al., J. Immunol. 147:60 (1991).  
       [0170] Exemplary bispecific antibodies can bind to two different epitopes, at least one of which originates in the protein antigen of the invention. Alternatively, an anti-antigenic arm of an immunoglobulin molecule can be combined with an arm which binds to a triggering molecule on a leukocyte such as a T-cell receptor molecule (e.g. CD2, CD3, CD28, or B7), or Fc receptors for IgG (FcγR), such as FcγRI (CD64), FcγRII (CD32) and FcγRIII (CD16) so as to focus cellular defense mechanisms to the cell expressing the particular antigen. Bispecific antibodies can also be used to direct cytotoxic agents to cells which express a particular antigen. These antibodies possess an antigen-binding arm and an arm which binds a cytotoxic agent or a radionuclide chelator, such as EOTUBE, DPTA, DOTA, or TETA. Another bispecific antibody of interest binds the protein antigen described herein and further binds tissue factor (TF).  
       [0171] Heteroconjugate Antibodies  
       [0172] Heteroconjugate antibodies are also within the scope of the present invention. Heteroconjugate antibodies are composed of two covalently joined antibodies. Such antibodies have, for example, been proposed to target immune system cells to unwanted cells (U.S. Pat. No. 4,676,980), and for treatment of HIV infection (WO 91/00360; WO 92/200373; EP 03089). It is contemplated that the antibodies can be prepared in vitro using known methods in synthetic protein chemistry, including those involving crosslinking agents. For example, immunotoxins can be constructed using a disulfide exchange reaction or by forming a thioether bond. Examples of suitable reagents for this purpose include iminothiolate and methyl-4-mercaptobutyrimidate and those disclosed, for example, in U.S. Pat. No. 4,676,980.  
       [0173] Effector Function Engineering  
       [0174] It can be desirable to modify the antibody of the invention with respect to effector function, so as to enhance, e.g., the effectiveness of the antibody in treating cancer. For example, cysteine residue(s) can be introduced into the Fc region, thereby allowing interchain disulfide bond formation in this region. The homodimeric antibody thus generated can have improved internalization capability and/or increased complement-mediated cell killing and antibody-dependent cellular cytotoxicity (ADCC). See Caron et al., J. Exp Med., 176: 1191-1195 (1992) and Shopes, J. Immunol., 148: 2918-2922 (1992). Homodimeric antibodies with enhanced anti-tumor activity can also be prepared using heterobifunctional cross-linkers as described in Wolff et al. Cancer- Research, 53: 2560-2565 (1993). Alternatively, an antibody can be engineered that has dual Fc regions and can thereby have enhanced complement lysis and ADCC capabilities. See Stevenson et al., Anti-Cancer Drug Design, 3: 219-230 (1989).  
       [0175] Immunoconjugates  
       [0176] The invention also pertains to immunoconjugates comprising an antibody conjugated to a cytotoxic agent such as a chemotherapeutic agent, toxin (e.g., an enzymatically active toxin of bacterial, fungal, plant, or animal origin, or fragments thereof), or a radioactive isotope (i.e., a radioconjugate).  
       [0177] Chemotherapeutic agents useful in the generation of such immunoconjugates have been described above. Enzymatically active toxins and fragments thereof that can be used include diphtheria A chain, nonbinding active fragments of diphtheria toxin, exotoxin A chain (from  Pseudomonas aeruginosa ), ricin A chain, abrin A chain, modeccin A chain, alpha-sarcin,  Aleurites fordii  proteins, dianthin proteins,  Phytolaca americana  proteins (PAPI, PAPII, and PAP-S), momordica charantia inhibitor, curcin, cirotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictocin, phenomycin, enomycin, and the tricothecenes. A variety of radionuclides are available for the production of radioconjugated antibodies. Examples include  212 Bi,  131 I,  131 In,  90 Y, and  186 Re.  
       [0178] Conjugates of the antibody and cytotoxic agent are made using a variety of bifunctional protein-coupling agents such as N-succinimidyl-3-(2-pyridyldithiol) propionate (SPDP), iminothiolane (IT), bifunctional derivatives of imidoesters (such as dimethyl adipimidate HCL), active esters (such as disuccinimidyl suberate), aldehydes (such as glutareldelhyde), bis-azido compounds (such as bis (p-azidobenzoyl) hexanediamine), bis-diazonium derivatives (such as bis-(p-diazoniumbenzoyl)-ethylenediamine), diisocyanates (such as tolyene 2,6-dilsocyanate), and bis-active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene). For example, a ricin immunotoxin can be prepared as described in Vitetta et al.,  Science,  238: 1098 (1987). Carbon-14-labeled 1-isothiocyanatobenzyl-3 -methyldiethylene triaminepentaacetic acid (MX-DTPA) is an exemplary chelating agent for conjugation of radionucleotide to the antibody. See WO94/11026.  
       [0179] In another embodiment, the antibody can be conjugated to a “receptor” (such streptavidin) for utilization in tumor pretargeting wherein the antibody-receptor conjugate is administered to the patient, followed by removal of unbound conjugate from the circulation using a clearing agent and then administration of a “ligand” (e.g., avidin) that is in turn conjugated to a cytotoxic agent.  
       [0180] Immunoliposomes  
       [0181] The antibodies disclosed herein can also be formulated as immunoliposomes. Liposomes containing the antibody are prepared by methods known in the art, such as described in Epstein et al., Proc. Natl. Acad. Sci. USA, 82: 3688 (1985); Hwang et al., Proc. Natl Acad. Sci. USA, 77: 4030 (1980); and U.S. Pat. Nos. 4,485,045 and 4,544,545. Liposomes with enhanced circulation time are disclosed in U.S. Pat. No. 5,013,556.  
       [0182] Particularly useful liposomes can be generated by the reverse-phase evaporation method with a lipid composition comprising phosphatidylcholine, cholesterol, and PEG-derivatized phosphatidylethanolamine (PEG-PE). Liposomes are extruded through filters of defined pore size to yield liposomes with the desired diameter. Fab′ fragments of the antibody of the present invention can be conjugated to the liposomes as described in Martin et al., J. Biol. Chem., 257: 286-288 (1982) via a disulfide-interchange reaction. A chemotherapeutic agent (such as Doxorubicin) is optionally contained within the liposome. See Gabizon et al., J. National Cancer Inst., 81(19): 1484 (1989).  
       [0183] Diagnostic Applications of Antibodies Directed Against the Proteins of the Invention  
       [0184] In one embodiment, methods for the screening of antibodies that possess the desired specificity include, but are not limited to, enzyme linked immunosorbent assay (ELISA) and other immunologically mediated techniques known within the art. In a specific embodiment, selection of antibodies that are specific to a particular domain of an NOVX protein is facilitated by generation of hybridomas that bind to the fragment of an NOVX protein possessing such a domain. Thus, antibodies that are specific for a desired domain within an NOVX protein, or derivatives, fragments, analogs or homologs thereof, are also provided herein.  
       [0185] Antibodies directed against a NOVX protein of the invention may be used in methods known within the art relating to the localization and/or quantitation of a NOVX protein (e.g., for use in measuring levels of the NOVX protein within appropriate physiological samples, for use in diagnostic methods, for use in imaging the protein, and the like). In a given embodiment, antibodies specific to a NOVX protein, or derivative, fragment, analog or homolog thereof, that contain the antibody derived antigen binding domain, are utilized as pharmacologically active compounds (referred to hereinafter as “Therapeutics”).  
       [0186] An antibody specific for a NOVX protein of the invention (e.g., a monoclonal antibody or a polyclonal antibody) can be used to isolate a NOVX polypeptide by standard techniques, such as immunoaffinity, chromatography or immunoprecipitation. An antibody to a NOVX polypeptide can facilitate the purification of a natural NOVX antigen from cells, or of a recombinantly produced NOVX antigen expressed in host cells. Moreover, such an anti-NOVX antibody can be used to detect the antigenic NOVX protein (e.g., in a cellular lysate or cell supernatant) in order to evaluate the abundance and pattern of expression of the antigenic NOVX protein. Antibodies directed against a NOVX protein can be used diagnostically to monitor protein levels in tissue as part of a clinical testing procedure, e.g., to, for example, determine the efficacy of a given treatment regimen. Detection can be facilitated by coupling (i.e., physically linking) the antibody to a detectable substance. Examples of detectable substances include various enzymes, prosthetic groups, fluorescent materials, luminescent materials, bioluminescent materials, and radioactive materials. Examples of suitable enzymes include horseradish peroxidase, alkaline phosphatase, β-galactosidase, or acetylcholinesterase; examples of suitable prosthetic group complexes include streptavidin/biotin and avidin/biotin; examples of suitable fluorescent materials include umbelliferone, fluorescein, fluorescein isothiocyanate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride or phycocrythrin; an example of a luminescent material includes luminol; examples of bioluminescent materials include luciferase, luciferin, and aequorin, and examples of suitable radioactive material include  125 I,  131 I,  35 S or  3 H.  
       [0187] Antibody Therapeutics  
       [0188] Antibodies of the invention, including polyclonal, monoclonal, humanized and fully human antibodies, may used as therapeutic agents. Such agents will generally be employed to treat or prevent a disease or pathology in a subject. An antibody preparation, preferably one having high specificity and high affinity for its target antigen, is administered to the subject and will generally have an effect due to its binding with the target. Such an effect may be one of two kinds, depending on the specific nature of the interaction between the given antibody molecule and the target antigen in question. In the first instance, administration of the antibody may abrogate or inhibit the binding of the target with an endogenous ligand to which it naturally binds. In this case, the antibody binds to the target and masks a binding site of the naturally occurring ligand, wherein the ligand serves as an effector molecule. Thus the receptor mediates a signal transduction pathway for which ligand is responsible.  
       [0189] Alternatively, the effect may be one in which the antibody elicits a physiological result by virtue of binding to an effector binding site on the target molecule. In this case the target, a receptor having an endogenous ligand which may be absent or defective in the disease or pathology, binds the antibody as a surrogate effector ligand, initiating a receptor-based signal transduction event by the receptor.  
       [0190] A therapeutically effective amount of an antibody of the invention relates generally to the amount needed to achieve a therapeutic objective. As noted above, this may be a binding interaction between the antibody and its target antigen that, in certain cases, interferes with the functioning of the target, and in other cases, promotes a physiological response. The amount required to be administered will furthermore depend on the binding affinity of the antibody for its specific antigen, and will also depend on the rate at which an administered antibody is depleted from the free volume other subject to which it is administered. Common ranges for therapeutically effective dosing of an antibody or antibody fragment of the invention may be, by way of nonlimiting example, from about 0.1 mg/kg body weight to about 50 mg/kg body weight. Common dosing frequencies may range, for example, from twice daily to once a week.  
       [0191] Pharmaceutical Compositions of Antibodies  
       [0192] Antibodies specifically binding a protein of the invention, as well as other molecules identified by the screening assays disclosed herein, can be administered for the treatment of various disorders in the form of pharmaceutical compositions. Principles and considerations involved in preparing such compositions, as well as guidance in the choice of components are provided, for example, in Remington: The Science And Practice Of Pharmacy 19th ed. (Alfonso R. Gennaro, et al., editors) Mack Pub. Co., Easton, Pa.: 1995; Drug Absorption Enhancement: Concepts, Possibilities, Limitations, And Trends, Harwood Academic Publishers, Langhorne, Pa., 1994; and Peptide And Protein Drug Delivery (Advances In Parenteral Sciences, Vol. 4), 1991, M. Dekker, New York.  
       [0193] If the antigenic protein is intracellular and whole antibodies are used as inhibitors, internalizing antibodies are preferred. However, liposomes can also be used to deliver the antibody, or an antibody fragment, into cells. Where antibody fragments are used, the smallest inhibitory fragment that specifically binds to the binding domain of the target protein is preferred. For example, based upon the variable-region sequences of an antibody, peptide molecules can be designed that retain the ability to bind the target protein sequence. Such peptides can be synthesized chemically and/or produced by recombinant DNA technology. See, e g., Marasco et al., Proc. Natl. Acad. Sci. USA, 90: 7889-7893 (1993). The formulation herein can also contain more than one active compound as necessary for the particular indication being treated, preferably those with complementary activities that do not adversely affect each other. Alternatively, or in addition, the composition can comprise an agent that enhances its function, such as, for example, a cytotoxic agent, cytokine, chemotherapeutic agent, or growth-inhibitory agent. Such molecules are suitably present in combination in amounts that are effective for the purpose intended.  
       [0194] The active ingredients can also be entrapped in microcapsules prepared, for example, by coacervation techniques or by interfacial polymerization, for example, hydroxymethylcellulose or gelatin-microcapsules and poly-(methylmethacrylate) microcapsules, respectively, in colloidal drug delivery systems (for example, liposomes, albumin microspheres, microemulsions, nano-particles, and nanocapsules) or in macroemulsions.  
       [0195] The formulations to be used for in vivo administration must be sterile. This is readily accomplished by filtration through sterile filtration membranes.  
       [0196] Sustained-release preparations can be prepared. Suitable examples of sustained-release preparations include semipermeable matrices of solid hydrophobic polymers containing the antibody, which matrices are in the form of shaped articles, e.g., films, or microcapsules. Examples of sustained-release matrices include polyesters, hydrogels (for example, poly(2-hydroxyethyl-methacrylate), or poly(vinylalcohol)), polylactides (U.S. Pat. No. 3,773,919), copolymers of L-glutamic acid and γ ethyl-L-glutamate, non-degradable ethylene-vinyl acetate, degradable lactic acid-glycolic acid copolymers such as the LUPRON DEPOT™ (injectable microspheres composed of lactic acid-glycolic acid copolymer and leuprolide acetate), and poly-D-(−)-3-hydroxybutyric acid. While polymers such as ethylene-vinyl acetate and lactic acid-glycolic acid enable release of molecules for over 100 days, certain hydrogels release proteins for shorter time periods.  
       [0197] ELISA Assay  
       [0198] An agent for detecting an analyte protein is an antibody capable of binding to an analyte protein, preferably an antibody with a detectable label. Antibodies can be polyclonal, or more preferably, monoclonal. An intact antibody, or a fragment thereof (e.g, F ab  or F (ab)2 ) can be used. The term “labeled”, with regard to the probe or antibody, is intended to encompass direct labeling of the probe or antibody by coupling (i.e., physically linking) a detectable substance to the probe or antibody, as well as indirect labeling of the probe or antibody by reactivity with another reagent that is directly labeled. Examples of indirect labeling include detection of a primary antibody using a fluorescently-labeled secondary antibody and end-labeling of a DNA probe with biotin such that it can be detected with fluorescently-labeled streptavidin. The term “biological sample” is intended to include tissues, cells and biological fluids isolated from a subject, as well as tissues, cells and fluids present within a subject. Included within the usage of the term “biological sample”, therefore, is blood and a fraction or component of blood including blood serum, blood plasma, or lymph. That is, the detection method of the invention can be used to detect an analyte mRNA, protein, or genomic DNA in a biological sample in vitro as well as in vivo. For example, in vitro techniques for detection of an analyte mRNA include Northern hybridizations and in situ hybridizations. In vitro techniques for detection of an analyte protein include enzyme linked immunosorbent assays (ELISAs), Western blots, immunoprecipitations, and immunofluorescence. In vitro techniques for detection of an analyte genomic DNA include Southern hybridizations. Procedures for conducting immunoassays are described, for example in “ELISA: Theory and Practice: Methods in Molecular Biology”, Vol. 42, J. R. Crowther (Ed.) Human Press, Totowa, N.J., 1995; “Immunoassay”, E. Diamandis and T. Christopoulus, Academic Press, Inc., San Diego, Calif., 1996; and “Practice and Thory of Enzyme Immunoassays”, P. Tijssen, Elsevier Science Publishers, Amsterdam, 1985. Furthermore, in vivo techniques for detection of an analyte protein include introducing into a subject a labeled anti-an analyte protein antibody. For example, the antibody can be labeled with a radioactive marker whose presence and location in a subject can be detected by standard imaging techniques.  
       [0199] NOVX Recombinant Expression Vectors and Host Cells  
       [0200] Another aspect of the invention pertains to vectors, preferably expression vectors, containing a nucleic acid encoding a NOVX protein, or derivatives, fragments, analogs or homologs thereof. As used herein, the term “vector” refers to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a “plasmid”, which refers to a circular double stranded DNA loop into which additional DNA segments can be ligated. Another type of vector is a viral vector, wherein additional DNA segments can be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors). Other vectors (e.g., non-episomal mammalian vectors) are integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively-linked. Such vectors are referred to herein as “expression vectors”. In general, expression vectors of utility in recombinant DNA techniques are often in the form of plasmids. In the present specification, “plasmid” and “vector” can be used interchangeably as the plasmid is the most commonly used form of vector. However, the invention is intended to include such other forms of expression vectors, such as viral vectors (e.g., replication defective retroviruses, adenoviruses and adeno-associated viruses), which serve equivalent functions.  
       [0201] The recombinant expression vectors of the invention comprise a nucleic acid of the invention in a form suitable for expression of the nucleic acid in a host cell, which means that the recombinant expression vectors include one or more regulatory sequences, selected on the basis of the host cells to be used for expression, that is operatively-linked to the nucleic acid sequence to be expressed. Within a recombinant expression vector, “operably-linked” is intended to mean that the nucleotide sequence of interest is linked to the regulatory sequence(s) in a manner that allows for expression of the nucleotide sequence (e g, in an in vitro transcription/translation system or in a host cell when the vector is introduced into the host cell).  
       [0202] The term “regulatory sequence” is intended to includes promoters, enhancers and other expression control elements (e.g., polyadenylation signals). Such regulatory sequences are described, for example, in Goeddel, GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif. (1990). Regulatory sequences include those that direct constitutive expression of a nucleotide sequence in many types of host cell and those that direct expression of the nucleotide sequence only in certain host cells (e.g., tissue-specific regulatory sequences). It will be appreciated by those skilled in the art that the design of the expression vector can depend on such factors as the choice of the host cell to be transformed, the level of expression of protein desired, etc. The expression vectors of the invention can be introduced into host cells to thereby produce proteins or peptides, including fusion proteins or peptides, encoded by nucleic acids as described herein (e.g., NOVX proteins, mutant forms of NOVX proteins, fusion proteins, etc.).  
       [0203] The recombinant expression vectors of the invention can be designed for expression of NOVX proteins in prokaryotic or eukaryotic cells. For example, NOVX proteins can be expressed in bacterial cells such as  Escherichia coli,  insect cells (using baculovirus expression vectors) yeast cells or mammalian cells. Suitable host cells are discussed further in Goeddel, GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif (1990). Alternatively, the recombinant expression vector can be transcribed and translated in vitro, for example using T7 promoter regulatory sequences and T7 polymerase.  
       [0204] Expression of proteins in prokaryotes is most often carried out in  Escherichia coli  with vectors containing constitutive or inducible promoters directing the expression of either fusion or non-fusion proteins. Fusion vectors add a number of amino acids to a protein encoded therein, usually to the amino terminus of the recombinant protein. Such fusion vectors typically serve three purposes: (i) to increase expression of recombinant protein; (ii) to increase the solubility of the recombinant protein; and (iii) to aid in the purification of the recombinant protein by acting as a ligand in affinity purification. Often, in fusion expression vectors, a proteolytic cleavage site is introduced at the junction of the fusion moiety and the recombinant protein to enable separation of the recombinant protein from the fusion moiety subsequent to purification of the fusion protein. Such enzymes, and their cognate recognition sequences, include Factor Xa, thrombin and enterokinase. Typical fusion expression vectors include pGEX (Pharmacia Biotech Inc; Smith and Johnson, 1988.  Gene  67: 31-40), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) that fuse glutathione S-transferase (GST), maltose E binding protein, or protein A, respectively, to the target recombinant protein.  
       [0205] Examples of suitable inducible non-fusion  E. coli  expression vectors include pTrc (Amrann et al., (1988) Gene 69:301-315) and pET 11d (Studier et al., GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif. (1990) 60-89).  
       [0206] One strategy to maximize recombinant protein expression in  E. coli  is to express the protein in a host bacteria with an impaired capacity to proteolytically cleave the recombinant protein. See, e.g., Gottesman, GENE EXPRESSION TECHNOLOGY: METHODS IN ENZYMOLOGY 185, Academic Press, San Diego, Calif. (1990) 119-128. Another strategy is to alter the nucleic acid sequence of the nucleic acid to be inserted into an expression vector so that the individual codons for each amino acid are those preferentially utilized in  E. coli  (see, e.g., Wada, et al., 1992.  Nucl. Acids Res.  20: 2111-2118). Such alteration of nucleic acid sequences of the invention can be carried out by standard DNA synthesis techniques.  
       [0207] In another embodiment, the NOVX expression vector is a yeast expression vector. Examples of vectors for expression in yeast  Saccharomyces cerivisae  include pYepSec1 (Baldari, et al., 1987.  EMBO. J.  6: 229-234), pMFa (Kurjan and Herskowitz, 1982.  Cell  30: 933-943), pJRY88 (Schultz et al., 1987.  Gene  54: 113-123), pYES2 (Invitrogen Corporation, San Diego, Calif.), and picZ (InVitrogen Corp, San Diego, Calif.).  
       [0208] Alternatively, NOVX can be expressed in insect cells using baculovirus expression vectors. Baculovirus vectors available for expression of proteins in cultured insect cells (e g., SF9 cells) include the pAc series (Smith, et al., 1983.  Mol. Cell. Biol.  3: 2156-2165) and the pVL series (Lucklow and Summers, 1989.  Virology  170: 31-39).  
       [0209] In yet another embodiment, a nucleic acid of the invention is expressed in mammalian cells using a mammalian expression vector. Examples of mammalian expression vectors include pCDM8 (Seed, 1987.  Nature  329: 840) and pMT2PC (Kaufman, et al., 1987.  EMBO J  6: 187-195). When used in mammalian cells, the expression vector&#39;s control functions are often provided by viral regulatory elements. For example, commonly used promoters are derived from polyoma, adenovirus 2, cytomegalovirus, and simian virus 40. For other suitable expression systems for both prokaryotic and eukaryotic cells see, e.g., Chapters 16 and 17 of Sambrook, et al., MOLECULAR CLONING: A LABORATORY MANUAL. 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press Cold Spring Harbor, N.Y., 1989.  
       [0210] In another embodiment, the recombinant mammalian expression vector is capable of directing expression of the nucleic acid preferentially in a particular cell type (e.g, tissue-specific regulatory elements are used to express the nucleic acid). Tissue-specific regulatory elements are known in the art. Non-limiting examples of suitable tissue-specific promoters include the albumin promoter (liver-specific; Pinkert, et al., 1987.  Genes Dev  1: 268-277), lymphoid-specific promoters (Calame and Eaton, 1988.  Adv. Immunol.  43: 235-275), in particular promoters of T cell receptors (Winoto and Baltimore, 1989.  EMBO J.  8: 729-733) and immunoglobulins (Banerji, et al., 1983.  Cell  33: 729-740; Queen and Baltimore, 1983.  Cell  33: 741-748), neuron-specific promoters (e.g., the neurofilament promoter; Byrne and Ruddle, 1989.  Proc Natl Acad Sci USA  86: 5473-5477), pancreas-specific promoters (Edlund, et al., 1985.  Science  230: 912-916), and mammary gland-specific promoters (e.g., milk whey promoter; U.S. Pat. No. 4,873,316 and European Application Publication No. 264,166). Developmentally-regulated promoters are also encompassed, e g., the murine hox promoters (Kessel and Gruss, 1990.  Science  249: 374-379) and the α-fetoprotein promoter (Campes and Tilghman, 1989.  Genes Dev.  3: 537-546).  
       [0211] The invention further provides a recombinant expression vector comprising a DNA molecule of the invention cloned into the expression vector in an antisense orientation. That is, the DNA molecule is operatively-linked to a regulatory sequence in a manner that allows for expression (by transcription of the DNA molecule) of an RNA molecule that is antisense to NOVX mRNA. Regulatory sequences operatively linked to a nucleic acid cloned in the antisense orientation can be chosen that direct the continuous expression of the antisense RNA molecule in a variety of cell types, for instance viral promoters and/or enhancers, or regulatory sequences can be chosen that direct constitutive, tissue specific or cell type specific expression of antisense RNA. The antisense expression vector can be in the form of a recombinant plasmid, phagemid or attenuated virus in which antisense nucleic acids are produced under the control of a high efficiency regulatory region, the activity of which can be determined by the cell type into which the vector is introduced. For a discussion of the regulation of gene expression using antisense genes see, e.g., Weintraub, et al., “Antisense RNA as a molecular tool for genetic analysis,”  Reviews - Trends in Genetics,  Vol. 1(1) 1986.  
       [0212] Another aspect of the invention pertains to host cells into which a recombinant expression vector of the invention has been introduced. The terms “host cell” and “recombinant host cell” are used interchangeably herein. It is understood that such terms refer not only to the particular subject cell but also to the progeny or potential progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein.  
       [0213] A host cell can be any prokaryotic or eukaryotic cell. For example, NOVX protein can be expressed in bacterial cells such as  E. coli,  insect cells, yeast or mammalian cells (such as Chinese hamster ovary cells (CHO) or COS cells). Other suitable host cells are known to those skilled in the art.  
       [0214] Vector DNA can be introduced into prokaryotic or eukaryotic cells via conventional transformation or transfection techniques. As used herein, the terms “transformation” and “transfection” are intended to refer to a variety of art-recognized techniques for introducing foreign nucleic acid (e g, DNA) into a host cell, including calcium phosphate or calcium chloride co-precipitation, DEAE-dextran-mediated transfection, lipofection, or electroporation. Suitable methods for transforming or transfecting host cells can be found in Sambrook, et al. (MOLECULAR CLONING: A LABORATORY MANUAL. 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989), and other laboratory manuals.  
       [0215] For stable transfection of mammalian cells, it is known that, depending upon the expression vector and transfection technique used, only a small fraction of cells may integrate the foreign DNA into their genome. In order to identify and select these integrants, a gene that encodes a selectable marker (e.g., resistance to antibiotics) is generally introduced into the host cells along with the gene of interest. Various selectable markers include those that confer resistance to drugs, such as G418, hygromycin and methotrexate. Nucleic acid encoding a selectable marker can be introduced into a host cell on the same vector as that encoding NOVX or can be introduced on a separate vector. Cells stably transfected with the introduced nucleic acid can be identified by drug selection (e.g., cells that have incorporated the selectable marker gene will survive, while the other cells die).  
       [0216] A host cell of the invention, such as a prokaryotic or eukaryotic host cell in culture, can be used to produce (i.e., express) NOVX protein. Accordingly, the invention further provides methods for producing NOVX protein using the host cells of the invention. In one embodiment, the method comprises culturing the host cell of invention (into which a recombinant expression vector encoding NOVX protein has been introduced) in a suitable medium such that NOVX protein is produced. In another embodiment, the method further comprises isolating NOVX protein from the medium or the host cell.  
       [0217] Transgenic NOVX Animals  
       [0218] The host cells of the invention can also be used to produce non-human transgenic animals. For example, in one embodiment, a host cell of the invention is a fertilized oocyte or an embryonic stem cell into which NOVX protein-coding sequences have been introduced. Such host cells can then be used to create nonhuman transgenic animals in which exogenous NOVX sequences have been introduced into their genome or homologous recombinant animals in which endogenous NOVX sequences have been altered. Such animals are useful for studying the function and/or activity of NOVX protein and for identifying and/or evaluating modulators of NOVX protein activity. As used herein, a “transgenic animal” is a non-human animal, preferably a mammal, more preferably a rodent such as a rat or mouse, in which one or more of the cells of the animal includes a transgene. Other examples of transgenic animals include non-human primates, sheep, dogs, cows, goats, chickens, amphibians, etc. A transgene is exogenous DNA that is integrated into the genome of a cell from which a transgenic animal develops and that remains in the genome of the mature animal, thereby directing the expression of an encoded gene product in one or more cell types or tissues of the transgenic animal. As used herein, a “homologous recombinant animal” is a non-human animal, preferably a mammal, more preferably a mouse, in which an endogenous NOVX gene has been altered by homologous recombination between the endogenous gene and an exogenous DNA molecule introduced into a cell of the animal, e.g., an embryonic cell of the animal, prior to development of the animal.  
       [0219] A transgenic animal of the invention can be created by introducing NOVX-encoding nucleic acid into the male pronuclei of a fertilized oocyte (e.g, by microinjection, retroviral infection) and allowing the oocyte to develop in a pseudopregnant female foster animal. The human NOVX cDNA sequences, i e., any one of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, can be introduced as a transgene into the genome of a non-human animal. Alternatively, a non-human homologue of the human NOVX gene, such as a mouse NOVX gene, can be isolated based on hybridization to the human NOVX cDNA (described further supra) and used as a transgene. Intronic sequences and polyadenylation signals can also be included in the transgene to increase the efficiency of expression of the transgene. A tissue-specific regulatory sequence(s) can be operably-linked to the NOVX transgene to direct expression of NOVX protein to particular cells. Methods for generating transgenic animals via embryo manipulation and microinjection, particularly animals such as mice, have become conventional in the art and arc described, for example, in U.S. Pat. Nos. 4,736,866; 4,870,009; and 4,873,191; and Hogan, 1986. In: MANIPULATING THE MOUSE EMBRYO, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. Similar methods are used for production of other transgenic animals. A transgenic founder animal can be identified based upon the presence of the NOVX transgene in its genome and/or expression of NOVX mRNA in tissues or cells of the animals. A transgenic founder animal can then be used to breed additional animals carrying the transgene. Moreover, transgenic animals carrying a transgene-encoding NOVX protein can further be bred to other transgenic animals carrying other transgenes.  
       [0220] To create a homologous recombinant animal, a vector is prepared which contains at least a portion of a NOVX gene into which a deletion, addition or substitution has been introduced to thereby alter, e.g., functionally disrupt, the NOVX gene. The NOVX gene can be a human gene (e.g, the cDNA of any one of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102), but more preferably, is a non-human homologue of a human NOVX gene. For example, a mouse homologue of human NOVX gene of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, can be used to construct a homologous recombination vector suitable for altering an endogenous NOVX gene in the mouse genome. In one embodiment, the vector is designed such that, upon homologous recombination, the endogenous NOVX gene is functionally disrupted (i.e., no longer encodes a functional protein; also referred to as a “knock out” vector).  
       [0221] Alternatively, the vector can be designed such that, upon homologous recombination, the endogenous NOVX gene is mutated or otherwise altered but still encodes functional protein (e g, the upstream regulatory region can be altered to thereby alter the expression of the endogenous NOVX protein). In the homologous recombination vector, the altered portion of the NOVX gene is flanked at its 5′- and 3′-termini by additional nucleic acid of the NOVX gene to allow for homologous recombination to occur between the exogenous NOVX gene carried by the vector and an endogenous NOVX gene in an embryonic stem cell. The additional flanking NOVX nucleic acid is of sufficient length for successful homologous recombination with the endogenous gene. Typically, several kilobases of flanking DNA (both at the 5′- and 3′-termini) are included in the vector. See, e g, Thomas, et al., 1987.  Cell  51: 503 for a description of homologous recombination vectors. The vector is ten introduced into an embryonic stem cell line (e.g. by electroporation) and cells in which the introduced NOVX gene has homologously-recombined with the endogenous NOVX gene are selected. See, e g., Li, et al., 1992.  Cell  69: 915.  
       [0222] The selected cells are then injected into a blastocyst of an animal (e g., a mouse) to form aggregation chimeras. See, e.g., Bradley, 1987. In: TERATOCARCINOMAS AND EMBRYONIC STEM CELLS: A PRACTICAL APPROACH, Robertson, ed. IRL, Oxford, pp. 113-152. A chimeric embryo can then be implanted into a suitable pseudopregnant female foster animal and the embryo brought to term. Progeny harboring the homologously-recombined DNA in their germ cells can be used to breed animals in which all cells of the animal contain the homologously-recombined DNA by germline transmission of the transgene. Methods for constructing homologous recombination vectors and homologous recombinant animals are described further in Bradley, 1991.  Curr. Opin Biotechnol.  2: 823-829; PCT International Publication Nos.: WO 90/11354; WO 91/01140; WO 92/0968; and WO 93/04169.  
       [0223] In another embodiment, transgenic non-humans animals can be produced that contain selected systems that allow for regulated expression of the transgene. One example of such a system is the cre/loxP recombinase system of bacteriophage P1. For a description of the cre/loxP recombinase system, See, e.g., Lakso, et al., 1992.  Proc. Natl. Acad. Sci. USA  89: 6232-6236. Another example of a recombinase system is the FLP recombinase system of  Saccharomyces cerevisiae  See, O&#39;Gorman, et al., 1991.  Science  251:1351-1355. If a cre/loxP recombinase system is used to regulate expression of the transgene, animals containing transgenes encoding both the Cre recombinase and a selected protein are required. Such animals can be provided through the construction of “double” transgenic animals, e.g., by mating two transgenic animals, one containing a transgene encoding a selected protein and the other containing a transgene encoding a recombinase.  
       [0224] Clones of the non-human transgenic animals described herein can also be produced according to the methods described in Wilmut, et al., 1997.  Nature  385: 810-813. In brief, a cell (e.g., a somatic cell) from the transgenic animal can be isolated and induced to exit the growth cycle and enter G 0  phase. The quiescent cell can then be fused, e g., through the use of electrical pulses, to an enucleated oocyte from an animal of the same species from which the quiescent cell is isolated. The reconstructed oocyte is then cultured such that it develops to morula or blastocyte and then transferred to pseudopregnant female foster animal. The offspring borne of this female foster animal will be a clone of the animal from which the cell (e g., the somatic cell) is isolated.  
       [0225] Pharmaceutical Compositions  
       [0226] The NOVX nucleic acid molecules, NOVX proteins, and anti-NOVX antibodies (also referred to herein as “active compounds”) of the invention, and derivatives, fragments, analogs and homologs thereof, can be incorporated into pharmaceutical compositions suitable for administration. Such compositions typically comprise the nucleic acid molecule, protein, or antibody and a pharmaceutically acceptable carrier. As used herein, “pharmaceutically acceptable carrier” is intended to include any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like, compatible with pharmaceutical administration. Suitable carriers arc described in the most recent edition of Remington&#39;s Pharmaceutical Sciences, a standard reference text in the field, which is incorporated herein by reference. Preferred examples of such carriers or diluents include, but are not limited to, water, saline, finger&#39;s solutions, dextrose solution, and 5% human serum albumin. Liposomes and non-aqueous vehicles such as fixed oils may also be used. The use of such media and agents for pharmaceutically active substances is well known in the art. Except insofar as any conventional media or agent is incompatible with the active compound, use thereof in the compositions is contemplated. Supplementary active compounds can also be incorporated into the compositions.  
       [0227] A pharmaceutical composition of the invention is formulated to be compatible with its intended route of administration. Examples of routes of administration include parenteral, e.g., intravenous, intradermal, subcutaneous, oral (e.g., inhalation), transdermal (i e, topical), transmucosal, and rectal administration. Solutions or suspensions used for parenteral, intradermal, or subcutaneous application can include the following components: a sterile diluent such as water for injection, saline solution, fixed oils, polyethylene glycols, glycerine, propylene glycol or other synthetic solvents; antibacterial agents such as benzyl alcohol or methyl parabens; antioxidants such as ascorbic acid or sodium bisulfite; chelating agents such as ethylenediaminetetraacetic acid (EDTA); buffers such as acetates, citrates or phosphates, and agents for the adjustment of tonicity such as sodium chloride or dextrose. The pH can be adjusted with acids or bases, such as hydrochloric acid or sodium hydroxide. She parenteral preparation can be enclosed in ampoules, disposable syringes or multiple dose vials made of glass or plastic.  
       [0228] Pharmaceutical compositions suitable for injectable use include sterile aqueous solutions (where water soluble) or dispersions and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersion. For intravenous administration, suitable carriers include physiological saline, bacteriostatic water, Cremophior EL™ (BASF, Parsippany, N.J.) or phosphate buffered saline (PBS). In all cases, the composition must be sterile and should be fluid to the extent that easy syringeability exists. It must be stable under the conditions of manufacture and storage and must be preserved against the contaminating action of microorganisms such as bacteria and fungi. The carrier can be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), and suitable mixtures thereof. The proper fluidity can be maintained, for example, by the use of a coating such as lecithin, by the maintenance of the required particle size in the case of dispersion and by the use of surfactants. Prevention of the action of microorganisms can be achieved by various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, ascorbic acid, thimerosal, and the like. In many cases, it will be preferable to include isotonic agents, for example, sugars, polyalcohols such as manitol, sorbitol, sodium chloride in the composition. Prolonged absorption of the injectable compositions can be brought about by including in the composition an agent which delays absorption, for example, aluminum monostearate and gelatin.  
       [0229] Sterile injectable solutions can be prepared by incorporating the active compound (e g., a NOVX protein or anti-NOVX antibody) in the required amount in an appropriate solvent with one or a combination of ingredients enumerated above, as required, followed by filtered sterilization. Generally, dispersions are prepared by incorporating the active compound into a sterile vehicle that contains a basic dispersion medium and the required other ingredients from those enumerated above. In the case of sterile powders for the preparation of sterile injectable solutions, methods of preparation are vacuum drying and freeze-drying that yields a powder of the active ingredient plus any additional desired ingredient from a previously sterile-filtered solution thereof.  
       [0230] Oral compositions generally include an inert diluent or an edible carrier. They can be enclosed in gelatin capsules or compressed into tablets. For the purpose of oral therapeutic administration, the active compound can be incorporated with excipients and used in the form of tablets, troches, or capsules. Oral compositions can also be prepared using a fluid carrier for use as a mouthwash, wherein the compound in the fluid carrier is applied orally and swished and expectorated or swallowed. Pharmaceutically compatible binding agents, and/or adjuvant materials call be included as part of the composition. The tablets, pills, capsules, troches and the like can contain any of the following ingredients, or compounds of a similar nature: a binder such as microcrystalline cellulose, gum tragacanith or gelatin; an excipient such as starch or lactose, a disintegrating agent such as alginic acid, Primogel, or corn starch; a lubricant such as magnesium stearate or Sterotes; a glidant such as colloidal silicon dioxide; a sweetening agent such as sucrose or saccharin; or a flavoring agent such as peppermint, methyl salicylate, or orange flavoring.  
       [0231] For administration by inhalation, the compounds are delivered in the form of an aerosol spray from pressured container or dispenser which contains a suitable propellant, e.g., a gas such as carbon dioxide, or a nebulizer.  
       [0232] Systemic administration can also be by transmucosal or transdermal means. For transmucosal or transdermal administration, penetrants appropriate to the barrier to be permeated are used in the formulation. Such penetrants are generally known in the art, and include, for example, for transmucosal administration, detergents, bile salts, and fusidic acid derivatives. Transmucosal administration can be accomplished through the use of nasal sprays or suppositories. For transdermal administration, the active compounds are formulated into ointments, salves, gels, or creams as generally known in the art.  
       [0233] The compounds can also be prepared in the form of suppositories (e g., with conventional suppository bases such as cocoa butter and other glycerides) or retention enemas for rectal delivery.  
       [0234] In one embodiment, the active compounds are prepared with carriers that will protect the compound against rapid elimination from the body, such as a controlled release formulation, including implants and microencapsulated delivery systems. Biodegradable, biocompatible polymers can be used, such as ethylene vinyl acetate, polyanhydrides, polyglycolic acid, collagen, polyorthoesters, and polylactic acid. Methods for preparation of such formulations will be apparent to those skilled in the art. The materials can also be obtained commercially from Alza Corporation and Nova Pharmaceuticals, Inc. Liposomal suspensions (including liposomes targeted to infected cells with monoclonal antibodies to viral antigens) can also be used as pharmaceutically acceptable carriers. These can be prepared according to methods known to those skilled in the art, for example, as described in U.S. Pat. No. 4,522,811.  
       [0235] It is especially advantageous to formulate oral or parenteral compositions in dosage unit form for ease of administration and uniformity of dosage. Dosage unit form as used herein refers to physically discrete units suited as unitary dosages for the subject to be treated; each unit containing a predetermined quantity of active compound calculated to produce the desired therapeutic effect in association with the required pharmaceutical carrier. The specification for the dosage unit forms of the invention are dictated by and directly dependent on the unique characteristics of the active compound and the particular therapeutic effect to be achieved, and the limitations inherent in the art of compounding such an active compound for the treatment of individuals.  
       [0236] The nucleic acid molecules of the invention can be inserted into vectors and used as gene therapy vectors. Gene therapy vectors can be delivered to a subject by, for example, intravenous injection, local administration (see, e.g., U.S. Pat. No. 5,328,470) or by stereotactic injection (see, e.g., Chen, et al., 1994.  Proc. Natl. Acad. Sci. USA  91: 3054-3057). The pharmaceutical preparation of the gene therapy vector can include the gene therapy vector in an acceptable diluent, or can comprise a slow release matrix in which the gene delivery vehicle is imbedded. Alternatively, where the complete gene delivery vector can be produced intact from recombinant cells, e.g., retroviral vectors, the pharmaceutical preparation can include one or more cells that produce the gene delivery system.  
       [0237] The pharmaceutical compositions can be included in a container, pack, or dispenser together with instructions for administration.  
       [0238] Screening and Detection Methods  
       [0239] The isolated nucleic acid molecules of the invention can be used to express NOVX protein (e.g., via a recombinant expression vector in a host cell in gene therapy applications), to detect NOVX mRNA (e.g., in a biological sample) or a genetic lesion in a NOVX gene, and to modulate NOVX activity, as described further, below. In addition, the NOVX proteins can be used to screen drugs or compounds that modulate the NOVX protein activity or expression as well as to treat disorders characterized by insufficient or excessive production of NOVX protein or production of NOVX protein forms that have decreased or aberrant activity compared to NOVX wild-type protein (e.g.; diabetes (regulates insulin release); obesity (binds and transport lipids); metabolic disturbances associated with obesity, the metabolic syndrome X as well as anorexia and wasting disorders associated with chronic diseases and various cancers, and infectious disease(possesses anti-microbial activity) and the various dyslipidemias. In addition, the anti-NOVX antibodies of the invention can be used to detect and isolate NOVX proteins and modulate NOVX activity. In yet a further aspect, the invention can be used in methods to influence appetite, absorption of nutrients and the disposition of metabolic substrates in both a positive and negative fashion.  
       [0240] The invention further pertains to novel agents identified by the screening assays described herein and uses thereof for treatments as described, supra.  
       [0241] Screening Assays  
       [0242] The invention provides a method (also referred to herein as a “screening assay”) for identifying modulators, i.e , candidate or test compounds or agents (e.g., peptides, peptidomimetics, small molecules or other drugs) that bind to NOVX proteins or have a stimulatory or inhibitory effect on, e g, NOVX protein expression or NOVX protein activity. The invention also includes compounds identified in the screening assays described herein.  
       [0243] In one embodiment, the invention provides assays for screening candidate or test compounds which bind to or modulate the activity of the membrane-bound form of a NOVX protein or polypeptide or biologically-active portion thereof. The test compounds of the invention can be obtained using any of the numerous approaches in combinatorial library methods known in the art, including: biological libraries; spatially addressable parallel solid phase or solution phase libraries; synthetic library methods requiring deconvolution; the “one-bead one-compound” library method; and synthetic library methods using affinity chromatography selection. The biological library approach is limited to peptide libraries, while the other four approaches are applicable to peptide, non-peptide oligomer or small molecule libraries of compounds. See, e.g., Lam, 1997.  Anticancer Drug Design  12: 145.  
       [0244] A “small molecule” as used herein, is meant to refer to a composition that has a molecular weight of less than about 5 kD and most preferably less than about 4 kD. Small molecules can be, e.g., nucleic acids, peptides, polypeptides, peptidomimetics, carbohydrates, lipids or other organic or inorganic molecules. Libraries of chemical and/or biological mixtures, such as fungal, bacterial, or algal extracts, are known in the art and can be screened with any of the assays of the invention.  
       [0245] Examples of methods for the synthesis of molecular libraries can be found in the art, for example in: DeWitt, et al., 1993.  Proc. Natl. Acad. Sci. U.S.A.  90: 6909; Erb, et al., 1994.  Proc. Natl. Acad. Sci. U.S.A.  91: 11422; Zuckermann, et al., 1994.  J. Med. Chem.  37: 2678; Cho, et al., 1993.  Science  261: 1303; Carrell, et al., 1994.  Angew. Chem. Int. Ed Engl  33: 2059; Carell, et al., 1994.  Angew. Chem. Int. Ed. Engl.  33: 2061; and Gallop, et al., 1994.  J. Med. Chem.  37: 1233.  
       [0246] Libraries of compounds may be presented in solution (e.g, Houghten, 1992.  Biotechniques  13: 412-421), or on beads (Lam, 1991.  Nature  354: 82-84), on chips (Fodor, 1993.  Nature  364: 555-556), bacteria (Ladner, U.S. Pat. No. 5,223,409), spores (Ladner, U.S. Pat. No. 5,233,409), plasmids (Cull, et al., 1992.  Proc Natl Acad. Sci. USA  89: 1865-1869) or on phage (Scott and Smith, 1990.  Science  249: 386-390; Devlin, 1990.  Science  249: 404-406; Cwirla, et al., 1990.  Proc. Natl. Acad. Sci. USA.  87: 6378-6382; Felici, 1991.  J. Mol. Biol.  222: 301-310; Ladner, U.S. Pat. No. 5,233,409.).  
       [0247] In one embodiment, an assay is a cell-based assay in which a cell which expresses a membrane-bound form of NOVX protein, or a biologically-active portion thereof, on the cell surface is contacted with a test compound and the ability of the test compound to bind to a NOVX protein determined. The cell, for example, can of mammalian origin or a yeast cell. Determining the ability of the test compound to bind to the NOVX protein can be accomplished, for example, by coupling the test compound with a radioisotope or enzymatic label such that binding of the test compound to the NOVX protein or biologically-active portion thereof can be determined by detecting the labeled compound in a complex. For example, test compounds can be labeled with  125 I,  35 S,  14 C, or  3 H, either directly or indirectly, and the radioisotope detected by direct counting of radioemission or by scintillation counting. Alternatively, test compounds can be enzymatically-labeled with, for example, horseradish peroxidase, alkaline phosphatase, or luciferase, and the enzymatic label detected by determination of conversion of an appropriate substrate to product. In one embodiment, the assay comprises contacting a cell which expresses a membrane-bound form of NOVX protein, or a biologically-active portion thereof, on the cell surface with a known compound which binds NOVX to form an assay mixture, contacting the assay mixture with a test compound, and determining the ability of the test compound to interact with a NOVX protein, wherein determining the ability of the test compound to interact with a NOVX protein comprises determining the ability of the test compound to preferentially bind to NOVX protein or a biologically-active portion thereof as compared to the known compound.  
       [0248] In another embodiment, an assay is a cell-based assay comprising contacting a cell expressing a membrane-bound form of NOVX protein, or a biologically-active portion thereof, on the cell surface with a test compound and determining the ability of the test compound to modulate (e.g., stimulate or inhibit) the activity of the NOVX protein or biologically-active portion thereof. Determining the ability of the test compound to modulate the activity of NOVX or a biologically-active portion thereof can be accomplished, for example, by determining the ability of the NOVX protein to bind to or interact with a NOVX target molecule. As used herein, a “target molecule” is a molecule with which a NOVX protein binds or interacts in nature, for example, a molecule on the surface of a cell which expresses a NOVX interacting protein, a molecule on the surface of a second cell, a molecule in the extracellular milieu, a molecule associated with the internal surface of a cell membrane or a cytoplasmic molecule. A NOVX target molecule can be a non-NOVX molecule or a NOVX protein or polypeptide of the invention. In one embodiment, a NOVX target molecule is a component of a signal transduction pathway that facilitates transduction of an extracellular signal (e.g a signal generated by binding of a compound to a membrane-bound NOVX molecule) through the cell membrane and into the cell. The target, for example, can be a second intercellular protein that has catalytic activity or a protein that facilitates the association of downstream signaling molecules with NOVX.  
       [0249] Determining the ability of the NOVX protein to bind to or interact with a NOVX target molecule can be accomplished by one of the methods described above for determining direct binding. In one embodiment, determining the ability of the NOVX protein to bind to or interact with a NOVX target molecule can be accomplished by determining the activity of the target molecule. For example, the activity of the target molecule can be determined by detecting induction of a cellular second messenger of the target (i.e intracellular Ca 2+ , diacylglycerol, IP 3 , etc.), detecting catalytic/enzymatic activity of the target an appropriate substrate, detecting the induction of a reporter gene (comprising a NOVX-responsive regulatory element operatively linked to a nucleic acid encoding a detectable marker, e g., luciferase), or detecting a cellular response, for example, cell survival, cellular differentiation, or cell proliferation.  
       [0250] In yet another embodiment, an assay of the invention is a cell-free assay comprising contacting a NOVX protein or biologically-active portion thereof with a test compound and determining the ability of the test compound to bind to the NOVX protein or biologically-active portion thereof. Binding of the test compound to the NOVX protein can be determined either directly or indirectly as described above. In one such embodiment, the assay comprises contacting the NOVX protein or biologically-active portion thereof with a known compound which binds NOVX to form an assay mixture, contacting the assay mixture with a test compound, and determining the ability of the test compound to interact with a NOVX protein, wherein determining the ability of the test compound to interact with a NOVX protein comprises determining the ability of the test compound to preferentially bind to NOVX or biologically-active portion thereof as compared to the known compound.  
       [0251] In still another embodiment, an assay is a cell-free assay comprising contacting NOVX protein or biologically-active portion thereof with a test compound and determining the ability of the test compound to modulate (e g stimulate or inhibit) the activity of the NOVX protein or biologically-active portion thereof. Determining the ability of the test compound to modulate the activity of NOVX can be accomplished, for example, by determining the ability of the NOVX protein to bind to a NOVX target molecule by one of the methods described above for determining direct binding. In an alternative embodiment, determining the ability of the test compound to modulate the activity of NOVX protein can be accomplished by determining the ability of the NOVX protein further modulate a NOVX target molecule. For example, the catalytic/enzymatic activity of the target molecule on an appropriate substrate can be determined as described, supra.  
       [0252] In yet another embodiment, the cell-free assay comprises contacting the NOVX protein or biologically-active portion thereof with a known compound which binds NOVX protein to form an assay mixture, contacting the assay mixture with a test compound, and determining the ability of the test compound to interact with a NOVX protein, wherein determining the ability of the test compound to interact with a NOVX protein comprises determining the ability of the NOVX protein to preferentially bind to or modulate the activity of a NOVX target molecule.  
       [0253] The cell-free assays of the invention are amenable to use of both the soluble form or the membrane-bound form of NOVX protein. In the case of cell-free assays comprising the membrane-bound form of NOVX protein, it may be desirable to utilize a solubilizing agent such that the membrane-bound form of NOVX protein is maintained in solution. Examples of such solubilizing agents include non-ionic detergents such as n-octylglucoside, n-dodecylglucoside, n-dodecylmaltoside, octanoyl-N-methylglucamide, decanoyl-N-methylglucamide, Triton® X-100, Triton® X-114, Thesit®, Isotridecypoly(ethylene glycol ether) n , N-dodecyl-N,N-dimethyl-3-ammonio-1-propane sulfonate, 3-(3-cholamidopropyl)dimethylamminiol-1-propane sulfonate (CHAPS), or 3-(3-cholamidopropyl)dimethylamminiol-2-hydroxy-1-propane sulfonate (CHAPSO).  
       [0254] In more than one embodiment of the above assay methods of the invention, it may be desirable to immobilize either NOVX protein or its target molecule to facilitate separation of complexed from uncomplexed forms of one or both of the proteins, as well as to accommodate automation of the assay. Binding of a test compound to NOVX protein, or interaction of NOVX protein with a target molecule in the presence and absence of a candidate compound, can be accomplished in any vessel suitable for containing the reactants. Examples of such vessels include microtiter plates, test tubes, and micro-centrifuge tubes. In one embodiment, a fusion protein can be provided that adds a domain that allows one or both of the proteins to be bound to a matrix. For example, GST-NOVX fusion proteins or GST-target fusion proteins can be adsorbed onto glutathione sepharose beads (Sigma Chemical, St. Louis, Mo.) or glutathione derivatized microtiter plates, that are then combined with the test compound or the test compound and either the non-adsorbed target protein or NOVX protein, and the mixture is incubated under conditions conducive to complex formation (e.g., at physiological conditions for salt and pH). Following incubation, the beads or microtiter plate wells are washed to remove any unbound components, the matrix immobilized in the case of beads, complex determined either directly or indirectly, for example, as described, supra. Alternatively, the complexes can be dissociated from the matrix, and the level of NOVX protein binding or activity determined using standard techniques.  
       [0255] Other techniques for immobilizing proteins on matrices can also be used in the screening assays of the invention. For example, either the NOVX protein or its target molecule can be immobilized utilizing conjugation of biotin and streptavidin. Biotinylated NOVX protein or target molecules can be prepared from biotin-NHS (N-hydroxy-succinimide) using techniques well-known within the art (e.g., biotinylation kit, Pierce Chemicals, Rockford, Ill.), and immobilized in the wells of streptavidin-coated 96 well plates (Pierce Chemical). Alternatively, antibodies reactive with NOVX protein or target molecules, but which do not interfere with binding of the NOVX protein to its target molecule, can be derivatized to the wells of the plate, and unbound target or NOVX protein trapped in the wells by antibody conjugation. Methods for detecting such complexes, in addition to those described above for the GST-immobilized complexes, include immunodetection of complexes using antibodies reactive with the NOVX protein or target molecule, as well as enzyme-linked assays that rely on detecting all enzymatic activity associated with the NOVX protein or target molecule.  
       [0256] In another embodiment, modulators of NOVX protein expression are identified in a method wherein a cell is contacted with a candidate compound and the expression of NOVX mRNA or protein in the cell is determined. The level of expression of NOVX mRNA or protein in the presence of the candidate compound is compared to the level of expression of NOVX mRNA or protein in the absence of the candidate compound. The candidate compound can then be identified as a modulator of NOVX mRNA or protein expression based upon this comparison. For example, when expression of NOVX mRNA or protein is greater (i.e., statistically significantly greater) in the presence of the candidate compound than in its absence, the candidate compound is identified as a stimulator of NOVX mRNA or protein expression. Alternatively, when expression of NOVX mRNA or protein is less (statistically significantly less) in the presence of the candidate compound than in its absence, the candidate compound is identified as an inhibitor of NOVX mRNA or protein expression. The level of NOVX mRNA or protein expression in the cells can be determined by methods described herein for detecting NOVX mRNA or protein.  
       [0257] In yet another aspect of the invention, the NOVX proteins can be used as “bait proteins” in a two-hybrid assay or three hybrid assay (see, e.g., U.S. Pat. No. 5,283,317; Zervos, et al., 1993.  Cell  72: 223-232; Madura, et al., 1993.  J. Biol. Chem.  268: 12046-12054; Bartel, et al., 1993.  Biotechniques  14: 920-924; Iwabuchi, et al., 1993.  Oncogene  8: 1693-1696; and Brent WO 94/10300), to identify other proteins that bind to or interact with NOVX (“NOVX-binding proteins” or “NOVX-bp”) and modulate NOVX activity. Such NOVX-binding proteins are also involved in the propagation of signals by the NOVX proteins as, for example, upstream or downstream elements of the NOVX pathway.  
       [0258] The two-hybrid system is based on the modular nature of most transcription factors, which consist of separable DNA-binding and activation domains. Briefly, the assay utilizes two different DNA constructs. In one construct, the gene that codes for NOVX is fused to a gene encoding the DNA binding domain of a known transcription factor (e.g., GAL-4). In the other construct, a DNA sequence, from a library of DNA sequences, that encodes an unidentified protein (“prey” or “sample”) is fused to a gene that codes for the activation domain of the known transcription factor. If the “bait” and the “prey” proteins are able to interact, in vivo, forming a NOVX-dependent complex, the DNA-binding and activation domains of the transcription factor are brought into close proximity. This proximity allows transcription of a reporter gene (e g , LacZ) that is operably linked to a transcriptional regulatory site responsive to the transcription factor. Expression of the reporter gene can be detected and cell colonies containing the functional transcription factor can be isolated and used to obtain the cloned gene that encodes the protein which interacts with NOVX.  
       [0259] The invention further pertains to novel agents identified by the aforementioned screening assays and uses thereof for treatments as described herein.  
       [0260] Detection Assays  
       [0261] Portions or fragments of the cDNA sequences identified herein (and the corresponding complete gene sequences) can be used in numerous ways as polynucleotide reagents. By way of example, and not of limitation, these sequences can be used to: (i) map their respective genes on a chromosome; and, thus, locate gene regions associated with genetic disease; (ii) identify an individual from a minute biological sample (tissue typing); and (iii) aid in forensic identification of a biological sample. Some of these applications arc described in the subsections, below.  
       [0262] Chromosome Mapping  
       [0263] Once the sequence (or a portion of the sequence) of a gene has been isolated, this sequence can be used to map the location of the gene on a chromosome. This process is called chromosome mapping. Accordingly, portions or fragments of the NOVX sequences of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or fragments or derivatives thereof, can be used to map the location of the NOVX genes, respectively, on a chromosome. The mapping of the NOVX sequences to chromosomes is an important first step in correlating these sequences with genes associated with disease.  
       [0264] Briefly, NOVX genes can be mapped to chromosomes by preparing PCR primers (preferably 15-25 bp in length) from the NOVX sequences. Computer analysis of the NOVX, sequences can be used to rapidly select primers that do not span more than one exon in the genomic DNA, thus complicating the amplification process. These primers can then be used for PCR screening of somatic cell hybrids containing individual human chromosomes. Only those hybrids containing the human gene corresponding to the NOVX sequences will yield an amplified fragment.  
       [0265] Somatic cell hybrids are prepared by fusing somatic cells from different mammals (e.g., human and mouse cells). As hybrids of human and mouse cells grow and divide, they gradually lose human chromosomes in random order, but retain the mouse chromosomes. By using media in which mouse cells cannot grow, because they lack a particular enzyme, but in which human cells can, the one human chromosome that contains the gene encoding the needed enzyme will be retained. By using various media, panels of hybrid cell lines can be established. Each cell line in a panel contains either a single human chromosome or a small number of human chromosomes, and a full set of mouse chromosomes, allowing easy mapping of individual genes to specific human chromosomes. See, e.g., D&#39;Eustachio, et al., 1983.  Science  220: 919-924. Somatic cell hybrids containing only fragments of human chromosomes can also be produced by using human chromosomes with translocations and deletions.  
       [0266] PCR mapping of somatic cell hybrids is a rapid procedure for assigning a particular sequence to a particular chromosome. Three or more sequences can be assigned per day using a single thermal cycler. Using the NOVX sequences to design oligonucleotide primers, sub-localization can be achieved with panels of fragments from specific chromosomes.  
       [0267] Fluorescence in situ hybridization (FISH) of a DNA sequence to a metaphase chromosomal spread can further be used to provide a precise chromosomal location in one step. Chromosome spreads can be made using cells whose division has been blocked in metaphase by a chemical like colcemid that disrupts the mitotic spindle. The chromosomes can be treated briefly with trypsin, and then stained with Giemsa. A pattern of light and dark bands develops on each chromosome, so that the chromosomes can be identified individually. The FISH technique can be used with a DNA sequence as short as 500 or 600 bases. However, clones larger than 1,000 bases have a higher likelihood of binding to a unique chromosomal location with sufficient signal intensity for simple detection. Preferably 1,000 bases, and more preferably 2,000 bases, will suffice to get good results at a reasonable amount of time. For a review of this technique, see, Verma, et al., HUMAN CHROMOSOMES: A MANUAL OF BASIC TECHNIQUES (Pergamon Press, New York 1988).  
       [0268] Reagents for chromosome mapping can be used individually to mark a single chromosome or a single site on that chromosome, or panels of reagents can be used for marking multiple sites and/or multiple chromosomes. Reagents corresponding to noncoding regions of the genes actually are preferred for mapping purposes. Coding sequences are more likely to be conserved within gene families, thus increasing the chance of cross hybridizations during chromosomal mapping.  
       [0269] Once a sequence has been mapped to a precise chromosomal location, the physical position of the sequence on the chromosome can be correlated with genetic map data. Such data are found, e.g., in McKusick, MENDELIAN INHERITANCE IN MAN, available on-line through Johns Hopkins University Welch Medical Library). The relationship between genes and disease, mapped to the same chromosomal region, can then be identified through linkage analysis (co-inheritance of physically adjacent genes), described in, e g, Egeland, et al., 1987.  Nature,  325: 783-787.  
       [0270] Moreover, differences in the DNA sequences between individuals affected and unaffected with a disease associated with the NOVX gene, can be determined. If a mutation is observed in some or all of the affected individuals but not in any unaffected individuals, then the mutation is likely to be the causative agent of the particular disease.  
       [0271] Comparison of affected and unaffected individuals generally involves first looking for structural alterations in the chromosomes, such as deletions or translocations that are visible from chromosome spreads or detectable using PCR based on that DNA sequence. Ultimately, complete sequencing of genes from several individuals can be performed to confirm the presence of a mutation and to distinguish mutations from polymorphisms.  
       [0272] Tissue Typing  
       [0273] The NOVX sequences of the invention can also be used to identify individuals from minute biological samples. In this technique, an individual&#39;s genomic DNA is digested with one or more restriction enzymes, and probed on a Southern blot to yield unique bands for identification. The sequences of the invention are useful as additional DNA markers for RFLP (“restriction fragment length polymorphisms,” described in U.S. Pat. No. 5,272,057).  
       [0274] Furthermore, the sequences of the invention can be used to provide an alternative technique that determines the actual base-by-base DNA sequence of selected portions of an individual&#39;s genome. Thus, the NOVX sequences described herein can be used to prepare two PCR primers from the 5′- and 3′-termini of the sequences. These primers can then be used to amplify an individual&#39;s DNA and subsequently sequence it.  
       [0275] Panels of corresponding DNA sequences from individuals, prepared in this manner, can provide unique individual identifications, as each individual will have a unique set of such DNA sequences due to allelic differences. The sequences of the invention can be used to obtain such identification sequences from individuals and from tissue. The NOVX sequences of the invention uniquely represent portions of the human genome. Allelic variation occurs to some degree in the coding regions of these sequences, and to a greater degree in the noncoding regions. It is estimated that allelic variation between individual humans occurs with a frequency of about once per each 500 bases. Much of the allelic variation is due to single nucleotide polymorphisms (SNPs), which include restriction fragment length polymorphisms (RFLPs).  
       [0276] Each of the sequences described herein can, to some degree, be used as a standard against which DNA from an individual can be compared for identification purposes. Because greater numbers of polymorphisms occur in the noncoding regions, fewer sequences are necessary to differentiate individuals. The noncoding sequences can comfortably provide positive individual identification with a panel of perhaps 10 to 1,000 primers that each yield a noncoding amplified sequence of 100 bases. If coding sequences, such as those of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, are used, a more appropriate number of primers for positive individual identification would be 500-2,000.  
       [0277] Predictive Medicine  
       [0278] The invention also pertains to the field of predictive medicine in which diagnostic assays, prognostic assays, pharmacogenomics, and monitoring clinical trials are used for prognostic (predictive) purposes to thereby treat an individual prophylactically. Accordingly, one aspect of the invention relates to diagnostic assays for determining NOVX protein and/or nucleic acid expression as well as NOVX activity, in the context of a biological sample (e g., blood, serum, cells, tissue) to thereby determine whether an individual is afflicted with a disease or disorder, or is at risk of developing a disorder, associated with aberrant NOVX expression or activity. The disorders include metabolic disorders, diabetes, obesity, infectious disease, anorexia, cancer-associated cachexia, cancer, neurodegenerative disorders, Alzheimer&#39;s Disease, Parkinson&#39;s Disorder, immune disorders, and hematopoietic disorders, and the various dyslipidemias, metabolic disturbances associated with obesity, the metabolic syndrome X and wasting disorders associated with chronic diseases and various cancers. The invention also provides for prognostic (or predictive) assays for determining whether an individual is at risk of developing a disorder associated with NOVX protein, nucleic acid expression or activity. For example, mutations in a NOVX gene can be assayed in a biological sample. Such assays can be used for prognostic or predictive purpose to thereby prophylactically treat an individual prior to the onset of a disorder characterized by or associated with NOVX protein, nucleic acid expression, or biological activity.  
       [0279] Another aspect of the invention provides methods for determining, NOVX protein, nucleic acid expression or activity in an individual to thereby select appropriate therapeutic or prophylactic agents for that individual (referred to herein as “pharmacogenomics”). Pharmacogenomics allows for the selection of agents (e.g., drugs) for therapeutic or prophylactic treatment of an individual based on the genotype of the individual (e.g., the genotype of the individual examined to determine the ability of the individual to respond to a particular agent.)  
       [0280] Yet another aspect of the invention pertains to monitoring the influence of agents (e.g., drugs, compounds) on the expression or activity of NOVX in clinical trials.  
       [0281] These and other agents are described in further detail in the following sections.  
       [0282] Diagnostic Assays  
       [0283] An exemplary method for detecting the presence or absence of NOVX in a biological sample involves obtaining a biological sample from a test subject and contacting the biological sample with a compound or an agent capable of detecting NOVX protein or nucleic acid (e.g., mRNA, genomic DNA) that encodes NOVX protein such that the presence of NOVX is detected in the biological sample. An agent for detecting NOVX mRNA or genomic DNA is a labeled nucleic acid probe capable of hybridizing to NOVX mRNA or genomic DNA. The nucleic acid probe can be, for example, a full-length NOVX nucleic acid, such as the nucleic acid of SEQ ID NO: 2n−1, wherein n is an integer between 1 and 102, or a portion thereof such as an oligonucleotide of at least 15, 30, 50, 100, 250 or 500 nucleotides in length and sufficient to specifically hybridize under stringent conditions to NOVX mRNA or genomic DNA. Other suitable probes for use in the diagnostic assays of the invention are described herein.  
       [0284] An agent for detecting NOVX protein is an antibody capable of binding to NOVX protein, preferably an antibody with a detectable label. Antibodies can be polyclonal, or more preferably, monoclonal. An intact antibody, or a fragment thereof (e.g., Fab or F(ab′) 2 ) can be used. The term “labeled”, with regard to the probe or antibody, is intended to encompass direct labeling of the probe or antibody by coupling (i e , physically linking) a detectable substance to the probe or antibody, as well as indirect labeling of the probe or antibody by reactivity with another reagent that is directly labeled. Examples of indirect labeling include detection of a primary antibody using, a fluorescently-labeled secondary antibody and end-labeling of a DNA probe with biotin such that it can be detected with fluorescently-labeled streptavidin. The term “biological sample” is intended to include tissues, cells and biological fluids isolated from a subject, as well as tissues, cells and fluids present within a subject. That is, the detection method of the invention can be used to detect NOVX mRNA, protein, or genomic DNA in a biological sample in vitro as well as in vivo. For example, in vitro techniques for detection of NOVX mRNA include Northern hybridizations and in situ hybridizations. In vitro techniques for detection of NOVX protein include enzyme linked immunosorbent assays (ELISAs), Western blots, immunoprecipitations, and immunofluorescence. In vitro techniques for detection of NOVX genomic DNA include Southern hybridizations. Furthermore, in vivo techniques for detection of NOVX protein include introducing into a subject a labeled anti-NOVX antibody. For example, the antibody can be labeled with a radioactive marker whose presence and location in a subject can be detected by standard imaging techniques.  
       [0285] In one embodiment, the biological sample contains protein molecules from the test subject. Alternatively, the biological sample can contain mRNA molecules from the test subject or genomic DNA molecules from the test subject. A preferred biological sample is a peripheral blood leukocyte sample isolated by conventional means from a subject.  
       [0286] In another embodiment, the methods further involve obtaining a control biological sample from a control subject, contacting the control sample with a compound or agent capable of detecting NOVX protein, mRNA, or genomic DNA, such that the presence of NOVX protein, mRNA or genomic DNA is detected in the biological sample, and comparing the presence of NOVX protein, mRNA or genomic DNA in the control sample with the presence of NOVX protein, mRNA or genomic DNA in the test sample.  
       [0287] The invention also encompasses kits for detecting the presence of NOVX in a biological sample. For example, the kit can comprise: a labeled compound or agent capable of detecting NOVX protein or mRNA in a biological sample; means for determining the amount of NOVX in the sample; and means for comparing the amount of NOVX in the sample with a standard. The compound or agent can be packaged in a suitable container. The kit can further comprise instructions for using the kit to detect NOVX protein or nucleic acid.  
       [0288] Prognostic Assays  
       [0289] The diagnostic methods described herein can furthermore be utilized to identify subjects having or at risk of developing a disease or disorder associated with aberrant NOVX expression or activity. For example, the assays described herein, such as the preceding diagnostic assays or the following assays, can be utilized to identify a subject having or at risk of developing a disorder associated with NOVX protein, nucleic acid expression or activity. Alternatively, the prognostic assays can be utilized to identify a subject having or at risk for developing a disease or disorder. Thus, the invention provides a method for identifying a disease or disorder associated with aberrant NOVX expression or activity in which a test sample is obtained from a subject and NOVX protein or nucleic acid (e.g., mRNA, genomic DNA) is detected, wherein the presence of NOVX protein or nucleic acid is diagnostic for a subject having or at risk of developing a disease or disorder associated with aberrant NOVX expression or activity. As used herein, a “test sample” refers to a biological sample obtained from a subject of interest. For example, a test sample can be a biological fluid (e.g., serum), cell sample, or tissue.  
       [0290] Furthermore, the prognostic assays described herein can be used to determine whether a subject can be administered an agent (e g., an agonist, antagonist, peptidomimetic, protein, peptide, nucleic acid, small molecule, or other drug candidate) to treat a disease or disorder associated with aberrant NOVX expression or activity. For example, such methods can be used to determine whether a subject can be effectively treated with an agent for a disorder. Thus, the invention provides methods for determining whether a subject can be effectively treated with an agent for a disorder associated with aberrant NOVX expression or activity in which a test sample is obtained and NOVX protein or nucleic acid is detected (e g., wherein the presence of NOVX protein or nucleic acid is diagnostic for a subject that can be administered the agent to treat a disorder associated with aberrant NOVX expression or activity).  
       [0291] The methods of the invention can also be used to detect genetic lesions in a NOVX gene, thereby determining if a subject with the lesioned gene is at risk for a disorder characterized by aberrant cell proliferation and/or differentiation. In various embodiments, the methods include detecting, in a sample of cells from the subject, the presence or absence of a genetic lesion characterized by at least one of an alteration affecting the integrity of a gene encoding a NOVX-protein, or the misexpression of the NOVX gene. For example, such genetic lesions can be detected by ascertaining the existence of at least one of: (i) a deletion of one or more nucleotides from a NOVX gene; (ii) an addition of one or more nucleotides to a NOVX gene; (iii) a substitution of one or more nucleotides of a NOVX gene, (iv) a chromosomal rearrangement of a NOVX gene; (v) an alteration in the level of a messenger RNA transcript of a NOVX gene (vi) aberrant modification of a NOVX gene, such as of the methylation pattern of the genomic DNA, (vii) the presence of a non-wild-type splicing pattern of a messenger RNA transcript of a NOVX gene, (viii) a non-wild-type level of a NOVX protein, (ix) allelic loss of a NOVX gene, and (x) inappropriate post-translational modification of a NOVX protein. As described herein, there are a large number of assay techniques known in the art which can be used for detecting lesions in a NOVX gene. A preferred biological sample is a peripheral blood leukocyte sample isolated by conventional means from a subject. However, any biological sample containing nucleated cells may be used, including, for example, buccal mucosal cells.  
       [0292] In certain embodiments, detection of the lesion involves the use of a probe/primer in a polymerase chain reaction (PCR) (see, e.g., U.S. Pat. Nos. 4,683,195 and 4,683,202), such as anchor PCR or RACE PCR, or, alternatively, in a ligation chain reaction (LCR) (see, e.g., Landegran, et al., 1988.  Science  241: 1077-1080; and Nakazawa, et al., 1994.  Proc Natl. Acad. Sci. USA  91: 360-364), the latter of which can be particularly useful for detecting point mutations in the NOVX-gene (see, Abravaya, et al., 1995.  Nacl. Acids Res.  23: 675-682). This method can include the steps of collecting a sample of cells from a patient, isolating nucleic acid (e.g., genomic, mRNA or both) from the cells of the sample, contacting the nucleic acid sample with one or more primers that specifically hybridize to a NOVX gene under conditions such that hybridization and amplification of the NOVX gene (if present) occurs, and detecting the presence or absence of an amplification product, or detecting the size of the amplification product and comparing the length to a control sample. It is anticipated that PCR and/or LCR may be desirable to use as a preliminary amplification step in conjunction with any of the techniques used for detecting mutations described herein.  
       [0293] Alternative amplification methods include: self sustained sequence replication (see, Guatelli, et al., 1990.  Proc. Natl. Acad. Sci. USA  87: 1874-1878), transcriptional amplification system (see, Kwoh, et al., 1989.  Proc. Natl. Acad. Sci. USA  86: 1173-1177); Qβ Replicase (see, Lizardi, et al, 1988.  BioTechnology  6: 1197), or any other nucleic acid amplification method, followed by the detection of the amplified molecules using techniques well known to those of skill in the art. These detection schemes are especially useful for the detection of nucleic acid molecules if such molecules are present in very low numbers.  
       [0294] In an alternative embodiment, mutations in a NOVX gene from a sample cell can be identified by alterations in restriction enzyme cleavage patterns. For example, sample and control DNA is isolated, amplified (optionally), digested with one or more restriction endonucleases, and fragment length sizes are determined by gel electrophoresis and compared. Differences in fragment length sizes between sample and control DNA indicates mutations in the sample DNA. Moreover, the use of sequence specific ribozymes (see, e.g., U.S. Pat. No. 5,493,531) can be used to score for the presence of specific mutations by development or loss of a ribozyme cleavage site.  
       [0295] In other embodiments, genetic mutations in NOVX can be identified by hybridizing a sample and control nucleic acids, e.g., DNA or RNA, to high-density arrays containing hundreds or thousands of oligonucleotides probes. See, e.g, Cronin, et al., 1996.  Human Mutation  7: 244-255; Kozal, et al., 1996.  Natl. Med.  2: 753-759. For example, genetic mutations in NOVX can be identified in two dimensional arrays containing light-generated DNA probes as described in Cronin, et al., supra. Briefly, a first hybridization array of probes can be used to scan through long stretches of DNA in a sample and control to identify base changes between the sequences by making linear arrays of sequential overlapping probes. This step allows the identification of point mutations. This is followed by a second hybridization array that allows the characterization of specific mutations by using smaller, specialized probe arrays complementary to all variants or mutations detected. Each mutation array is composed of parallel probe sets, one complementary to the wild-type gene and the other complementary to the mutant gene.  
       [0296] In yet another embodiment, any of a variety of sequencing reactions known in the art can be used to directly sequence the NOVX gene and detect mutations by comparing the sequence of the sample NOVX with the corresponding wild-type (control) sequence. Examples of sequencing reactions include those based on techniques developed by Maxim and Gilbert, 1977.  Proc. Natl. Acad. Sci. USA  74: 560 or Sanger, 1977.  Proc Natl Acad Sci. USA  74: 5463. It is also contemplated that any of a variety of automated sequencing procedures can be utilized when performing the diagnostic assays (see, e g. Naeve, et al., 1995.  Biotechniques  19: 448), including sequencing by mass spectrometry (see, e.g., PCT International Publication No. WO 94/16101; Cohen, et al., 1996.  Adv Chromatography  36: 127-162; and Griffin, et al., 1993.  Appl. Biochem. Biotechnol  38: 147-159).  
       [0297] Other methods for detecting mutations in the NOVX gene include methods in which protection from cleavage agents is used to detect mismatched bases RNA/RNA or RNA/DNA heteroduplexes. See. e g, Myers, et al., 1985.  Science  230: 1242. In general, the art technique of “mismatch cleavage” starts by providing heteroduplexes of formed by hybridizing (labeled) RNA or DNA containing the wild-type NOVX sequence with potentially mutant RNA or DNA obtained from a tissue sample. The double-stranded duplexes are treated with an agent that cleaves single-stranded regions of the duplex such as which will exist due to basepair mismatches between the control and sample strands. For instance, RNA/DNA duplexes can be treated with RNase and DNA/DNA hybrids treated with S 1  nuclease to enzymatically digesting the mismatched regions. In other embodiments, either DNA/DNA or RNA/DNA duplexes can be treated with hydroxylamine or osmium tetroxide and with piperidine in order to digest mismatched regions. After digestion of the mismatched regions, the resulting material is then separated by size on denaturing polyacrylamide gels to determine the site of mutation. See, e.g., Cotton, et al., 1988.  Proc. Natl. Acad. Sci USA  85: 4397; Saleeba, et al., 1992.  Methods Enzymol.  217: 286-295. In an embodiment, the control DNA or RNA can be labeled for detection.  
       [0298] In still another embodiment, the mismatch cleavage reaction employs one or more proteins that recognize mismatched base pairs in double-stranded DNA (so called “DNA mismatch repair” enzymes) in defined systems for detecting and mapping point mutations in NOVX cDNAs obtained from samples of cells. For example, the mutY enzyme of  E. coli  cleaves A at G/A mismatches and the thymidine DNA glycosylase from HeLa cells cleaves T at G/T mismatches. See, e.g., Hsu, et al., 1994.  Carcinogenesis  15: 1657-1662. According to an exemplary embodiment, a probe based on a NOVX sequence, e.g., a wild-type NOVX sequence, is hybridized to a cDNA or other DNA product from a test cell(s). The duplex is treated with a DNA mismatch repair enzyme, and the cleavage products, if any, can be detected from electrophoresis protocols or the like. See, e.g, U.S. Pat. No. 5,459,039.  
       [0299] In other embodiments, alterations in electrophoretic mobility will be used to identify mutations in NOVX genes. For example, single strand conformation polymorphism (SSCP) may be used to detect differences in electrophoretic mobility between mutant and wild type nucleic acids. See, e.g., Orita, et al., 1989.  Proc Natl Acad. Sci USA:  86: 2766; Cotton, 1993.  Mutat. Res.  285: 125-144; Hayashi, 1992.  Genet. Anal. Tech Appl  9: 73-79. Single-stranded DNA fragments of sample and control NOVX nucleic acids will be denatured and allowed to renature. The secondary structure of single-stranded nucleic acids varies according to sequence, the resulting alteration in electrophoretic mobility enables the detection of even a single base chance. The DNA fragments may be labeled or detected with labeled probes. The sensitivity of the assay may be enhanced by using RNA (rather than DNA), in which the secondary structure is more sensitive to a change in sequence. In one embodiment, the subject method utilizes heteroduplex analysis to separate double stranded heteroduplex molecules on the basis of changes in electrophoretic mobility. See, e.g, Keen, et al., 1991.  Trends Genet  7: 5.  
       [0300] In yet another embodiment, the movement of mutant or wild-type fragments in polyacrylamide gels containing a gradient of denaturant is assayed using denaturing gradient gel electrophoresis (DGGE). See, e.g., Myers, et al., 1985.  Nature  313: 495. When DGGE is used as the method of analysis, DNA will be modified to insure that it does not completely denature, for example by adding a GC clamp of approximately 40 bp of high-melting GC-rich DNA by PCR. In a further embodiment, a temperature gradient is used in place of a denaturing gradient to identify differences in the mobility of control and sample DNA. See, e.g., Rosenbaum and Reissner, 1987.  Biophys. Chem.  265: 12753.  
       [0301] Examples of other techniques for detecting point mutations include, but are not limited to, selective oligonucleotide hybridization, selective amplification, or selective primer extension. For example, oligonucleotide primers may be prepared in which the known mutation is placed centrally and then hybridized to target DNA under conditions that permit hybridization only if a perfect match is found. See, e.g., Saiki, et al.. 1986.  Nature  324: 163; Saiki, et al., 1989.  Proc. Natl Acad Sci USA  86: 6230. Such allele specific oligonucleotides are hybridized to PCR amplified target DNA or a number of different mutations when the oligonucleotides are attached to the hybridizing membrane and hybridized with labeled target DNA.  
       [0302] Alternatively, allele specific amplification technology that depends on selective PCR amplification may be used in conjunction with the instant invention. Oligonucleotides used as primers for specific amplification may carry the mutation of interest in the center of the molecule (so that amplification depends on differential hybridization; see, e g, Gibbs, et al., 1989.  Nucl. Acids Res  17: 2437-2448) or at the extreme 3′-terminus of one primer where, under appropriate conditions, mismatch can prevent, or reduce polymerase extension (.see, e.g., Prossner, 1993.  Tibtech  11: 238). In addition it may be desirable to introduce a novel restriction site in the region of the mutation to create cleavage-based detection. See, e g., Gasparini, et al, 1992.  Mol Cell Probes  6: 1. It is anticipated that in certain embodiments amplification may also be performed using Taq ligase for amplification. See, e g., Barany, 1991.  Proc. Natl. Acad. Sci. USA  88: 189. In such cases, ligation will occur only if there is a perfect match at the 3′-terminus of the 5′ sequence, making it possible to detect the presence of a known mutation at a specific site by looking for the presence or absence of amplification.  
       [0303] The methods described herein may be performed, for example, by utilizing pre-packaged diagnostic kits comprising at least one probe nucleic acid or antibody reagent described herein, which may be conveniently used, e g, in clinical settings to diagnose patients exhibiting symptoms or family history of a disease or illness involving a NOVX gene.  
       [0304] Furthermore, any cell type or tissue, preferably peripheral blood leukocytes, in which NOVX is expressed may be utilized in the prognostic assays described herein. However, any biological sample containing nucleated cells may be used, including, for example, buccal mucosal cells.  
       [0305] Pharmacogenomics  
       [0306] Agents, or modulators that have a stimulatory or inhibitory effect on NOVX activity (e.g., NOVX gene expression), as identified by a screening assay described herein can be administered to individuals to treat (prophylactically or therapeutically) disorders. The disorders include but are not limited to, e.g., those diseases, disorders and conditions listed above, and more particularly include those diseases, disorders, or conditions associated with homologs of a NOVX proteins such as those summarized in Table A.  
       [0307] In conjunction with such treatment, the pharmacogenomics (i.e., the study of the relationship between an individual&#39;s genotype and that individual&#39;s response to a foreign compound or drug) of the individual may be considered. Differences in metabolism of therapeutics can lead to severe toxicity or therapeutic failure by altering the relation between dose and blood concentration of the pharmacologically active drug. Thus, the pharmacogenomics of the individual permits the selection of effective agents (e g., drugs) for prophylactic or therapeutic treatments based on a consideration of the individual&#39;s genotype. Such pharmacogenomics can further be used to determine appropriate dosages and therapeutic regimens. Accordingly, the activity of NOVX protein, expression of NOVX nucleic acid, or mutation content of NOVX genes in an individual can be determined to thereby select appropriate agent(s) for therapeutic or prophylactic treatment of the individual.  
       [0308] Pharmacogenomics deals with clinically significant hereditary variations in the response to drugs due to altered drug disposition and abnormal action in affected persons. See e g, Eichelbaum, 1996.  Clin. Exp Pharmacol. Physiol.,  23: 983-985; Linder, 1997.  Clin Chem,  43:254-266. In general, two types of pharmacogenetic conditions can be differentiated. Genetic conditions transmitted as a single factor altering the way drugs act on the body (altered drug action) or genetic conditions transmitted as single factors altering the way the body acts on drugs (altered drug metabolism). These pharmacogenetic conditions can occur either as rare defects or as polymorphisms. For example, glucose-6-phosphate dehydrogenase (G6PD) deficiency is a common inherited enzymopathy in which the main clinical complication is hemolysis after ingestion of oxidant drugs (anti-malarials, sulfonamides, analgesics, nitrofurans) and consumption of fava beans.  
       [0309] As an illustrative embodiment, the activity of drug metabolizing enzymes is a major determinant of both the intensity and duration of drug action. The discovery of genetic polymorphisms of drug metabolizing enzymes (e.g., N-acetyltransferase 2 (NAT 2) and cytochrome pregnancy zone protein precursor enzymes CYP2D6 and CYP2C19) has provided an explanation as to why some patients do not obtain the expected drug effects or show exaggerated drug response and serious toxicity after taking the standard and safe dose of a drug. These polymorphisms are expressed in two phenotypes in the population, the extensive metabolizer (EM) and poor metabolizer (PM). The prevalence of PM is different among different populations. For example, the gene coding for CYP2D6 is highly polymorphic and several mutations have been identified in PM, which all lead to the absence of functional CYP2D6. Poor metabolizers of CYP2D6 and CYP2C19 quite frequently experience exaggerated drug response and side effects when they receive standard doses. If a metabolite is the active therapeutic moiety, PM show no therapeutic response, as demonstrated for the analgesic effect of codeine mediated by its CYP2D6-formed metabolite morphine. At the other extreme are the so called ultra-rapid metabolizers who do not respond to standard doses. Recently, the molecular basis of ultra-rapid metabolism has been identified to be due to CYP2D6 gene amplification.  
       [0310] Thus, the activity of NOVX protein, expression of NOVX nucleic acid, or mutation content of NOVX genes in an individual can be determined to thereby select appropriate agent(s) for therapeutic or prophylactic treatment of the individual. In addition, pharmacogenetic studies can be used to apply genotyping of polymorphic alleles encoding drug-metabolizing enzymes to the identification of an individual&#39;s drug responsiveness phenotype. This knowledge, when applied to dosing or drug selection, can avoid adverse reactions or therapeutic failure and thus enhance therapeutic or prophylactic efficiency when treating a subject with a NOVX modulator, such as a modulator identified by one of the exemplary screening assays described herein.  
       [0311] Monitoring of Effects During Clinical Trials  
       [0312] Monitoring the influence of agents (e.g., drugs, compounds) on the expression or activity of NOVX (e.g., the ability to modulate aberrant cell proliferation and/or differentiation) can be applied not only in basic drug screening, but also in clinical trials. For example, the effectiveness of an agent determined by a screening assay as described herein to increase NOVX gene expression, protein levels, or upregulate NOVX activity, can be monitored in clinical trails of subjects exhibiting decreased NOVX gene expression, protein levels, or downregulated NOVX activity. Alternatively, the effectiveness of an agent determined by a screening assay to decrease NOVX gene expression, protein levels, or downregulate NOVX activity, can be monitored in clinical trails of subjects exhibiting increased NOVX gene expression, protein levels, or upregulated NOVX activity. In such clinical trials, the expression or activity of NOVX and, preferably, other genes that have been implicated in, for example, a cellular proliferation or immune disorder can be used as a “read out” or markers of the immune responsiveness of a particular cell.  
       [0313] By way of example, and not of limitation, genes, including NOVX, that are modulated in cells by treatment with an agent (e g., compound, drug or small molecule) that modulates NOVX activity (e.g., identified in a screening assay as described herein) can be identified. Thus, to study the effect of agents on cellular proliferation disorders, for example, in a clinical trial, cells can be isolated and RNA prepared and analyzed for the levels of expression of NOVX and other genes implicated in the disorder. The levels of (gene expression (i e., a gene expression pattern) can be quantified by Northern blot analysis or RT-PCR, as described herein, or alternatively by measuring the amount of protein produced, by one of the methods as described herein, or by measuring the levels of activity of NOVX or other genes. In this manner, the gene expression pattern can serve as a marker, indicative of the physiological response of the cells to the agent. Accordingly, this response state may be determined before, and at various points during, treatment of the individual with the agent.  
       [0314] In one embodiment, the invention provides a method for monitoring the effectiveness of treatment of a subject with an agent (e g., an agonist, antagonist, protein, peptide, peptidomimetic, nucleic acid, small molecule, or other drug candidate identified by the screening assays described herein) comprising the steps of (i) obtaining a pre-administration sample from a subject prior to administration of the agent; (ii) detecting the level of expression of a NOVX protein, mRNA, or genomic DNA in the preadministration sample; (iii) obtaining one or more post-administration samples from the subject; (iv) detecting the level of expression or activity of the NOVX protein, mRNA, or genomic DNA in the post-administration samples; (v) comparing the level of expression or activity of the NOVX protein, mRNA, or genomic DNA in the pre-administration sample with the NOVX protein, mRNA, or genomic DNA in the post administration sample or samples; and (vi) altering the administration of the agent to the subject accordingly. For example, increased administration of the agent may be desirable to increase the expression or activity of NOVX to higher levels than detected, i.e., to increase the effectiveness of the agent. Alternatively, decreased administration of the agent may be desirable to decrease expression or activity of NOVX to lower levels than detected, i.e., to decrease the effectiveness of the agent.  
       [0315] Methods of Treatment  
       [0316] The invention provides for both prophylactic and therapeutic methods of treating a subject at risk of (or susceptible to) a disorder or having a disorder associated with aberrant NOVX expression or activity. The disorders include but are not limited to, e.g., those diseases, disorders and conditions listed above, and more particularly include those diseases, disorders, or conditions associated with homologs of a NOVX protein, such as those summarized in Table A.  
       [0317] These methods of treatment will be discussed more fully, below.  
       [0318] Diseases and Disorders  
       [0319] Diseases and disorders that are characterized by increased (relative to a subject not suffering from the disease or disorder) levels or biological activity may be treated with Therapeutics that antagonize (i.e., reduce or inhibit) activity. Therapeutics that antagonize activity may be administered in a therapeutic or prophylactic manner. Therapeutics that may be utilized include, but are not limited to: (i) an aforementioned peptide, or analogs, derivatives, fragments or homologs thereof; (ii) antibodies to an aforementioned peptide; (iii) nucleic acids encoding an aforementioned peptide; (iv) administration of antisense nucleic acid and nucleic acids that are “dysfunctional” (i.e., due to a heterologous insertion within the coding sequences of coding sequences to an aforementioned peptide) that are utilized to “knockout” endogenous function of an aforementioned peptide by homologous recombination (see, e.g., Capecchi, 1989.  Science  244: 1288-1292); or (v) modulators (i e, inhibitors, agonists and antagonists, including additional peptide mimetic of the invention or antibodies specific to a peptide of the invention) that alter the interaction between an aforementioned peptide and its binding partner.  
       [0320] Diseases and disorders that are characterized by decreased (relative to a subject not suffering from the disease or disorder) levels or biological activity may be treated with Therapeutics that increase (i.e., are agonists to) activity. Therapeutics that upregulate activity may be administered in a therapeutic or prophylactic manner. Therapeutics that may be utilized include, but are not limited to, an aforementioned peptide, or analogs, derivatives, fragments or homologs thereof, or an agonist that increases bioavailability.  
       [0321] Increased or decreased levels can be readily detected by quantifying peptide and/or RNA, by obtaining a patient tissue sample (e.g., from biopsy tissue) and assaying it in vitro for RNA or peptide levels, structure and/or activity of the expressed peptides (or mRNAs of an aforementioned peptide). Methods that are well-known within the art include, but are not limited to, immunoassays (e.g., by Western blot analysis, immunoprecipitation followed by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis, immunocytochemistry, etc.) and/or hybridization assays to detect expression of mRNAs (e.g., Northern assays, dot blots, in situ hybridization, and the like).  
       [0322] Prophylactic Methods  
       [0323] In one aspect, the invention provides a method for preventing, in a subject, a disease or condition associated with an aberrant NOVX expression or activity, by administering to the subject an agent that modulates NOVX expression or at least one NOVX activity. Subjects at risk for a disease that is caused or contributed to by aberrant NOVX expression or activity can be identified by, for example, any or a combination of diagnostic or prognostic assays as described herein. Administration of a prophylactic agent can occur prior to the manifestation of symptoms characteristic of the NOVX aberrancy, such that a disease or disorder is prevented or, alternatively, delayed in its progression. Depending upon the type of NOVX aberrancy, for example, a NOVX agonist or NOVX antagonist agent can be used for treating the subject. The appropriate agent can be determined based on screening assays described herein. The prophylactic methods of the invention are further discussed in the following subsections.  
       [0324] Therapeutic Methods  
       [0325] Another aspect of the invention pertains to methods of modulating NOVX expression or activity for therapeutic purposes. The modulatory method of the invention involves contacting a cell with an agent that modulates one or more of the activities of NOVX protein activity associated with the cell. An agent that modulates NOVX protein activity can be an agent as described herein, such as a nucleic acid or a protein, a naturally-occurring cognate ligand of a NOVX protein, a peptide, a NOVX peptidomimetic, or other small molecule. In one embodiment, the agent stimulates one or more NOVX protein activity. Examples of such stimulatory agents include active NOVX protein and a nucleic acid molecule encoding NOVX that has been introduced into the cell. In another embodiment, the agent inhibits one or more NOVX protein activity. Examples of such inhibitory agents include antisense NOVX nucleic acid molecules and anti-NOVX antibodies. These modulatory methods can be performed in vitro (e.g., by culturing the cell with the agent) or, alternatively, in vivo (e.g., by administering the agent to a subject). As such, the invention provides methods of treating an individual afflicted with a disease or disorder characterized by aberrant expression or activity of a NOVX protein or nucleic acid molecule. In one embodiment, the method involves administering an agent (e.g., an agent identified by a screening assay described herein), or combination of agents that modulates (e.g., up-regulates or down-regulates) NOVX expression or activity. In another embodiment, the method involves administering a NOVX protein or nucleic acid molecule as therapy to compensate for reduced or aberrant NOVX expression or activity.  
       [0326] Stimulation of NOVX activity is desirable in situations in which NOVX is abnormally downregulatcd and/or in which increased NOVX activity is likely to have a beneficial effect. One example of such a situation is where a subject has a disorder characterized by aberrant cell proliferation and/or differentiation (e.g., cancer or immune associated disorders). Another example of such a situation is where the subject has a gestational disease (e.g., preclampsia).  
       [0327] Determination of the Biological Effect of the Therapeutic  
       [0328] In various embodiments of the invention, suitable in vitro or in vivo assays are performed to determine the effect of a specific Therapeutic and whether its administration is indicated for treatment of the affected tissue.  
       [0329] In various specific embodiments, in vitro assays may be performed with representative cells of the type(s) involved in the patient&#39;s disorder, to determine if a given Therapeutic exerts the desired effect upon the cell type(s). Compounds for use in therapy may be tested in suitable animal model systems including, but not limited to rats, mice, chicken, cows, monkeys, rabbits, and the like, prior to testing in human subjects. Similarly, for in vivo testing, any of the animal model system known in the art may be used prior to administration to human subjects.  
       [0330] Prophylactic and Therapeutic Uses of the Compositions of the Invention  
       [0331] The NOVX nucleic acids and proteins of the invention are useful in potential prophylactic and therapeutic applications implicated in a variety of disorders. The disorders include but are not limited to, e.g., those diseases, disorders and conditions listed above, and more particularly include those diseases, disorders, or conditions associated with homologs of a NOVX protein, such as those summarized in Table A.  
       [0332] As an example, a cDNA encoding the NOVX protein of the invention may be useful in gene therapy, and the protein may be useful when administered to a subject in need thereof. By way of non-limiting example, the compositions of the invention will have efficacy for treatment of patients suffering from diseases, disorders, conditions and the like, including but not limited to those listed herein.  
       [0333] Both the novel nucleic acid encoding the NOVX protein, and the NOVX protein of the invention, or fragments thereof, may also be useful in diagnostic applications, wherein the presence or amount of the nucleic acid or the protein are to be assessed. A further use could be as an anti-bacterial molecule (i.e., some peptides have been found to possess anti-bacterial properties). These materials are further useful in the generation of antibodies, which immunospecifically-bind to the novel substances of the invention for use in therapeutic or diagnostic methods.  
       [0334] The invention will be further described in the following examples, which do not limit the scope of the invention described in the claims.  
     
    
    
     EXAMPLES  
     Example A  
     [0335] Polynucleotide and Polypeptide Sequences, and Homology Data  
     Example 1  
     [0336] The NOV1 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 1A.  
               TABLE 1A                       NOV1 Sequence Analysis                                                    SEQ ID NO: 1   3163 bp                             NOV1a,     CTCCCCACGGCGCCAGGAGGAGGGGCGAGGGCCGGCAGCCCCCTCTCCCCCGCGCGGC             CG113254-01       DNA Sequence     GCAGGAGCCGAGCCCAGCCCCGGGGACCCGCCGCCGCCGGTC   ATGT GGGCCGGACTGC                   TCCTTCGGGCCGCCTGTGTCGCGCTCCTGCTGCCGGGGGCACCAGCCCGAGGCTACAC                   CGGGAGGAAGCCGCCCGGGCACTTCGCGGCCGAGAGACGCCGACTGGGCCCCCACGTC                   TGCCTCTCTGGGTTTGGGAGTGGCTGCTGCCCTGGCTGGGCGCCCTCTATGGGTGGTG                   GGCACTGCACCCTACCCCTCTACTCCTTCGGCTGTGGGAGTGGCATCTGCATCGCTCC                   CAATGTCTGCTCCTGCCAGGATGGAGAGCAAGGGCCCACCTGCCCAGAAACCCATGGA                   CCATGTGGGGAGTACGGCTGTGACCTTACCTGCAACCATGGAGGCTGTCAGGAGGTGG                   CCCGAGTGTGCCCCGTGGGCTTCTCGATGACGGAGACAGCTGTTGGCATCAGGTGTAC                   AGACATTGACGAATGTGTAACCTCCTCCTGCGAGGGCCACTGTGTGAACACAGAAGGT                   GGGTTTGTGTGCGAGTGTGGGCCGGGCATGCAGCTGTCTGCCGACCGCCACAGCTGCC                   AAGACACTGACGAATGCCTAGGGACTCCCTGTCAGCAGAGATGTAAAAACAGCATTGG                   CAGCTACAAGTGTTCCTGTCGAACTGGCTTCCACCTTCATGGCAACCGGCACTCCTGT                   GTAGATGTAAACGAGTGTCGGAGGCCATTGGAGAGGCGAGTCTGTCACCATTCCTCCC                   ACAACACCGTGGGCAGCTTCCTATGCACATGCCGACCTGGCTTCAGGCTCCGAGCTGA                   CCGCGTGTCCTGTGAAGCTTTCCCGAAAGCCGTGCTGGCCCCATCTGCCATCCTGCAA                   CCCCGGCAACACCCGTCCAAGATGCTTCTGTTGCTTCCTGAGGCCGGCCGGCCTGCCC                   TGTCCCCAGGACATAGCCCTCCTTCTGGGGCTCCAGGGCCCCCAGCCGGAGTCAGGAC                   CACCCGCCTGCCATCTCCCACCCCACGACTACCCACATCCTCCCCTTCTGCCCCTGTG                   TGGCTGCTGTCCACCCTGCTGGCCACCCCAGTGCCTACTGCCTCCCTGCTGCGGAACC                   TCAGACCCCCCTCACTCCTTCAGGGGGAGGTGATGGGGACCCCTTCCTCACCCAGGGG                   CCCTGAGTCCCCCCGACTGGCAGCAGGGCCCTCTCCCTGCTGGCACCTGGGAGCCATG                   CATGAATCAAGGAGTCGCTGGACAGAGCCTGGGTGTTCCCAGTGCTGGTGCGAGGACG                   GGAAGGTGACCTGTGAAAAGGTGAGGTGTGAAGCTGCTTGTTCCCACCCAATTCCCTC                   CAGAGATGGTGGGTGCTGCCCATCGTGCACAGGCTGTTTTCACACTGGTGTCGTCCGA                   GCTGAAGGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTCTGTGTCTGTCTGG                   CTGGAAACGTGTCCTGCATCTCTCCTGAGTGTCCTTCTGGCCCCTGTCACACCCCCCC                   ACAGACGGATTGCTGTACTTGTGTTCCAGTGAGATGCTATTTCCACGGCCGGTGGTAC                   GCAGACGGGGCTGTGTTCAGTGGGGGTGGTGACGAGTGTACCACCTGTGTTTGCCAGA                   ATGGGGACGTCGAGTGCTCCTTCATGCCCTGCCCTGAGCTGGCCTGCCCCCGAGAAGA                   GTGGCGGCTGGGCCCTGGGCAGTGTTGCTTCACCTGCCAGGAGCCCACACCCTCGACA                   GGTTGCTCTCTTGACGACAACGGGGTTGAGTTTCCGATTGGACAGATCTGGTCGCCTG                   GTGACCCCTGTAGATGGCTCGGTGAGCTGCAAGAGGACAGACTGTGTGGACTCCTGCC                   CTCACCCGATCCGGATCCCTGGACAGTGCTGCCCAGACTGTTCAGCAGGTTGCACCTA                   CACAGGCAGAATCTTCTA TAA   CAACGAGACCTTCCCGTCTGTGCTGGACCCATGTCTG                       AGCTCCATCTGCCTGACAGACTGCAACTACGAGGGAAGGAAGGTGGCGAATGGCCAGG                       TGTTCACCTTGGATGATGAACCCTGCACCCGGTGCACGTGCCAGCTAGATTCCCTGTC                       TCCTCTGGAAGAAAAGCAGGGGCTCTCCCCTCACGGAAATGTGGCATTCAGCAAAGCT                       GGTCGGAGCCTGCATGGAGACACTGAGGCCCCTGTCAACTGTAGCTCCTGTCCTCGGC                       CCCCGACAGCATCACCCTCGAGGCCGGTGCTTCATCTCCTCCAGCTCCTTTTAAGAAC                       GAACTTGATGAAAACACAGACTTTACCTACAAGCCCGGCAGGAGCTCATGGTCCACAC                       TCACTCGCTTTGGGGCTGACACCCACTTTCCCAGGGGAGCCTGGGGCCTCCCCTCGAC                       TCTCACCAGGGCCTTCGACCCCTCCAGGAGCCCCCACTCTACCTCTAGCTTCCCCAGG                       GGCTCCTCAGCCACCTCCTGTGACTCCAGAGCGCTCGTTCTCAGCCTCTGGGGCCCAG                       ATAGTGTCCAGGTGGCCTCCTCTGCCTGGCACCCTCCTGACGGAAGCTTCAGCACTTT                       CCATGATGGACCCCAGCCCCTCGAAGACCCCCATCACCCTCCTCGGGCCTCGCGTGCT                       TTCTCCCACCACCTCTAGACTCTCCACAGCCCTTGCAGCCACCACCCACCCTGGCCCC                       CAGCAGCCCCCAGTGGGGGCTTCTCGGGGGGAAGAGTCCACCATGTAAGGAGGTCACT                       GTGTCCGGGAGACTCTGGAGAGAGGACCTCTGCCAGTGGCCCAGGGTGTGTGCAGGGC                       AGCTCCAAGGATGAACCTGGTGGGGATGCCTGGGCTCCCTCCTGCAGGGGCCCTGGTG                       AGGATGGAAGACCCCCAAGGCTGGATGTAACCTTGTTCCCAAGAAGTGTTTGGAATGT                       GCTGTAAGAATGGAGGAAGTCGTTTCCACTGTCAGCATCCTCCCTGGACCGCGTGGCT                       GGCTCATCTTTTGAGAAGGGTTGGGACTGCCAAGTTCTCCTGGAGGAAGAGTTGCGTC                       CGGCTGGGATTCCACTCACTGGGACTGTACCGCCAGGTGTCATGCGTCTCTCTGAGGT                       TTCCTGATTAAAGGTTGTCTCGGTTTCAAAA                                           ORF Start: ATG at 101   ORF Stop: TAA at 1991                                         SEQ ID NO: 2   630 aa   MW at 66952.5 kD                             NOV1a,   MWAGLLLRAACVALLLPGAPARGYTGRKPPGHFAAERRRLGPHVCLSGFGSGCCPGWA           CG113254-01       Protein Sequence   PSMGGGHCTLPLYSFGCGSGICIAPNVCSCQDGEQGATCPETHGPCGEYGCDLTCNHG                   CCQEVARVCPVGFSMTETAVGIRCTDIDECVTSSCEGHCVNThGGFVCECGPGMQLSA                   DRHSCQDTDECLGTPCQQRCKNSIGSYKCSCRTGFHLHGNRHSCVDVNECRRPLERRV                   CHHSCHNTVGSFLCTCRPGFRLRADRVSCEAFPKAVLAPSAILQPRQHPSKMLLLLPE                   AGRPALSPGHSPPSGAPGPPAGVRTTRLPSPTPRLPTSSPSAPVWLLSTLLATPVPTA                   SLLGNLRPPSLLQGEVMGTPSSPRGPESPRLAAGPSPCWHLGAMHESRSRWTEPGCSQ                   CWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGCFHSGVVRAEGDVFSPPNENCT                   VCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPVRCYFHGRWYADGAVFSGGGDECT                   TCVCQNGEWECSFMPCPELACPREEWRLGPGQCCFTCQEPTPSTCCSLDDNGVEFPIG                   QIWSPGDPCRWLGELQEDRLCGLLPSPDPDPWTVLPRLFSRLHLHRQNLL                                         SEQ ID NO:3   1830 bp                             NOV1b,     GGTC   ATG TGCGCCGGACTGCTCCTTCGGGCCGCCTGTGTCGCGCTCCTGCTGCCGGGG           CG113254-02       DNA Sequence   CCACCAGCCCGAGGCTACACCCCGACGAAGCCGCCCGGGCACTTCGCGGCCGAGAGAC                   GCCGACTGGGCCCCCACGTCTGCCTCTCTGGGTTTGGGAGTGCCTGCTGCCCTGGCTG                   GGCGCCCTCTATGGGTGGTGGGCACTGCACCCTGCCCCTCTGCTCCTTCGGCTGTGGG                   AGTGGCATCTCCATCGCTCCCAATGTCTGCTCCTGCCAGGATGGAGAOCAACGGGCCA                   CCTGCCCAGAAACCCATGGACCATGTGGGGAGTACGGCTGTGACCTTACCTGCAGCCA                   TGGAGGCTGTCAGGAGGTGGCCCGAGTGTGCCCCGTGGGCTTCTCGATGACGGAGACA                   GCTGTTCGCATCACGTGTACAGACATTGACGAATGTGTAACCTCCTCCTGCGACGGCC                   ACTGTGTGAACACAGAAGGTGGGTTTGTGTGCGAGTGTGGGCCGGGCATGCAGCTGTC                   TGCCGACCGCCACAGCTGCCAAGACACTGACGAATGCCTAGGGACTCCCTCTCAGCAG                   AGATGTPAAAACAGCATTGGCACCTACAAGTCTTCCTGTCGAACTGGCTTCCACCTTC                   ATGCCAACCGGCACTCCTGTGTAGCTTTCCCGAAACCCGTGCTGGCCCCATCTGCCAT                   CCTGCAACCCCGGCAACACCCGTCCAAGATGCTTCTGTTGCTTCCTGAGGCCGGCCGG                   CCTGCCCTGTCCCCAGGACATAGCCCTCCTTCTGGGGCTCCAGGGCCCCCAGCCGGAG                   TCAGGACCACCCGCCTGCCATCTCCCACCCCACGACTACCCACATCCTCCCCTTCTGC                   CCCTGTGTGGCTGCTGTCCACCCTGCTGGCCACCCCAGTGCCTACTGCCTCCCTGCTC                   GGGAACCTCAGACCCCCCTCACTCCTTCAGGGGGAGGTGATGGGGACCCCTTCCTCAC                   CCAGGCGCCCTGAGTCCCCCCGACTGGCAGCAGGGCCCTCTCCCTGCTGGCACCTGGG                   AGCCATGCATGAATCAAGGAGTCGCTCGACAGAGCCTGGGTGTTCCCAGTGCTGGTGC                   GAGGACGGGAACCTCACCTGTCAAAAGGTGAGGTGTGAAGCTGCTTGTTCCCACCCAA                   TTCCCTCCAGAGATGGTCGCTCCTGCCCATCGTGCACACGCTGTTTTCACACTGGTGT                   CCTCCGAGCTGAACGGGATGTGTTTTCACCTCCCAATGAGAACTGCACCGTCTGTGTC                   TGTCTGGCTGGAAACGTGTCCTGCATCTCTCCTGAGTGTCCTTCTGGCCCCTGTCAGA                   CCCCCCCACAGACGGATTGCTGTACTTGTGTTCCAGTGAGATGCTATTTCCACGGCCG                   GTGGTACGCAGACGGAGCTGTGTTCAGTGGGGGTGGTGACGAGTGTACCACCTGTGTT                   TGCCAGAATCCCGAGGTGGAGTGCTCCTTCATGCCCTGCCCTGAGCTGGCCTCCCCCC                   GAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTCACCTGCCAGGAGCCCACACC                   CTCGACAGGCTGCTCTCTTGACGACAACGGGGTTGAGTTTCCGATTGGACAGATCTGG                   TCGCCTGGTGACCCCTGTGAGTTATGCATCTGCCAGGCAGATGGCTCGGTGAGCTGCA                   AGAGGACAGACTGTGTGGACTCCTGCCCTCACCCGATCCGGATCCCTGGACAGTGCTC                   CCCAGACTGTTCAGCAGGTAATCCCCTGCCTCTGCCCCAAGCCCCCAGGGCAGGGCAT                                         ORF Start: ATG at 5   ORF Stop: TAA at 1817                                         SEQ ID NO: 4   604 aa   MW at 63127.1 kD                             NOV1b,   MWAGLLLRAACVALLLPGAPARGYTGRKPPGHFAAERRRLGPHVCLSGFGSCCCPGWA           CG113254-02       Protein Sequence   PSMGGGHCTLPLCSFGCGSGICIAPNVCSCQDGEQGATCPETHGPCGEYGCDLTCSHC                   GCQEVARVCPVGFSMTETAVGIRCTDIDECVTSSCEGHCVNTEGGFVCECGPGMQLSA                   DRHSCQDTDECLGTPCQQRCKNSIGSYKCSCRTGFHLHGNRHSCVAFPKAVLAPSAIL                   QPRQHPSKMLLLLPEAGRPALSPGHSPPSGAPGPPAGVRTTRLPSPTPRLPTSSPSAP                   VWLLSTLLATPVPTASLLGNLRPPSLLQGEVMGTPSSPRGPESPRLAAGPSPCWHLGA                   MHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCTGCFHSGVV                   RAEGDVFSPPNENCTVCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPVRCYFHGRW                   YADGAVFSGGGDECTTCVCQNGEVECSFMPCPELACPREEWRLGPGQCCFTCQEPTPS                   TGCSLDDNGVEFPIGQIWSPGDPCELCICQADGSVSCKRTDCVDSCPHPIRIPCQCCP                   DCSAGNPLPLPQAPRAGHLRHRAP                                         SEQ ID NO:5   597 bp                             NOV1c,   GGTACCTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGTCGCTGGACAGAGCCTG           211648303 DNA       Sequence   GGTGTTCCCAGTGCTGGTGCGAGGACGGGAAGGTGACCTGTGAAAAGGTGAGGTGTGA                   AGCTCCTTGTTCCCACCCAATTCCCTCCAGAGATGGTGGGTGCTGCCCATCGTGCACA                   GGCTGTTTTCACAGTGGTGTCGTCCGAGCTGAAGGGGATGTGTTTTCACCTCCCAATG                   AGAACTGCACCGTCTGTGTCTGTCTGGCTGGAAACGTGTCCTGCATCTCTCCTGAGTG                   TCCTTCTGGCCCCTGTCAGACCCCCCCACAGACGGATTGCTGTACTTGTGTTCCAGTG                   AGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCTGTGTTCAGTGGCGGTGGTG                   ACGAGTGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGCTCCTTCATGCCCTG                   CCCTGAGCTGGCCTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTC                   ACCTGCCAGGAGCCCACACCCTCGACAGGCTGCTCTCTTGACGACAACGGGGTTGAGT                   TTCCGATTGGAGTCGAC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO:6   199 aa   MW at 21235.6 kD                             NOV1c,   GTCWHLGAMHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCT           211648303       Protein Sequence   GCFHSGVVRAEGDVFSPPNENCTVCVCLAGNVSCISPECPSGPCQTPPQTDCCTCVPV                   RCYFHGRWYADGAVFSGGGDECTTCVCQNGEVECSFMPCPELACPREEWRLGPGQCCF                   TCQEPTPSTGCSLDDNGVEFPIGVD                                         SEQ ID NO:7   597 bp                             NOV1d,     GGT ACCTGCTGGCACCTGGGAGCCATGCATGAATCAAGGAGTCGCTGGACAGAGCCTG           212170920 DNA       Sequence   GGTGTTCCCAGTGCTGGTGCGAGGACGGGAAGGTGACCTGTGAAAAGGTGAGGTGTGA                   AGCTGCTTGTTCCCACCCAATTCCCTCCACAGATGGTCGGTGCTGCCCATCGTGCACA                   GGCTGTTTTCACAGTGGTGTCGTCCGAGCTGAAGGGGATGTGTTTTCACCTCCCAATG                   AGAACTGCACCGTCTGTGTCTGTCTGGCTGQAAACGTGTCCTGCATCTCTCCAGAGTG                   TCCTTCTGGCCCCTGTCAGGCCCCCCCACAGACCGATTGCTGTACTTGTGTTCCAGTG                   AGATGCTATTTCCACGGCCGGTGGTACGCAGACGGGGCTGTATTCACTGGGGGTGGTG                   ACGAGTGTACCACCTGTGTTTGCCAGAATGGGGAGGTGGAGTGCTCCTTCATGCCCTA                   CCCTGAGCTGGCCTGCCCCCGAGAAGAGTGGCGGCTGGGCCCTGGGCAGTGTTGCTTC                   ACCTGCCAGGAGCCCACACCCTCGACAGGCTGCTCTCTTGACGACAACGGGGTTGAGT                   TTCCGATTGGAGTCGAC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO:8   199 aa   MW at 21265.6 kD                             NOV1d,   GTCWHLGAMHESRSRWTEPGCSQCWCEDGKVTCEKVRCEAACSHPIPSRDGGCCPSCT           212170920       Protein Sequence   GCFHSGVVRAEGDVFSPPNENCTVCVCLAGNVSCISPECPSGPCQAPPQTDCCTCVPV                   RCYFHGRWYADGAVFSGGGDECTTCVCQNGEVECSFMPYPELACPREEWRLGPGQCCF                   TCQEPTPSTGCSLDDNGVEFPIGVD                  
 
     [0337] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 1B.  
               TABLE 1B                          Comparison of NOV1a against NOV1b through NOV1d.                                         Identities/                   Similarities               NOV1a Residues/   for the           Protein Sequence   Match Residues   Matched Region                       NOV1b   1 . . . 589   477/589 (80%)               1 . . . 546   478/589 (80%)           NOV1c   386 . . . 580    179/195 (91%)               3 . . . 197   179/195 (91%)           NOV1d   386 . . . 580    193/195 (98%)               3 . . . 197   193/195 (98%)                      
 
     [0338] Further analysis of the NOV1a protein yielded the following properties shown in Table 1C.  
               TABLE 1C                       Protein Sequence Properties NOV1a                                                PSort   0.5947 probability located in outside; 0.1900           analysis:   probability located in lysosome (lumen);               0.1000 probability located in endoplasmic               reticulum (membrane); 0.1000 probability               located in endoplasmic reticulum (lumen)           SignalP   Cleavage site between residues 22 and 23           analysis:                      
 
     [0339] A search of the NOV1a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 1D.  
               TABLE 1D                          Geneseq Results for NOV1a                                     Protein/       Identities/               Organism/   NOV1a   Similarities           Length   Residues/   for the       Geneseq   [Patent #,   Match   Matched   Expect       Identifier   Date]   Residues   Region   Value               AAM99920   Human polypeptide   389 . . . 589   201/201 (100%)   e−133           SEQ ID NO 36 -    5 . . . 205   201/201 (100%)             Homo sapiens , 272           aa. [WO200155173-           A2, 02 AUG. 2001]       AAM99933   Human polypeptide   389 . . . 589   197/201 (98%)   e−131           SEQ ID NO 49 -  Homo      5 . . . 205   198/201 (98%)             sapiens , 212 aa           [WO200155173-A2,           02 AUG. 2001]       AAB85364   Novel Von   284 . . . 489   206/206 (100%)   e−128           Willebrand/    1 . . . 206   206/206 (100%)           thrombosporin-           like polypeptide -             Homo sapiens , 235 aa.           [WO200153485-A1,           26 JUL. 2001]       AAB85365   Novel Von   302 . . . 489   188/188 (100%)   e−117           Willebrand/    1 . . . 188   188/188 (100%)           thrombosporin-           like mature protein           sequence -             Homo sapiens , 217 aa.           [WO200153485-A1,           26 JUL. 2001]       ABG15393   Novel human    70 . . . 138   68/69 (98%)   2e−37           diagnostic    959 . . . 1027   68/69 (98%)           protein #15384 -             Homo sapiens ,           1028 aa.           [WO200175067-A2,           11 OCT. 2001]                  
 
     [0340] In a BLAST search of public sequence datbases, the NOV1a protein was found to have homology to the proteins shown in the BLASTP data in Table 1E.  
               TABLE 1E                          Public BLASTP Results for NOV1a                                             Identities/                   NOV1a   Similarities       Protein   Protein/   Residues/   for the       Accession   Organism/   Match   Matched   Expect       Number   Length   Residues   Portion   Value                                         Q96DN2   CDNA FLJ32009 fis,   1 . . . 589   587/589 (99%)   0.0           clone   1 . . . 589   587/589 (99%)           NT2RP7009498,           weakly similar to           fibulin-1, isoform           A precursor -             Homo sapiens             (Human), 955 aa.       Q9DBE2   1300015B04Rik   1 . . . 615   517/615 (84%)   0.0           protein -  Mus     1 . . . 607   547/615 (88%)             musculus  (Mouse),           608 aa.       Q9IBG7   Kielin -  Xenopus     368 . . . 589     79/227 (34%)   2e−32             laevis  (African   1483 . . . 1695    109/227 (47%)           clawed frog),           2327 aa.       Q91V88   POEM (NEPHRONECTIN   44 . . . 373    103/364 (28%)   1e−31           short   35 . . . 383    153/364 (41%)           isoform) -  Mus               musculus  (Mouse),           561 aa.       Q9CXD8   6130401L20Rik   53 . . . 261     79/221 (35%)   7e−31           protein -  Mus     96 . . . 308    101/221 (44%)             musculus  (Mouse),           528 aa.                  
 
     [0341] PFam analysis indicates that the NOV1a protein contains the domains shown in the Table 1F.  
               TABLE 1F                          Domain Analysis of NOV1a                                     Identities/                   Similarities           NOV1a Match   for the Matched       Pfam Domain   Region   Region   Expect Value               EGF   146 . . . 179   16/47 (34%)   0.0045                23/47 (49%)       EGF   185 . . . 218   12/47 (26%)   0.011                25/47 (53%)       TIL   166 . . . 224   13/70 (19%)   0.53                 40/70 (57%)       EGF   224 . . . 261   12/48 (25%)   0.034                26/48 (54%)       vwc   386 . . . 440   21/84 (25%)   7.8e−08               40/84 (48%)       vwc   443 . . . 496   21/84 (25%)   5.8e−05               37/84 (44%)       vwc   501 . . . 559   22/84 (26%)   1.3e−09               41/84 (49%)                  
 
     Example 2  
     [0342] The NOV2 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 2A.  
               TABLE 2A                       NOV2 Sequence Analysis                                                    SEQ ID NO: 9   4036 bp                             NOV2a,     TCCTGG   ATG AGGCAGCTCAGTCACAGAGGGTGGGCCCCCAGAGAAGGGAAAATTGTGA           CG122729-01       DNA Sequence   GCAGCCCACACTGCTGGCAGATGCGGCATAAGTGTCCCAGCCAGGCTAGGGAGGCGGT                   GGGCACTGGGTGCACACGATGGCCCTGTGGTTGCTGTCTCAGTCCCGGGCTGTGCTTC                   CAGGCTTCTCCAGACCACGCCACCAGCCAACAGAAGCGAGACTTCCAGTCCGAGGTCC                   TGCTTTCTGCTATGGAACTATTCCACATGACAAGTGGAGGTGATGCAGCCATGTTCAG                   AGACGGCAAAGAGCCTCAGCCAAGTGCAGAAGCTGCTGCTGCCCCTTCTCTTGCCAAC                   ATCTCCTGCTTCACCCAGAAGCTGGTGGAGAAGCTGTACAGTGGGATGTTCTCGGCAG                   ACCCCAGGCATATCCTCCTCTTCATCCTGGAGCACATCATGGTGGTCATTGAGACTGC                   CTCTTCTCAAAGGGACACTGTCCTCAGCACTTTATACAGCAGTTTAAATAAAGTCATT                   CTTTATTGCCTATCCAAGCCCCAGCAGTCCCTCTCCGAATGCCTCGGCCTTCTCAGCA                   TCCTGCGCTTTCTGCAGGAGCACTGGGATGTTGTCTTTGCCACCTACAATTCCAACAT                   CACCTTCCTCCTGTGTCTCATGCATTGCCTTTTGCTACTCAATGAGAGAAGTTACCCA                   GAAGGATTTGGATTGGAGCCCAAGCCTAGAATGTCTACTTATCATCAAGTCTTCCTTT                   CCCCAAATGAAGACGTGAAAGAAAAAAGAGAAGACTTACCAAGTTTCAGTGATGTCCA                   ACACAACATCCAGAAGACAGTGCACACTCTCTGGCAGCAGCTGGTGGCACAAAGGCAG                   CAGACCCTGGAGGATGCCTTCAAGATCGATCTCTCTGTGAAACCTGGAGAGAGCGAAG                   TGAAGATTGAAGAGGTCACACCGCTCTGGGAGGAGACGATGCTCAAGGCCTGGCAGCA                   TTACTTAGCATCTGAGAAGAAGTCACTGGCAAGTCGTTCAAATGTTGCACACCACACC                   AAAGTCACTTTGTGGAGTGGAAGCCTGTCCTCAGCCATCAAGCTGATGCCCGGGCGGC                   AGGCCAAGGACCCTGAGTGCAAGACAGAGGATTTTGTGTCATGTATAGAGAACTACAG                   AAGAAGAGGACAAGAGCTATATGCATCTTTATACAAAGACCATGTGCAPAGGCGAAAA                   TGTGGCAACATCAAGGCAGCCAACGCCTGGGCCAGGATCCAGGAGCAGCTTTTTGGGG                   AGCTGGGCTTGTGGAGCCAGGGGGAAGAAACCAAGCCCTGTTCCCCATCGGAACTCGA                   CTGGAGAGAAGGACCAGCTCGAATGAGGAAACGCATCAAACGCTTGTCTCCTTTGGAG                   GCCCTCAGCTCAGGAAGGCACAAGGAAAGCCAAGACAAAAATGATCATATTTCTCAAA                   CAAATGCTGAAAACCAAGATGAACTGACACTGAGGGAGGCTGAGGGCGAGCCGGACGA                   GGTGGGGGTGGACTGCACCCAGCTCACCTTCTTCCCAGCCTTACACGAAAGTCTGCAC                   TCAGAAGACTTCTTGGAACTGTGTCGGGAAAGACAAGTTATTTTACAAGAGCTTCTTG                   ATAAAGAAAAGGTGACGCAGAAGTTCTCCCTGGTGATTGTGCAGGGCCACCTGGTGTC                   AGAAGGGCTCCTGCTTTTTGGCCACCAACACTTCTACATCTGCGAGAACTTCACACTG                   TCTCCCACGGGTGATGTCTACTGTACCCGTCACTGCTTATCCAACATCAGCGATCCGT                   TCATTTTCAACCTGTGCACCAAAGACAGGTCCACTGACCATTACTCGTGCCAGTCCCA                   CAGCTACGCTGACATGCGGGAGCTACGGCAGGCTCGCTTCCTCCTGCAGGACATCGCC                   CTGGAGATCTTCTTCCACAATGGATATTCCAAGTTTCTTGTCTTCTACAACAATGATC                   GGAGTAAGCCCTTTAAAACCTTCTGCTCTTTCCAACCCAGCCTGAAGGGGAAAGCCAC                   CTCGGAGGACACCCTCAATCTAAGGAGATACCCCCCCTCTGACACCATCATGCTGCAG                   AAGTGGCAGAAAAGGGACATCAGCAATTTTGAGTATCTCATCTACCTCAACACCGCGG                   CTGGGAGAACCTGCAATGACTACATGCAGTACCCAGTGTTCCCCTGGGTCCTCGCAGA                   CTACACCTCAGACACATTGAACTTGGCAAATCCGAAGATTTTCCGGGATCTTTCAAAG                   CCCATGGGGGCTCAGACCAAGGAAAGCAAGCTGAAATTTATCCAGAGGTTTAAAGAAG                   TTGAGAAUXCTGAAGGAGACATGACTGTCCACTGCCACTACTACACCCACTACTCCTC                   GGCCATCATCGTGGCCTCCTACCTGGTCCGGATGCCACCCTTCACCCAGGCCTTCTGC                   GCTCTGCAGGGCGGAAGCTTCGACGTGGCAGACAGAATGTTCCACAGTGTGAAGAGCA                   CGTGGGAGTCGGCCTCCAGAGAGAACATGAGTGACGTCAGGGAGCTGACCCCAGAGTT                   CTTCTACCTGCCTGAGTTCTTAACCAACTGCAACGGGGTAGAGTTCGGCTGCGTGCAG                   GACGGGACTGTGCTAGGAGACGTGCAGCTCCCTCCCTGGGCTGATGGGGACCCTCGGA                   AATTCATCAGCCTGCACAGAAAGGCCCTGGAAAGTGACTTTGTCAGTGCCAACCTCCA                   CCATTGGATAGACCTTATTTTTGGGTACAAGCAGCAGGGGCCAGCCGCAGTGGATGCT                   GTTAATATCTTCCACCCCTACTTCTACGGTGACAGAATGGACCTCAGCAGCATCACTG                   ACCCCCTCATCAAAAGCACCATCCTGGGGTTTGTCAGCAACTTTGGACAGGTGCCCAA                   ACAGCTCTTTACCAAACCTCACCCAGCCAGGACTGCAGCAGGGAAGCCTCTGCCTGGA                   AAGGATATCTCCACCCCCGTGAGCCTGCCTGGCCACCCACAGCCCTTTTTCTACAGCC                   TGCAGTCGCTGAGGCCCTCCCAGGTCACGGTCAAAGATATGTACCTCTTTTCTCTAGG                   CTCAGAGTCCCCCAAAGGGGCCATTGGCCACATTGTCTCTACTGAGAAGACCATTCTG                   GCTGTAGAGAGGAACAAAGTGCTGCTGCCTCCTCTCTGGAACAGGACCTTCAGCTGCG                   GCTTTGATGACTTCAGCTGCTGCTTGGGGAGCTACGGCTCCGACAAGGTCCTGATGAC                   ATTCGAGAACCTGGCTGCCTGGGGCCGCTGTCTGTGCGCCGTGTGCCCATCCCCAACA                   ACGATTGTCACCTCTGGGACCAGCACTGTGGTGTGTGTGTGGGAGCTCAGCATGACCA                   AAGGCCGCCCGAGGCGCTTGCGCCTCCGGCAGGCCTTGTATGGACACACACAGGCTGT                   CACGTGCCTGGCAGCGTCAGTCACCTTCAGCCTCCTGGTGAGCGGCTCCCAGGACTGC                   ACCTGTATCCTGTGGGATCTGGACCACCTCACCCACGTGACCCGCCTGCCCCCCCATC                   GGGAAGGCATCTCAGCCATCACCATCAGTGACGTCTCAGGCACCATTGTCTCCTGTGC                   GGGAGCACACTTGTCCCTGTGGAATCTCAATGGACAGCCCCTGGCCAGCATCACCACA                   GCCTGGGGCCCAGAAGGAGCCATAACCTGTTGCTGCCTGATGGAGGGCCCAGCATGGG                   ACACAAGCCAGATCATCATCACCGGGAGTCAAGACGGCATGGTCCGGGTTTGGAAGAC                   TGAGGATGTGAAGATGTCTGTTCCTCGACGGCCAGCAGGAGAGGAGCCCCTGGCTCAG                   CCTCCAAGCCCAAGAGGCCACAAGTGGGAGAAGAACCTGGCCTTGAGTCGAGAGCTGG                   ACGTTAGCATTGCTTTGACAGGGAAGCCCAGCAAAACCAGCCCCGCAGTGACTGCTCT                   GGCCGTGTCCAGAAACCACACCAAACTCCTGGTTGGTGATGAGAGGGGGAGAATATTC                   TGCTGGTCTGCAGATGGG TAG   GAAGAGAGAGGCA                                           ORF Start: ATG at 7   ORF Stop: TAG at 4021                                         SEQ ID NO 10   1338 aa   MW at 150546.1 kD                             NOV2a,   MRQLSHRGWAPREGKIVSSPHCWQMRHKCPSQAREAVGTGCTRWPCGCCLSPGLCFQA           CG122729-01       Protein Sequence   SPDHATSQQKRDFQSEVLLSAMELFHMTSGGDAAMFRDGKEPQPSAEAAAAPSLANIS                   CFTQKLVEKLYSGMFSADPRHILLFILEHIMVVIETASSQRDTVLSTLYSSLNKVILY                   CLSKPQQSLSECLGLLSILGFLQEHWDVVFATYNSNISFLLCLMHCLLLLNERSYPEG                   FGLEPKPRMSTYHQVFLSPNEDVKEKREDLPSLSDVQHNIQKTVQTLWQQLVAQRQQT                   LEDAFKIDLSVKPGEREVKIEEVTPLWEETMLKAWQHYLASEKKSLASRSNVAHHSKV                   TLWSGSLSSAMKLMPGRQAKDPECKTEDFVSCIENYRRRGQELYASLYKDHVQRRKCG                   NIKAANAWARIQEQLFGELGLWSQGEETKPCSPWELDWREGPARMRKRIKRLSPLEAL                   SSGRHKESQDKNDHISQTNAENQDELTLREAEGEPDEVGVDCTQLTFFPALHESLHSE                   DFLELCRERQVILQELLDKEKVTQKFSLVIVQGHLVSEGVLLFGHQHFYICENFTLSP                   TGDVYCTRHCLSNISDPFIFNLCSKDRSTDHYSCQCHSYADMRELRQARFLLQDIALE                   IFFHNGYSKFLVFYNNDRSKAFKSFCSFQPSLKGKATSEDTLNLRRYPGSDRIMLQKW                   QKRDTSNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPM                   GAQTKERKLKFIQRFKEVEKTEGDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCAL                   QGGSFDVADRMFHSVKSTWESASRENNSDVRELTPEFFYLPEFLTNCNGVEFGCVQDG                   TVLGDVQLPPWADGDPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVN                   IFHPYFYGDRMDLSSITDPLIKSTILGFVSNFGQVPKQLFTKPHPARTAAGKPLPGKD                   ISTPVSLPGHPQPFFYSLQSLRPSQVTVKDMYLFSLGSESPKGATGHIVSTEKTILAV                   ERNKVLLPPLWNRTFSWGFDDFSCCLGSYGSDKVLMTFENLAAWGRCLCALCPSPTTI                   VTSGTSTVVCVWELSMTKGRPRGLRLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTC                   ILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGAHLSLWNVNGQPLASITTAW                   GPEGAITCCCLMEGPAWDTSQIIITGSQDGMVRVWKTEDVKMSVPGRPAGEEPLAQPP                   SPRGHKWEKNLALSRELDVSIALTGKPSKTSPAVTALAVSRNHTKLLVGDERGRIFCW                   SADG                  
 
     [0343] Further analysis of the NOV2a protein yielded the following properties shown in Table 2B.  
               TABLE 2B                       Protein Sequence Properties NOV2a                                                PSort   0.9000 probability located in Golgi body; 0.7900           analysis:   probability located in plasma membrane; 0.6000               probability located in nucleus; 0.5147 probability               located in microbody (peroxisome)           SignalP   No Known Signal Sequence Indicated           analysis:                      
 
     [0344] A search of the NOV2a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 2C.  
               TABLE 2C                          Geneseq Results for NOV2a                                     Protein/       Identities/               Organism/   NOV2a   Similarities           Length   Residues/   for the       Geneseq   [Patent #,   Match   Matched   Expect       Identifier   Date]   Residues   Region   Value                                         AAY79179   Haematopoietic stem   675 . . . 1329    563/656 (85%)   0.0           cell specific   1 . . . 656    603/656 (91%)           protein -  Mus               musculus , 693 aa.           [WO200011168-A2,           02 MAR. 2000]       ABB64158   Drosophila   54 . . . 1262    450/1303 (34%)    0.0           melanogaster   1758 . . . 3021     674/1303 (51%)            polypeptide SEQ           ID NO 19266 -             Drosophila               melanogaster ,           3309 aa.           [WO200171042-A2,           27 SEP. 2001]       AAR99800   NTII-1 nerve   649 . . . 1269    334/633 (52%)   0.0           protein, facilitates   4 . . . 621    441/633 (68%)           regeneration of           nerve cells - Homo               sapiens , 887 aa.           [WO9617865-A2,           13 JUN. 1996]       AAM40075   Human polypeptide   1017 . . . 1338      322/322 (100%)   0.0           SEQ ID NO   1 . . . 322     322/322 (100%)           3220 - homo sapiens ,           322 aa.           [WO200153312-A1,           26 JUL. 2001]       AAM41861   Human polypeptide   1016 . . . 1338     283/339 (83%)   e−160           SEQ ID NO6792 -  Homo     9 . . . 331    290/339 (85%)             sapiens , 346 aa.           [WO200153312-A1,           26 JUL. 2001]                  
 
     [0345] In a BLAST search of public sequence datbases, the NOV2a protein was found to have homology to the proteins shown in the BLASTP data in Table 2D.  
               TABLE 2D                          Public BLASTP Results for NOV2a                                             Identities/                   NOV2a   Similarities       Protein   Protein/   Residues/   for the       Accession   Organism/   Match   Matched   Expect       Number   Length   Residues   Portion   Value                                         Q9HCG5   KIAA1607 protein -   69 . . . 1338    1268/1270 (99%)   0.0             Homo sapiens     1 . . . 1270   1270/1270 (99%)           (Human), 1270 aa           (fragment).       Q8TEN7   FLJ00156 protein -   57 . . . 1288    1212/1237 (97%)   0.0             Homo sapiens     614 . . . 1850    1218/1237 (97%)           (Human), 1887 aa           (fragment).       BAA76837   KIAA0993 protein -   49 . . . 1269     498/1314 (37%)   0.0             Homo sapiens     5 . . . 1288    747/1314 (55%)           (Human), 1556 aa           (fragment).       Q96N85   CDNA FLJ31244 fis,   708 . . . 1335     339/649 (52%)   0.0           clone KIDNE2005042,   1 . . . 634     450/649 (69%)           moderately similar           to lysosomal           trafficking           regulator - Homo               sapiens             (Human), 722 aa.       Q96BE1   Hypothetical   1019 . . . 1338      319/320 (99%)   0.0           34.6 kDa protein -   4 . . . 323     319/320 (99%)             Homo sapiens             (Human), 323 aa           (fragment).                  
 
     [0346] PFam analysis indicates that the NOV2a protein contains the domains shown in the Table 2E.  
               TABLE 2E                          Domain Analysis of NOV2a                                     Identities/                   Similarities           NOV2a Match   for the   Expect       Pfam Domain   Region   Matched Region   Value               Beach   693 . . . 975   174/287 (61%)    1.8e−181               240/287 (84%)        WD40   1128 . . . 1164   16/37 (43%)   0.00021               28/37 (76%)       WD40   1213 . . . 1254   11/42 (26%)   0.25               32/42 (76%)                  
 
     Example 3  
     [0347] The NOV3 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 3A.  
               TABLE 3A                       NOV3 Sequence Analysis                                                    SEQ ID NO:11   552 bp                             NOV3a,     GTGAC   ATG TTGGGCTGTGGGATCCCAGCGCTGGGCCTGCTCCTGCTGCTGCAGGGCTC           CG122777-01       DNA Sequence   GGCAGACGGAAATGGAATCCAGGGATTCTTCTACCCATGGAGTTCCCCAGGCTGTGAG                   GGTGACATATGGGACCGGGAGAGCTGTGGGGGCCAGGCGGCCATCGATAGCCCCAACC                   TCTGCCTGCGTCTCCGGTGCTGCTACCGCAATGGGGTCTGCTACCACCAGCGTCCAGA                   CGAAAACGTGCGGAGGAAGCACATGTGGCCGCTGGTCTGGACGTGCAGCGGCCTCCTC                   CTCCTGAGCTGCAGCATCTGCTTGTTCTGGTGGGCCAAGCGCCGGGACGTGCTGCATA                   TGCCCGGTTTCCTGGCGGGTCCGTGTGACATGTCCAAGTCCGTCTCGCTGCTCTCCAA                   GCACCGAGGGACCAAGAAGACGCCGTCCACGGGCAGCGTGCCAGTCGCCCTGTCCAAA                   GAGTCCAGGGATGTGGAGGGAGGCACCGAGGGGGAAGGGACGGAGGAGGGTGAGGAGA                   CAGAGGGCGAGGAAGAGGAGGATTAGGGGA                                         ORF Start: ATG at 6   ORF Stop: TAG at 546                                         SEQ ID NO: 12   180 aa   Mw at 19698.1 kD                             NOV3a,   MLGCGIPALGLLLLLQGSADGNGIQGFFYPWSSPGCEGDIWDRESCGGQAAIDSPNLC           CG122777-01       Protein Sequence   LRLRCCYRNGVCYHQRPDENVRRKHMWALVWTCSGLLLLSCSICLFWWAKRRDVLHMP                   GFLAGPCDMSKSVSLLSKHRGTKKTPSTGSVPVALSKESRDVEGGTEGEGTEEGEETE                   GEEEED                  
 
     [0348] Further analysis of the NOV3a protein yielded the following properties shown in Table 3B.  
               TABLE 3B                       Protein Sequence Properties NOV3a                                        PSort   0.4600 probability located in plasma membrane; 0.1000       analysis:   probability located in endoplasmic reticulum (membrane);           0.1000 probability located in endoplasmic reticulum           (lumen); 0.1000 probability located in outside       SignalP   Cleavage site between residues 22 and 23       analysis:                  
 
     [0349] A search of the NOV3a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 3C.  
               TABLE 3C                          Geneseq Results for NOV3a                                         NOV3a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAW75084   Human secreted protein encoded by    1 . . . 180   177/180 (98%)     e−105           gene 28 clone HHFGL62 -  Homo      1 . . . 177   177/180 (98%)              sapiens , 178 aa. [WO9839446-A2,           11 SEP. 1998]       AAW75146   Human secreted protein encoded by    1 . . . 52   48/52 (92%)   2e−21           gene 28 clone HHFGL62 -  Homo      1 . . . 49   48/52 (92%)             sapiens , 50 aa. [WO9839446-A2,           11 SEP. 1998]       ABP25902   Streptococcus polypeptide SEQ ID   110 . . . 177   25/72 (34%)   1.0           NO 980 -  Streptococcus agalactiae ,   432 . . . 502   31/72 (42%)           1266 aa. [WO200234771-A2,           02 MAY 2002]       ABP25903   Streptococcus polypeptide SEQ ID   110 . . . 177   24/72 (33%)   1.3           NO 982 -  Streptococcus pyogenes ,   423 . . . 493   31/72 (42%)           1257 aa. [WO200234771-A2,           02 MAY 2002]       AAO12986   Human polypeptide SEQ ID NO   124 . . . 179   20/56 (35%)   1.3           26878 -  Homo sapiens , 984 aa.   271 . . . 326   25/56 (43%)           [WO200164835-A2, 07 SEP. 2001]                  
 
     [0350]               TABLE 3D                          Public BLASTP Results for NOV3a                                             Identities/                   NOV3a   Similarities       Protein       Residues/   for the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q8WZ59   MDAC1 -  Homo sapiens  (Human),   1 . . . 180   177/180 (98%)     e−105           177 aa.   1 . . . 177   177/180 (98%)        Q9D2E9   4930572D21Rik protein -  Mus     1 . . . 177   112/178 (62%)    4e−60             musculus  (Mouse), 166 aa.   1 . . . 166   129/178 (71%)        AAH27748   Similar to complement component 8,   36 . . . 70    16/35 (45%)   2.3           alpha polypeptide- Mus musculus     74 . . . 102    18/35 (50%)           (Mouse), 587 aa.       AAL96855   Putative   110 . . . 177    24/72 (33%)   3.1           phosphoribosylformylglycinamidine   423 . . . 493    31/72 (42%)           synthase II -  Streptococcus pyogenes             (serotype M18), 1257 aa.       Q9A1Z2   Putative   110 . . . 177    24/72 (33%)   3.1           phosphoribosylformylglycinamidine   423 . . . 493    31/72 (42%)           synthase II -  Streptococcus pyogenes ,           1257 aa.                    
     [0351] PFam analysis indicates that the NOV3a protein contains the domains shown in the Table 3E.  
               TABLE 3E                          Domain Analysis of NOV3a                                     Identities/                   Similarities           NOV3a Match   for the       Pfam Domain   Region   Matched Region   Expect Value                         No Significant Matches Found                  
 
     Example 4  
     [0352] The NOV4 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 4A.  
               TABLE 4A                       NOV4 Sequence Analysis                                                    SEQ ID NO: 13   994 bp                             NOV4a,     TGTCGCCCCATCCCTGCGCGCCCAGCCTGCCAAGCAGCGTGCCCCGGTTGCAGGCGTC             CG124229-01       DNA Sequence     ATG CAGCGGGCGCGACCCACGCTCTGGGCCGCTGCGCTGACTCTGCTGGTGCTGCTCC                   GCGGGCCGCCGGTGGCGCGGGCTGGCGCGAGCTCGGGGGGCTTGGGTCCCGTGGTGCG                   CTGCGAGCCGTGCGACGCGCGTGCACTGGCCCAGTGCGCGCCTCCGCCCGCCGTGTGC                   GCGGAGCTGGTGCGCGAGCCGGGCTQCGGCTGCTGCCTGACGTGCGCACTGACCGAGG                   GCCAGCCGTGCGGCATCTACACCGAGCGCTGTGGCTCCGGCCTTCGCTGCCAGCCGTC                   GCCCGACGAGGCGCGACCGCTGCAGGCGCTGCTGGACGGCCGCGGGCTCTGCGTCAAC                   GCTAGTGCCGTCAGCCGCCTGCGCGCCTACCTGCTGCCACCCCCGCCAGCTCCAGGTG                   AGCCGCCCGCTCCAGGAAATGCTAGTGAGTCGGAGGAAGACCGCAGCGCCGCCAGTGT                   GGAGAGCCCGTCCGTCTCCAGCACGCACCGGGTGTCTGATCCCAAGTTCCACCCCCTC                   CATTCAAAGATAATCATCATCAAGAAAGGGCATGCTAAAGACAGCCAGCGCTACAAAG                   TTGACTACGAGTCTCAGAGCACACATACCCAGAACTTCTCCTCCGAGTCCAAGCGGGA                   GACAGAATATGGTCCCTGCCCTAGAGAAATGGAAOACACACTGAATCACCTGAAGTTC                   CTCAATGTGCTGAGTCCCAGGGGTGTACACATTCCCAACTGTGACAAGAAGGGATTTT                   ATAAGAAAAAGCAGTGTCGCCCTTCCAAAGGCAGGAAGCGGGGCTTCTGCTGGTGTGT                   GGATAAGTATGGGCAGCCTCTCCCAGGCTACACCACCAAGGGGAAGGAGGACGTGCAC                   TGCTACAGCATGCAGAGCAAGTAGACGCCTGCCGCAAGGTTAATGTGGAGCTCAAATA                     TGCCTTAT                                           ORF Start: ATG at 59   ORF Stop: TAG at 950                                         SEQ ID NO 14   297 aa   MW at 32208.4 kD                             NOV4a,   MQRARPTLWAAALTLLVLLRGPPVARAGASSGGLGPVVRCEPCDARALAQCAPPPAVC           CG124229-01       Protein Sequence   AELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVN                   ASAVSRLRAYLLPAPPAPGEPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPL                   HSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNRLKF                   LNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVH                   CYSMQSK                  
 
     [0353] Further analysis of the NOV4a protein yielded the following properties shown in Table 4B.  
               TABLE 4B                       Protein Sequence Properties NOV4a                                        PSort   0.3703 probability located in outside; 0.1900 probability       analysis:   located in lysosome (lumen); 0.1080 probability located in           nucleus; 0.1000 probability located in endoplasmic           reticulum (membrane)       SignalP   Cleavage site between residues 28 and 29       analysis:                  
 
     [0354] A search of the NOV4a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 4C.  
               TABLE 4C                          Geneseq Results for NOV4a                                             Identities/                   NOV4a   Similarities               Residues/   for the       Geneseq   Protein/Organism/Length   Match   Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABB09209   Human ibp3 CNN family protein   1 . . . 297   291/297 (97%)   e−175           sequence SEQ ID NO: 19 -  Homo     1 . . . 291   291/297 (97%)             sapiens , 291 aa. [US2002049304-           A1, 25 APR. 2002]       AAU85512   Clone #19095 (L549S) of lung   1 . . . 297   291/297 (97%)   e−175           tumour protein -  Homo sapiens ,   1 . . . 291   291/297 (97%)           291 aa. [WO200204514-A2, 17           JAN. 2002]       AAB59880   IGFBP-3 protein -  Homo sapiens ,   1 . . . 297   291/297 (97%)   e−175           291 aa. [WO200078341-A1, 28   1 . . . 291   291/297 (97%)           DEC. 2000]       AAB76857   Human lung tumour protein related   1 . . . 297   291/297 (97%)   e−175           protein sequence SEQ ID NO: 333 -   1 . . . 291   291/297 (97%)             Homo sapiens , 291 aa.           [WO200100828-A2, 04 JAN. 2001]       AAR89273   Insulin like growth factor binding   1 . . . 297   291/297 (97%)   e−175           protein-3 -  Homo sapiens , 291 aa.   1 . . . 291   291/297 (97%)           [WO9601636-A1, 25 JAN. 1996]                  
 
     [0355] In a BLAST search of public sequence datbases, the NOV4a protein was found to have homology to the proteins shown in the BLASTP data in Table 4D.  
               TABLE 4D                          Public BLASTP Results for NOV4a                                             Identities/                   NOV4a   Similarities       Protein       Residues/   for the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               P17936   Insulin-like growth factor binding   1 . . . 297   291/297 (97%)   e−174           protein 3 precursor (IGFBP-3) (IBP-   1 . . . 291   291/297 (97%)           3) (IGF-binding protein 3) -  Homo               sapiens  (Human), 291 aa.       Q9TTIO   Insulin-like growth factor-binding   1 . . . 297   243/299 (81%)   e−147           protein 3 -  Sus scrofa  (Pig), 293 aa.   1 . . . 293   260/299 (86%)       Q9GJV5   Insulin-like growth factor binding   1 . . . 297   242/299 (80%)   e−145           protein-3 -  Bos taurus  (Bovine), 291   1 . . . 291   257/299 (85%)           aa.       P20959   Insulin-like growth factor binding   1 . . . 297   239/299 (79%)   e−143           protein 3 precursor (IGFBP-3) (IBP-   1 . . . 291   255/299 (84%)           3) (IGF-binding protein 3) -  Bos               taurus  (Bovine), 291 aa.       P15473   Insulin-like growth factor binding   1 . . . 297   239/299 (79%)   e−142           protein 3 precursor (IGFBP-3) (IBP-   1 . . . 292   255/299 (84%)           3) (IGF-binding protein 3) -  Rattus               norvegicus  (Rat), 292 aa.                  
 
     [0356] PFam analysis indicates that the NOV4a protein contains the domains shown in the Table 4E.  
               TABLE 4E                          Domain Analysis of NOV4a                                     Identities/                   Similarities       Pfam Domain   NOV4a Match Region   for the Matched Region   Expect Value               IGFBP    40 . . . 99   39/84 (46%)   2.1e−26               56/84 (67%)       thyroglobulin_1   219 . . . 291   37/81 (46%)   1.6e−32               66/81 (81%)                  
 
     Example 5  
     [0357] The NOV5 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 5A.  
               TABLE 5A                       NOV5 Sequence Analysis                                                    SEQ ID NO: 15   1854 bp                             NOV5a,     GGACGAAGGAAACGAACGAGGGGGAGGGAGGTCCCTGTTTTGGAGGAGCTAGGAGCGT             CG124445-02       DNA Sequence     TGCCGGCCCCTGAAGTGGAGCGAGAGGGAGGTCCTTCGCCGTTTCTCCTGCCAGGGGA                       GGTCCCGGCTTCCCGTGGAGGCTCCGGACCAAGCCCCTTCAGCTTCTCCCTCCGGATC                       GATGTGCTGCTGTTAACCCGTGAGGAGGCGGCGGCGGCCACCAGCGGCAGCGGAAG   ATG                     GTGTTGCTGAGAGTGTTAATTCTGCTCCTCTCCTGGGCGGCGGGGATGGGAGGTCAGT                   ATGGGAATCCTTTAAATAAATATATCAGACATTATGAAGGATTATCTTACAATGTGGA                   TTCATTACACCAAAAACACCAGCGTGCCAAAAGAGCAGTCTCTCACATTACTTTTGCT                   CACGAAGTTGGACATAACTTTGGATCCCCACATGATTCTGGAACAGAGTGCACACCAG                   GAGAATCTAAGAATTTGGGTCAAAAAGAAAATGGCAATTACATCATGTATGCAAGAGC                   AACATCTGGGGACAAACTTAACAACAATAAATTCTCACTCTGTAGTATTAGAAATATA                   AGCCAAGTTCTTGAGAAGAAGAGAAACAACTGTTTTGTTGAATCTGGCCAACCTATTT                   TAAAGATGAATCCTGCTTCGATGCAAATCAACCAGAGCGAAGAAAATGCAAACTGAAA                   CCTGGGAAACAGTGCAGTCCAAGTCAAGGTCCTTGTTGTACAGCACAGTGTGCATTCA                   AGTCAAAGTCTGAGAAGTGTCGGGATGATTCAGACTGTGCAAGGGAAGGAATATGTAA                   TGGCTTCACAGCTCTCTGCCCAGCATCTGACCCTAAACCAAACTTCACAGACTGTAAT                   AGGCATACACAACTGTCCATTAATGGGCAATGTGCAGGTTCTATCTGTGAGAAATATG                   GCTTAGAGGAGTGTACGTGTGCCAGTTCTGATGGCAAAGATGATAAAGAATTATGCCA                   TGTATGCTGTATGAAGAAAATGGACCCATCAACTTGTGCCAGTACAGGGTCTGTGCAG                   TGGAGTAGGCACTTCAGTGGTCGAACCATCACCCTGCAACCTGGATCCCCTTGCAACG                   ATTTTAGAGGTTACTGTGATGTTTTCATGCGGTGCAGATTAGTAGATGCTGATGGTCC                   TCTAGCTAGGCTTAAAAAAGCAATTTTTAGTCCAGAGCTCTATGAAAACATTGCTGAA                   TGGATTGTGGCTCATTGGTGGGCAGTATTACTTATGGGAATTGCTCTGATCATGCTAA                   TGGCTGGATTTATTAAGATATGCAGTGTTCATACTCCAAGTAGTAATCCAAAGTTGCC                   TCCTCCTAAACCACTTCCAGGCACTTTAAAGAGGAGGAGACCTCCACAGCCCATTCAG                   CAACCCCAGCGTCAGCGGCCCCGAGAGACTTATCAAATGGGACACATGAGACGC TAA   C                       TGCAGCTTTTGCCTTGGTTCTTCCTAGTGCCTACAATGGGAAAACTTCACTCCAAAGA                       GAAACCTATTAAGTCATCATCTCCAAACTAAACCCTCACAAGTAACAGTTGAAGAAAA                       AATGGCAAGAGATCATATCCTCAGACCAGGTGGAATTACTTAAATTTTAAAGCCTGAA                       AATTCCAATTTGGGGGTGGGAGGTGGAAAAGGAACCCAATTTTCTTATGAACAGATAT                       TTTTAACTTAATGGCACAAAGTCTTAGAATATTATTATGTGCCCCGTGTTCCCTGTTC                       TTCGTTGCTGCATTTTCTTCACTTGCAGGCAAACTTGGCTCTCAATAAACTTTTCG                                           ORF Start: ATG at 230   ORF Stop: TAA at 1505                                         SEQ ID NO: 16   425 aa   MW at 47237.5 kD                             NOV5a,   IVIVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHITF           CG124445-02       Protein Sequence   AHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCS IRN                   ISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKL~                   KPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDC                   NRHTQVCINGQCACSICEKYGLEECTCASSDGKDDKELCHVCCMKKNDPSTCASTGSV                   QWSRHFSGRTITLQPGSPCNDFRGYCDVPMRCRLVDADGPLARLKKAIFSPELYENIA                   EWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPI                   QQPQRQRPRESYQMGHMRR                  
 
     [0358] Further analysis of the NOV 5protein yielded the following properties shown in   
               TABLE 5B                       Table 5B. Protein Sequence Properties NOV5a                                        PSort   0.4600 probability located in plasma membrane;       analysis:   0.1800 probability located in nucleus; 0.1000 probability           located in endoplasmic reticulum (membrane); 0.1000           probability located in endoplasmic reticulum (lumen)       SignalP   Cleavage site between residues 20 and 21       analysis:                  
 
     [0359] A search of the NOV5a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 5C.  
               TABLE 5C                          Geneseq Results for NOV5a                                         NOV5a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAB62520   Human ADAM10 polypeptide -   8 . . . 425   381/422 (90%)   0.0             Homo sapiens , 748 aa.   327 . . . 748    389/422 (91%)           [US6228648-B1, 08 MAY 2001]       AAG64048   Human ADAM10 protein -  Homo     8 . . . 425   381/422 (90%)   0.0             sapiens , 748 aa. [JP2001128677-A,   327 . . . 748    389/422 (91%)           15 MAY 2001]       AAY79033   Human Kuz amino acid sequence -   8 . . . 425   381/422 (90%)   0.0             Homo sapiens , 691 aa.   270 . . . 691    389/422 (91%)           [WO200002897-A2, 20 JAN. 2000]       AAY16776   Human disintegrin metalloprotease   8 . . . 425   381/422 (90%)   0.0           (KUZ) polypeptide -  Homo sapiens ,   327 . . . 748    389/422 (91%)           748 aa. [EP921197-A2, 09 JUN.           1999]       AAW56132     Homo sapiens  transmembrane KUZ   8 . . . 425   381/422 (90%)   0.0           protein -  Homo sapiens , 748 aa.   327 . . . 748    389/422 (91%)           [WO9808933-A1, 05 MAR. 1998]                  
 
     [0360] In a BLAST search of public sequence datbases, the NOV5a protein was found to have homology to the proteins shown in the BLASTP data in Table 5D.  
               TABLE 5D                          Public BLASTP Results for NOV5a                                             Identities/                   NOV5a   Similarities       Protein       Residues/   for the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value                                         S52920   disintegrin (EC 3.4.24.-) - human,   8 . . . 425   381/422 (90%)   0.0           491 aa (fragment).   70 . . . 491    389/422 (91%)       Q10742   Disintegrin-metalloprotease MADM -   8 . . . 425   381/422 (90%)   0.0             Homo sapiens  (Human), 691 aa   270 . . . 691    389/422 (91%)           (fragment).       O14672   ADAM10 -  Homo sapiens  (Human),   8 . . . 425   381/422 (90%)   0.0           748 aa.   327 . . . 748    389/422 (91%)       Q10743   Disintegrin-metalloprotease   8 . . . 425   371/422 (87%)   0.0           precursor (EC 3.4.24.-)(Myelin-   123 . . . 544    386/422 (90%)           associated metalloproteinase)           (MADM)- Rattus norvegicus  (Rat),           544 aa(fragment).       O35598   Kuzbanian -  Mus musculus  (Mouse),   8 . . . 425   370/422 (87%)   0.0           749 aa.   328 . . . 749    385/422 (90%)                  
 
     [0361] PFam analysis indicates that the NOV5a protein contains the domains shown in the Table 5E.  
               TABLE 5E                          Domain Analysis of NOV5a                                             Identities/                       Similarities                   for the           Pfam   NOV5a Match   Matched   Expect           Domain   Region   Region   Value                                                 squash   200 . . . 221    8/22 (36%)   0.25                   12/22 (55%)           disintegrin   143 . . . 226   33/85 (39%)   2.2e−08                   54/85 (64%)                      
 
     Example 6  
     [0362] The NOV6 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 6A.  
               TABLE 6A                       NOV6 Sequence Analysis                                                    SEQ ID NO:17   725 bp                             NOV6a,     GAGGTAGGTCCAGGACGGGCGCACAGCAGCAGCCGAGGCTGGCCGGGAGAGGGAGGAA             CG124590-02       DNA Sequence     GAGG   ATG GCAGGGCCACGCCGCAGCCCATGGGCCAGGCTGCTCCTGGCAGCCTTGATC                   AGCGTCACCCTCTCTGGGACCTTGGCAAACCGCTGCAAGAAGGCCCCAGTGAAGAGCT                   GCACGGAGTGTGTCCGTGTGGATAAGGACTGCGCCTACTGCGCAGACGAGATGTTCAG                   GGACCGGCGCTGCAACACCCAGGCGGAGCTGCTGGCCGCGGGCTGCCAGCGGGAGAGC                   ATCGTGGTCATGGAGAGCAGCTTCCAAATCACAGAGGAGACCCAGATTGACACCACCC                   TGCGGCGCAGCCAGATGTCCCCCCAAGGCCTGCGGGTCCGTCTGCGGCCCGGTGAGGA                   GCGGCATTTTGAGCTGGAGGTGTTTGACCCACTGGACAGCCCCGTGGACCTGTACATC                   CTCATGGACTTCTCCAACTCCATGTCCGATGATCTGGACAACCTCAAGAAGATGGGGC                   AGAACCTGGCTCGGGTCCTGAGCCAGCTCACCAGCGCCACCGAGCCCTTCCTAGTGGA                   TGGGCCGACCCTGGGGGCCCAGCACCTGGAGGCAGGCGGCTCCCTCACCCGGCATGTG                   ACCCAGGAGTTTGTGAGCCGGACACTGACCACCAGCGGAACCCTTAGCACCCACATGG                   ACCAACAGTTCTTCCAAACT TGA   CCGCAC                                           ORF Start: ATG at 63   ORF Stop: TGA at 717                                         SEQ ID NO: 18   218 aa   MW at 24305.3 kD                             NOV6a,   MAGPRPSPWARLLLAALISVSLSGTLANRCKKAPVKSCTECVRVDKDCAYCADEMFRD           CG124590-02       Protein Sequence   RRCNTQAELLAAGCQRESIVVMESSFQITEETQIDTTLRRSQMSPQGLRVRLRPGEER                   HFELEVFEPLESPVDLYILMDFSNSMSDDLDNLKKMGQNLARVLSQLTSATEPFLVDG                   PTLGAQHLEAGGSLTRHVTQEFVSRTLTTSGTLSTHMDQQFFQT                  
 
     [0363] Further analysis of the NOV6a protein yielded the following properties shown in Table 6B.  
               TABLE 6B                       Protein Sequence Properties NOV6a                                        PSort   0.5135 probability located in outside; 0.1000 probability       analysis:   located in endoplasmic reticulum (membrane); 0.1000           probability located in endoplasmic reticulum (lumen);           0.1000 probability located in microbody (peroxisome)       SignalP   Cleavage site between residues 28 and 29       analysis:                  
 
     [0364] A search of the NOV6a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 6C.  
               TABLE 6C                          Geneseq Results for NOV6a                                             Identities/                   NOV6a   Similarities               Residues/   for the       Geneseq   Protein/Organism/Length   Match   Matched   Expect       Identifier   [Patent#, Date]   Residues   Region   Value               AAB68089   Amino acid sequence of the beta4   1 . . . 165   164/165 (99%)   2e−90           part of alpha6beta4 integrin -  Homo     1 . . . 165   164/165 (99%)             sapiens , 1875 aa. [WO200130854-           A2, 03 MAY 2001]       AAR55273   Beta subunit of integrin cell surface   1 . . . 165   164/165 (99%)   2e−90           receptor -  Homo sapiens , 1822 aa.   1 . . . 165   164/165 (99%)           [US5320942-A, 14 JUN. 1994]       AAM35512   Peptide #9549 encoded by probe for   89 . . . 156    68/68 (100%)   1e−32           measuring placental gene expression -   1 . . . 68    68/68 (100%)             Homo sapiens , 68 aa.           [WO200157272-A2, 09 AUG. 2001]       AAM20582   Peptide #7016 encoded by probe for   89 . . . 156    68/68 (100%)   1e−32           measuring cervical gene expression -   1 . . . 68    68/68 (100%)             Homo sapiens , 68 aa.           [WO200157278-A2, 09 AUG. 2001]       AAM75399   Human bone marrow expressed   89 . . . 156    68/68 (100%)   1e−32           probe encoded protein SEQ ID NO:   1 . . . 68    68/68 (100%)           35705 -  Homo sapiens , 68 aa.           [WO200157276-A2, 09 AUG. 2001]                  
 
     [0365] In a BLAST search of public sequence datbases, the NOV6a protein was found to have homology to the proteins shown in the BLASTP data in Table 6D.  
               TABLE 6D                          Public BLASTP Results for NOV6a                                             Identities/                   NOV6a   Similarities       Protein       Residues/   for the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               JC5545   integrin beta-4 precursor, splice   1 . . . 165   164/165 (99%)   4e−90           form E - human, 964 aa.   1 . . . 165   164/165 (99%)       A36429   integrin beta-4 chain precursor -   1 . . . 165   164/165 (99%)   4e−90           human, 1875 aa.   1 . . . 165   164/165 (99%)       P16144   Integrin beta-4 precursor (GP150)   1 . . . 165   164/165 (99%)   4e−90           (CD104 antigen) -  Homo sapiens     1 . . . 165   164/165 (99%)           (Human), 1822 aa.       Q64632   Integrin beta-4 precursor (GP150)   1 . . . 165   123/165 (74%)   5e−69           (CD104 antigen) -  Rattus     1 . . . 165   145/165 (87%)             norvegicus  (Rat), 1807 aa.       JN0786   integrin beta-4 chain precursor -   1 . . . 165   126/166 (75%)   1e−67           mouse, 1748 aa.   1 . . . 166   145/166 (86%)                  
 
     [0366] PFam analysis indicates that the NOV6a protein contains the domains shown in the Table 6E.  
               TABLE 6E                          Domain Analysis of NOV6a                                             Identities/                       Similarities                   for the           Pfam   NOV6a Match   Matched   Expect           Domain   Region   Region   Value                       integrin_B   37 . . . 165   65/143 (45%)   2.3e−89                   129/143 (90%)                       
 
     Example 7  
     [0367] The NOV7 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 7A.  
               TABLE 7A                       NOV7 Sequence Analysis                                                    SEQ ID NO:19   1140 bp                             NOV7a,     AGGACAACCCCAGCA   ATG TGGAGAAGCCTGGGGCTTGCCCTGGCTCTCTGTCTCCTCC           CG124916-01       DNA Sequence   CATCGGGAGGAACACAGAGCCAGGACCAAAGCTCCTTATGTAAGCAACCCCCAGCCTG                   GAGCATAAGAGATCAAGATCCAATGCTAAACTCCAATGGTTCAGTGACTGTGGTTGCT                   CTTCTTCAAGCCTCATTTTATGTATTTCTTCCCAAATATTTTAGATTAGAAGACCTGC                   GAGTAAAACTGAAGAAAGAAGGATATTCTAATATTTCTTATATTGTTGTTAATCATCA                   AGCAATCTCTTCTCGATTAAAATACACACATCTTAAGAATAAGGTTTCAGAGCATATT                   CCTGTTTATCAACAAGAAGAAAACCAAACAGATGTCTGGACTCTTTTAAATGGAAGCA                   AAGATGACTTCCTCATATATGATAGGTGTGGCCGTCTTGTATATCATCTTGGTTTGCC                   TTTTTCCTTCCTAACTTTCCCATATGTAGAAGAAGCCATTAAGATTGCTTACTGTGAA                   AAGAAATGTGGAAACTGCTCTCTCACGACTCTCAAAGATGAAGACTTTTGTAAACGTG                   TATCTTTGGCTACTGTGGATAAAACAGTTGAAACTCCATCGCCTCATTACCATCATGA                   GCATCATCACAATCATGGACATCAGCACCTTGGCAGCAGTGAGCTTTCAGAGAATCAC                   CAACCAGGAGCACCAAATGCTCCTACTCATCCTGCTCCTCCACGCCTTCATCACCACC                   ATAAGCACAAGGGTCAGCATAGGCAGGGTCACCCAGAGAACCGAGATATGCCAGCAAG                   TGAAGATTTACAAGATTTACAAAAGAAGCTCTGTCGAAAGAGATGTATAAATCAATTA                   CTCTGTAAATTGCCCACAGATTCAGAGTTGGCTCCTAGGAGC TGA   TGCTGCCATTGTC                       GACATCTGATATTTGAAAAAACAGGGTCTGCAATCACCTGACAGTGTAAAGAAAACCT                       CCCATCTTTATGTAGCTGACAGGGACTTCGGGCAGAGGAGAACATAACTGAATCTTGT                       CAGTGACGTTTGCCTCCAGCTGCCTGACAPATAAGTCAGCAGCTTATACCCACAGAAG                       CCAGTGCCAGTTGACGCTGAAAGAATCAGGCAAAAAAG                                           ORF Start: ATG at 16   ORF Stop: TGA at 913                                         SEQ ID NO 20   299 aa   MW at 34008.2 kD                             NOV7a,   MWRSLGLALALCLLPSGGTESQDQSSLCKQPPAWSIRDQDPMLNSNGSVTVVALLQAS           CG124916-01       Protein Sequence   FYVFLPKYFRLEDLRVKLKKEGYSNISYIVVNHQGISSRLKYTHLKNKVSEHIPVYQQ                   EENQTDVWTLLNGSKDDFLIYDRCGRLVYHLGLPFSFLTFPYVEEAIKIAYCEKKCGN                   CSLTTLKDEDFCKRVSLATVDKTVETPSPHYHHEHHHNHGHQHLGSSELSENQQPGAP                   NAPTHPAPPGLHHHHKHKGQHRQGHPENRDMPASEDLQDLQKKLCRKRCINQLLCKLP                   TDSELAPRS                  
 
     [0368] Further analysis of the NOV7a protein yielded the following properties shown in Table 7B.  
               TABLE 7B                       Protein Sequence Properties NOV7a                                        PSort   0.5135 probability located in outside; 0.1900 probability       analysis:   located in lysosome (lumen); 0.1000 probability located           in endoplasmic reticulum (membrane); 0.1000 probability           located in endoplasmic reticulum (lumen)       SignalP   Cleavage site between residues 22 and 23       analysis:                  
 
     [0369] A search of the NOV7a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 7C.  
               TABLE 7C                          Geneseq Results for NOV7a                                             Identities/                   NOV7a   Similarities               Residues/   for the       Geneseq   Protein/Organism/Length   Match   Matched   Expect       Identifier   [Patent#, Date]   Residues   Region   Value               AAU84306   Human endometrial cancer related   1 . . . 299   290/299 (96%)    e−176           protein, SEPP1 -  Homo sapiens , 381   1 . . . 299   294/299 (97%)               aa. [W0200209573-A2, 07 FEB.           2002]       AAB03188   Human selenoprotein P -  Homo     1 . . . 299   290/299 (96%)    e−176             sapiens , 381 aa. [WO200031131-   1 . . . 299   294/299 (97%)           A1, 02 JUN. 2000]       AAB57080   Human prostate cancer antigen   60 . . . 299    232/240 (96%)    e−142           protein sequence SEQ ID NO: 1658 -   1 . . . 240   236/240 (97%)             Homo sapiens , 240 aa.           [WO200055174-A1, 21 SEP. 2000]       AAG03755   Human secreted protein, SEQ ID   219 . . . 299    81/81 (100%)   8e−45           NO:7836 -  Homo sapiens , 110 aa.   30 . . . 110    81/81 (100%)           [EP1033401-A2, 06 SEP. 2000]       AAO06297   Human polypeptide SEQ ID NO   70 . . . 147    64/113 (56%)   8e−24           20189 -  Homo sapiens , 113 aa.   1 . . . 113   69/113 (60%)           [WO200164835-A2, 07 SEP. 2001]                  
 
     [0370] In a BLAST search of public sequence datbases, the NOV7a protein was found to have homology to the proteins shown in the BLASTP data in Table 7D.  
               TABLE 7D                          Public BLASTP Results for NOV7a                                             Identities/                   NOV7a   Similarities       Protein       Residues/   for the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               P49908   Selenoprotein P precursor (SeP) -   1 . . . 299   290/299 (96%)   e−176             Homo sapiens  (Human), 381   1 . . . 299   294/299 (97%)           aa.       Q9N2H6   Selenoprotein P -  Bos taurus     1 . . . 296   217/300 (72%)   e−124           (Bovine), 386 aa.   1 . . . 300   241/300 (80%)       P25236   Selenoprotein P precursor (SeP) -   1 . . . 299   215/304 (70%)   e−123             Rattus norvegicus  (Rat), 385   1 . . . 304   243/304 (79%)           aa.       AAA42129   Selenoprotein P precursor -   1 . . . 299   214/304 (70%)   e−122             Rattus norvegicus  (Rat), 385 aa.   1 . . . 304   242/304 (79%)       P70274   Selenoprotein P precursor (SeP) -   1 . . . 299   211/301 (70%)   e−121             Mus musculus  (Mouse), 380   1 . . . 299   244/301 (80%)           aa.                  
 
     [0371] PFam analysis indicates that the NOV7a protein contains the domains shown in the Table 7E.  
               TABLE 7E                          Domain Analysis of NOV7a                                             Identities/                       Similarities               NOV7a   for the           Pfam   Match   Matched   Expect           Domain   Region   Region   Value                                     No Significant Matches Found                      
 
     Example 8  
     [0372] The NOV8 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 8A.  
               TABLE 8A                       NOV8 Sequence Analysis                                                    SEQ ID NO 21   3123 bp                             NOV 8a,     GATTCCAAGTCGCTGCTGTGCAGAGCAGCAAGTGCTCCGTGCAGGGCTGTTGCTATCA             CG126224-01       DNA Sequence     CTTGGAGGTGAACAGCCTCTTTGCCGGTATTCAGTGAAGAAAGCAAGTCTAAATATGC                       AGTTCTCTCACTGGAGTGAAAGATGTTTGTTCATTTCTAATCAACT   ATG CTAGACAGC                   TGCAAGCTGAAAAGTGCCTGCAATTTGCCATTTATTTGTAATAAGAAAATAATAAACA                   CTGCTGGAACCAGTAATGCAGAAGTCCCCTTGGCTGATCCCGGAATGTACCAGCTGGA                   CATTACATTAAGAAGGGGTCAAAGTTTAGCTGCTCGAGATCGAGGAGGGACGAGTGAT                   CCATATGTGAAGTTTAAAATCGGAGGAAAAGAAGTTTTTAGAAGTAAGATAATACACA                   AGAACCTCAACCCTGTGTGGGAAGAAAAAGCTTGTATTCTGGTTGATCATCTTAGGGA                   GCCATTGTATATAAAGGTATTTGACTATGATTTTGGACTACAGGATGACTTTATGGGC                   TCAGCCTTTCTGGATCTGACACAATTGGAGTTAAACAGGCCCACAGATGTGACCCTTA                   CTCTGAAAGATCCTCATTATCCTGACCATGATCTTGGAATCATTTTGCTCTCAGTCAT                   CCTTACCCCTAAAGAAGGAGAGTCCAGGGAGTTTCAGACCCAAAGTTTACGCCTATCA                   GACCTACACAGAAAATCGCATCTTTGGAGAGGAATAGTCAGCATCACCTTGATTGAAG                   GGAGAGACCTCAAGGCCATGGATTCCAACGGGTTGAGCGATCCCTACGTGAAGTTCCG                   GCTTGGGCATCAGAAGTACAAGAGCAAGATTATGCCAAAAACGTTGAATCCTCAGTGG                   AGGGAACAATTTGATTTTCACCTTTATGAAGAAAGAGGAGGAGTCATTGATATCACTG                   CATGGGACAAAGATGCTGGGAAAAGGGATGATTTCATTGGCAGGTGCCAGGTCGACCT                   GTCAGCCCTCAGTAGGGAACAGACGCACAAGCTGGAGTTGCAGCTGGAAGAGGGTGAG                   GGACACCTGGTGCTGCTGGTCACTCTGACAGCATCAGCCACAGTCAGCATCTCTGACC                   TGTCTGTCAACTCCCTGGAGGACCAGAAGGAACGAGAGGAGATATTAAAGAGATATAG                   CCCATTGAGGATATTTCACAACCTGAGAGATGTGGGATTTCTCCAGGTGAAAGTCATC                   AGAGCGGAAGGGTTAATCGCTGCCGACGTCACTGGAAAAAGTGACCCATTTTGTGTGG                   TAGAACTGAACAAAGATAGACTGCTAACACATACTGTCTACAAAAATCTCAATCCTGA                   GTGGAATAAAGTCTTCACGTTCAACATTAAAGATATCCATTCAGTTCTTGAAGTGACA                   GTTTATGATGAAGATCGGGATCGAAGTGCTGACTTTCTGGGCAAAGTTGCTATACCAT                   TGCTGTCTATTCAAAATGGTGAACAGAAAGCCTACGTCTTGAAAAACAGGCAGCTGAC                   AGGGCCAACAAAGGGGGTCATCTATCTTGAAATAGATGTGATTTTTAATGCTGTGAAA                   GCCAGCTTACGAACATTAATACCCAAAGAACAGAAGTACATTGAAGAGGAAAACAGAC                   TCTCTAAACAGCTGCTACTAAGAAACTTTATCAGAATGAAACGTTGTGTCATGGTGCT                   GGTAAATGCTGCATACTACGTTAATAGTTGCTTTGATTGGGATTCACCCCCAAGGAGT                   CTCGCTGCTTTTGTGGTAGTGGAGGACATGCTAGAGGACGAGGAAGAAGAAGATGACA                   AAGATGACAAGGACAGTGPAAAAAAGGGATTTATAAATAAAATCTATGCCATCCAGGA                   GGTATGTGTCAGTGTCCAGAACATCCTAGATGAAGTGGCTTCCTTTGGCGAAAGGATA                   AAGAGTACTTTCAACTGGACTGTCCCATTCTTAAGCTGGCTGGCCATTGTAGCCCTCT                   GTGTGTTCACAGCCATCCTGTACTGCATTCCGCTGAGATACATTGTCCTTGTCTGGGC                   CATCAATAAATTTACAAAAAAGCTTCGCAGTCCATATGCAATTGATAACAATGAACTA                   CTTGACTTCCTTTCCAGAGTCCCTTCAGATGTACAAGTGGTGCAATACCAAGAACTGA   ee                    AACCAGATCCTTCTCATAGCCCATATAAAAGAAAGAAAAACAATCTTGGC TAG   CCAGC                       TCCCAGCACTGAGGAGACCAGCATCTGTTTGGGAAGATAAAAGAAAAAGCCCTCAGCC                       TCAGCAGCATTTCCTTTCTTTCTGCTTTTTATTTATTTTGCCTTTTTATCATGATCGA                       GAGAATCTGTAAATAGTGTACAAAGGCATATGTCTTTGAATATATACTTCTATTGTAC                       AGACTCAACTTGATAAAGGTTTTGCTACTGCTGTGTCAAAACCTTGTTAGCTGTGGAT                       AATAATATAACACACTGAAAGAACAAATATAAGAATGATAACACTGGAAGATATATTC                       TTATCTAATTACAAGTGGATTkAATACTCACCTGTGCTCTGATTAAATCTACATCAAT                       TGTAAATGTCGATTTGATTTTAAAGTTTTTTTTTAATGCGACTATTTTTTATCTGAAA                       AGTAATCCATTACACTTTTCTATGTTTTATACATTTCAAAAGGGAGGGAAATTCCAAA                       GCCTGAATAATGGAATGGATACATTTCAATTTAACATATATTCTGGCTTTAGATCCCG                       ACATTCACTCCTGTGCAAATTACTTAGGTATGACTTAGGCTAATTTTAAGCTAATAAG                       TGAAGGTACATTCACTCCCTCAAGAGAATCAATACTCAGAAGGTTACAAAGTTTTCTT                       TATAGAATTTCAATCAATCATTCCATCTAAAACCTTAAAATCTCTACAGGACTACATA                       ACATAAATACTGCCAGTTTATAAACGATTGCCTATCTGAATTTTTATACCTACCACTA                       CTTTAATTTATACAGTTAGTTAGCAAATTAGCAACCCAGTAAGTACAGTTATCAAAAA                       TACTAGGAAACTATATCCATATCGCTTTTGGTGTCAGATTGTATCTGTGCATCTAAAA                       ATATTTTAATAAATACTCAAGTGCTCTCAGAGAAAAAAAAAAAAAAAAA                                           ORF Start: ATG at 163   ORF Stop: TAG at 2197                                         SEQ ID NO: 22   678 aa   MW at 77717.4 kD                             NOV8a,   MLDSCKLKSACNLPFICNKKIINTAGTSNAEVPLADPGMYQLDITLRRGQSLAARDRC           CG126224-01       Protein Sequence   GTSDPYVKFKIGGKEVFRSKIIHKNLNPVWEEKACILVDHLREPLYIKVFDYDFGLQD                   DFMGSAFLDLTQLELNRPTDVTLTLKDPHYPDHDLGIILLSVILTPKEGESREFQTQS                   LRLSDLHRKSHLWRGIVSITLIEGRDLKAMDSNGLSDPYVKFRLGHQKYKSKIMPKTL                   NPQWREQFDFHLYEERGGVIDITAWDKDAGKRDDFIGRCQVDLSALSREQTHKLELQL                   EEGEGHLVLLVTLTASATVSISDLSVNSLEDQKEREEILKRYSPLRIFHNLRDVGFLQ                   VKVIRAEGLMAADVTGKSDPFCVVELNKDRLLTHTVYKNLNPEWNKVFTFNIKDIHSV                   LEVTVYDEDRDRSADFLGKVAIPLLSIQNGEQKAYVLKNRQLTGPTKGVIYLEIDVIF                   NAVKASLRTLIPKEQKYIEEENRLSKQLLLRNFIRMKRCVMVLVNAAYYVNSCFDWDS                   PPRSLAAFVVVEDMLEDEEEEDDKDDKDSEKKGFINKIYAIQEVCVSVQNILDEVASF                   GERIKSTFNWTVPFLSWLAIVALCVFTAILYCIPLRYIVLVWGINKFTKKLRSPYAID                   NNELLDFLSRVPSDVQVVQYQELKPDPSHSPYKRKKNNLG                  
 
     [0373] Further analysis of the NOV8a protein yielded the following properties shown in Table 8B.  
               TABLE 8B                       Protein Sequence Properties NOV8a                                        PSort   0.8500 probability located in endoplasmic reticulum       analysis:   (membrane); 0.4400 probability located in plasma membrane;           0.3000 probability located in microbody (peroxisome);           0.1000 probability located in mitochondrial           inner membrane       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0374] A search of the NOV8a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 8C.  
               TABLE 8C                          Geneseq Results for NOV8a                                         NOV8a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAB93562   Human protein sequence SEQ ID   250 . . . 677   254/465 (54%)    e−140           NO: 12957 -  Homo sapiens , 466 aa.    2 . . . 466   329/465 (70%)           [EP1074617-A2, 07 FEB. 2001]       ABB11104   Human C2 domain homologue, SEQ   168 . . . 400   226/233 (96%)    e−129           ID NO: 1474 -  Homo sapiens , 485    18 . . . 250   230/233 (97%)           aa. [WO200157188-A2, 09 AUG.           2001]       ABB70130   Drosophila melanogaster   168 . . . 676   228/552 (41%)    e−102           polypeptide SEQ ID NO 37182 -   452 . . . 975   326/552 (58%)             Drosophila melanogaster , 983 aa.           [WO200171042-A2, 27 SEP. 2001]       AAU87251   Novel central nervous system   201 . . . 365   164/165 (99%)   4e−90           protein #161 -  Homo sapiens , 166    1 . . . 165   165/165 (99%)           aa. [WO200155318-A2, 02 AUG.           2001]       AAG66417   Human C2 domains protein,   532 . . . 678   146/147 (99%)   4e−81           BioHC2 -  Homo sapiens , 175 aa.    29 . . . 175   147/147 (99%)           [CN1296954-A, 30 MAY 2001]                  
 
     [0375] In a BLAST search of public sequence datbases, the NOV8a protein was found to have homology to the proteins shown in the BLASTP data in Table 8D.  
               TABLE 8D                          Public BLASTP Results for NOV8a                                         NOV8a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q96LX0   CDNA FLJ33132 fis, clone   1 . . . 678   672/692 (97%)   0.0           UMVEN2000133, weakly similar   1 . . . 692   677/692 (97%)           to rabphilin-3A -  Homo sapiens             (Human), 692 aa.       AAH30005   Hypothetical 68.5 kDa protein -   1 . . . 533   514/593 (86%)   0.0             Homo sapiens  (Human), 600 aa.   1 . . . 593   522/593 (87%)       Q9H6E8   CDNA: FLJ22344 fis, clone   358 . . . 678   320/321 (99%)   0.0           HRC06080 -  Homo sapiens     1 . . . 321   320/321 (99%)           (Human), 321 aa.       Q8SZ34   RE18318p -  Drosophila     168 . . . 676   238/552 (43%)   e−113             melanogaster  (Fruit fly), 596 aa.   51 . . . 588   337/552 (60%)       Q9V8M4   CG15078 protein -  Drosophila     168 . . . 676   228/552 (41%)   e−102             melanogaster  (Fruit fly), 983 aa.   452 . . . 975   326/552 (58%)                  
 
     [0376] PFam analysis indicates that the NOV8a protein contains the domains shown in the Table 8E.  
               TABLE 8E                          Domain Analysis of NOV8a                                             Identities/                       Similarities           Pfam   NOV8a   for the   Expect           Domain   Match Region   Matched Region   Value                       C2    42 . . . 123   30/97 (31%)   4e−18                   61/97 (63%)           C2   191 . . . 272   37/97 (38%)   3e−27                   68/97 (70%)           C2   347 . . . 427   37/97 (38%)   1.9e−20                     61/97 (63%)                      
 
     Example 9  
     [0377] The NOV9 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 9A.  
               TABLE 9A                       NOV9 Sequence Analysis                                                    SEQ ID NO: 23   2376 bp                             NOV9a,     ATG AATGACACAGAAAAACCAGCAGATACTCCCTCTGAGGAAGAGGACTTTGGTGATC           CG126233-01       DNA Sequence   CAAGGACATATGACCCAGATTTCAAGGGGCCTGTTGCCAACAGGAGTTGTACAGATGT                   TCTGTGCTGTATGATCTTCCTACTGTGTATTATTGGCTACATTGTTTTAGGACTTGTC                   GCCTGGGTACATGGGGACCCCAGAAGAGCAGCCTATCCTACAGACAGCCAGGGCCACT                   TTTGTGGCCAGAAGGGCACTCCCAATGAGAACAAGACCATTTCGTTTTACTTTAACCT                   GTTACGCTGTACCAGTCCCTCCGTATTCCTAAACCTACAGTGCCCTACCACACAGATC                   TGTGTCTCCAAGTGCCCAGAAAAATTTTTAACCTATGTGGAAATGCAACTTTTGTACA                   CAAAAGACAAAAGCTACTGGGAAGACTACCGTCAGTTCTGTAAGACCACTGCTAAGCC                   TGTGAAGTCTCTCACACAGCTTTTACTGGATGATGATTGTCCAACAGCGATTTTTCCC                   AGCAAACCTTGTCTCCAGAGATGTTTCCCTGACTTCTCTACCAAAAATGGCACTTTAA                   CAATAGGAAGTAACATGATGTTCCAAGATGGAAATGGACGGACAAGAAGTGTTGTAGA                   ACTCGGGATTGCTGCAAATGGTATCAATAAACTTCTTGATGCAAAGTCACTTGGATTG                   AAAGTGTTTGAAGACTATGCAAGAACTTGGTATTGGATTCTCATTGGCCTGACGATTG                   CCATGGTCCTTAGTTGGATATTTTTGATACTTCTGAGGTTCATAGCTGGATGCCTCTT                   CTGGGTCTTCATGATTGGTGTGATTGGAATTATAGGTTATGGAATATGGCACTGTTAC                   CAGCAGTACACCAATCTTCAGGAACGCCCAAGTTCTGTATTAACTATCTATGACATCG                   GGATTCAGACTAACATAAGCATGTACTTTGAACTGCAACAAACATGGTTCACATTTAT                   GATAATACTCTGCATCATTGAAGTGATTGTCATCCTCATGCTGATCTTCCTCAGGAAT                   CGAATCCGAGTCGCCATTATCCTGCTGAAGGAAGGAAGCAAAGCCATTGGATATGTTC                   CTAGTACATTAGTCTATCCAGCTTTAACTTTCATTTTGCTCTCAATCTGCATTTGCTA                   CTGGGTCGTGACACCAGTGTATCAGATTTTTAATACAACTGAAATTGCCAAAGCTTGC                   CCTGGGGCTCTGTGTAACTTTGCTTTCTATGGTGGAAAGAGCTTGTACCATCAGTACA                   TCCCTACCTTCCATGTATACAACTTATTTGTCTTTCTCTGGCTTATAAACTTCGTCAT                   TGCATTAGGTCAGTGCGCCCTTGCTGGTGCATTCGCTACTTATTACTGGCCCATGAAA                   AAACCTGATGACATCCCACGATATCCACTTTTTACTGCATTTGGACGAGCCATACCAT                   ATCACACAGGATCCCTAGCATTTGGATCTTTAATTATTGCATTAATTCAAATGTTTAA                   AATTGTACTAGAATACTTGGACCACCGTCTTAAACGTACCCAGAACACATTGTCTAAA                   TTCCTACAATGCTGCCTGAGATGCTGCTTCTGGTGTTTGGAAAATGCAATAAAGTTTT                   TAAACAGAAATGCCTATATTATGATTGCAATATATGGCAGAAACTTCTGCAGGTCAGC                   AAAAGATGCTTTCAATCTGCTGATGAGAAATATACTAAAAGTTGCAGTTACAGATGAA                   GTTACATACTTTGTATTATTCCTGGGGAAACTTCTAGTTGCTGGAAGTATAGGTGTTC                   TGGCCTTCCTATTCTTCACACAAAGACTGCCAGTGATTGCACAACGACCAGCATCTTT                   AAATTACTACTGGGTACCTTTGCTGACAGTCATTTTTGGGTCTTACCTGATTGCACAT                   GGGTTCTTCACCGTCTATGCAATGTGTGTTGAAACAATTTTCATCTGCTTCTTGGAAG                   ATTTAGAAAGAAATGATGGTTCTACTGCPAGACCTTATTATGTGAGTCAACCTTTGCT                   GAAGATTTTCCAGGAGGAATCCACAAACTAGGAAGCAG TAG   AAGAGCAAAACTGGTC                       GTCCTACAGCTGTGTGTTACCTTTTCTCCATCTGCTGTGTCTGTGCAACATTTGTTTC                       ATAAGTGCTTTGTGTTTAGCAACACTGTATTCACGACCTTGTTGGCTTGCATTTGCAT                       GTTTTATACCAAAGCTTATACTGTACTATGTGAAGCCATCAGAAGTCGCAAGGGAATT                       GTTAATAACATAAAACATTTTTATACTAAGATCATTTGTTTTGTIATTCGTTTTTAAA                       GAGTGGCTTGGATGTTTTGAAAATACTACTGAATATGTTAATATTCTTTTAAATCT                                           ORf Start: ATG at 1   ORf Stop: TAG at 2071                                         SEQ ID NO:24   690 aa   MW at 78829.8 kD                             NOV9a,   MNDTEKPADTPSEEEDFGDPRTYDPDFKGPVANRSCTDVLCCMIFLLCIIGYIVLGLV           CG126233-01       Protein Sequence   AWVHGDPRRAAYPTDSQGHFCGQKGTPNENKTISFYFNLLRCTSPSVLLNLQCPTTQI                   CVSKCPEKFLTYVEMQLLYTKDKSYWEDYRQFCKTTAKPVKSLTQLLLDDDCPTAIFP                   SKPCLQRCFPDFSTKNGTLTIGSKMMFQDGNGRTRSVVELGIAANGINKLLDAKSLGL                   KVFEDYARTWYWILIGLTIAMVLSWIFLILLRFIAGCLFWVFMIGVIGIIGYGIWHCY                   QQYTNLQERPSSVLTIYDIGIQTNISMYEELQQTWFTFMIILCIIEVIVILMLIFLRN                   RIRVAIILLKEGSKAIGYVPSTLVYPALTPILLSICICYWVVTAVYQIFNTTEIAKAC                   PGALCNFAFYGGKSLYHQYIPTFHVYNLFVFLWLINFVIALGQCALAGAFATYYWANK                   KPDDIPRYPLFTAFGRAIRYHTGSLAFGSLIIALIQMFKIVLEYLDHRLKRTQNTLSK                   FLQCCLRCCFWCLENAIKFLNRNAYIMIAIYGRNFCRSAKDAFNLLMRNILKVAVTDE                   VTYFVLFLGKLLVAGSIGVLAFLFFTQRLPVIAQGPASLNYYWVPLLTVIFGSYLIAH                   GFFSVYAMCVETIFICFLEDLERNDGSTARPYYVSQPLLKIFQEENPQTRKQ                  
 
     [0378] Further analysis of the NOV9a protein yielded the following properties shown in Table 9B.  
               TABLE 9B                       Protein Sequence Properties NOV9a                                        PSort   0.6000 probability located in plasma membrane; 0.4000       analysis:   probability located in Golgi body; 0.3000 probability           located in endoplasmic reticulum (membrane); 0.0300           probability located in mitochondrial inner membrane       SignalP   Cleavage site between residues 64 and 65       analysis:                  
 
     [0379] A search of the NOV9a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 9C.  
               TABLE 9C                          Geneseq Results for NOV9a                                         NOV9a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value                                         AAB95155   Human protein sequence SEQ ID   17 . . . 684   374/694 (53%)   0.0           NO: 17188 -  Homo sapiens , 704 aa.   10 . . . 698   499/694 (71%)           [EP1074617-A2, 07 FEB. 2001]       AAM40010   Human polypeptide SEQ ID NO   18 . . . 684   374/693 (53%)   0.0           3155 -  Homo sapiens , 706 aa.   13 . . . 700   499/693 (71%)           [WO200153312-A1, 26 JUL. 2001]       AAB42144   Human ORFXORF 1908   18 . . . 684   374/694 (53%)   0.0           polypeptide sequence SEQ ID   13 . . . 701   499/694 (71%)           NO: 3816 -  Homo sapiens , 707 aa.           [WO200058473-A2, 05 OCT. 2000]       AAB24284   Human H38087 (clone GTB6)   17 . . . 684   373/694 (53%)   0.0           protein sequence SEQ ID NO: 7 -   10 . . . 698   499/694 (71%)             Homo sapiens , 704 aa.           [WO200061746-A1, 19 OCT. 2000]       AAB68406   Amino acid sequence of a human   18 . . . 684   373/693 (53%)   0.0           choline transporter like protein 2 -   13 . . . 700   498/693 (71%)             Homo sapiens , 706 aa.           [WO200132704-A1, 10 MAY           2001]                  
 
     [0380] In a BLAST search of public sequence datbases, the NOV9a protein was found to have homology to the proteins shown in the BLASTP data in Table 9D.  
               TABLE 9D                          Public BLASTP Results for NOV9a                                         NOV9a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value                                         Q95JW2   Hypothetical 81.6 kDa protein -   1 . . . 690   661/717 (92%)   0.0             Macaca fascicularis  (Crab eating   1 . . . 717   677/717 (94%)           macaque) (Cynomolgus monkey),           717aa.       AAH28743   Hypothetical 81.7 kDa protein -   1 . . . 690   666/719 (92%)   0.0             Homo sapiens  (Human), 719 aa.   1 . . . 719   677/719 (93%)       Q95JX5   Hypothetical 53.6 kDa protein -   251 . . . 690   424/467 (90%)   0.0             Macaca fascicularis  (Crab eating   2 . . . 468   434/467 (92%)           macaque) (Cynomolgus monkey),           468 aa.       Q9NY68   CTL2 protein -  Homo sapiens     18 . . . 684   374/693 (53%)   0.0           (Human), 706 aa.   13 . . . 700   499/693 (71%)       Q91VA1   RIKEN CDNA 2210409B01 gene   12 . . . 684   320/711 (45%)   0.0           (NG22) -  Mus musculus  (Mouse),   6 . . . 696   457/711 (64%)           707 aa.                  
 
     [0381] PFam analysis indicates that the NOV9a protein contains the domains shown in the Table 9E.  
               TABLE 9E                          Domain Analysis of NOV9a                                             Identities/                       Similarities           Pfam   NOV9a   for the   Expect           Domain   Match Region   Matched Region   Value                             No Significant Matches Found                  
 
     Example 10  
     [0382] The NOV10 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 10A.  
               TABLE 10A                       NOV10 Sequence Analysis                                                    SEQ ID NO: 25   6065 bp                             NOV10a,   CCAGAGGAGCGCCTTCTGCCTCAGAACGGCGTGACTCGGAGAATTGGAGCGTTATTCA           CG126600-01       DNA Sequence     GTATATTAATGTCTTATTGATA   ATG GCAGAACATCCACCACTACTGGATACAACTCAG                   ATCTTAAGTAGTGATATTTCTCTTTTGTCTGCCCCTATTGTGAATGCAGATGGAACAC                   AACAGGTTATTCTGGTACAAGTTAACCCAGGAGAAGCATTTACAATAAGAAGAGAAGA                   TGGACAGTTTCAGTGCATTACAGGTCCTGCTCAGGTTCCAATGATGTCCCCAAATGGT                   TCTGTGCCTCCTATCTATGTGCCTCCTGGATATGCCCCACAGGTTATTGAAGACAATG                   GTCTTCGAAGAGTTGTCGTCGTCCCTCAGGCACCAGAGTTTCACCCTGGTAGTCACAC                   AGTTCTCCACCGTTCTCCACATCCTCCTCTACCTGGTTTCATTTCTGTCCCAACTATG                   ATGCCGCCTCCACCACGTCATATGTACTCACCCGTGACTGGAGCTGGAGACATGACAA                   CACAGTATATGCCACAGTATCAGTCTTCACAAGTCTATGGAGATGTAGATGCTCACTC                   TACACATGGAAGGTCCAACTTTAGAGATGAACGATCTAGTAAAACATATGAACGTTTG                   CAGAAAAAATTGAAGGATCGCCAAGGAACACAGAAAGATAAAATGAGCAGTCCACCAT                   CATCACCCCAGAAATGCCCTTCTCCCATTAATGAACATAATGGACTTATAAAAGGACA                   AATTGCTGGTGGTATAAACACAGGATCAGCAAAAATCAAGTCTGGGAAGGGGAAAGGT                   GGTACACAAGTTGATACAGAAATTGAAGAAAAAGATGAAGAAACTAAAGCATTTGAAG                   CACTTCTTTCCAACATTGTCAAACCAGTGGCCTCCGACATCCAGGCAAGGACAGTAGT                   ACTTACCTGGTCACCACCTTCCAGCCTCATTAATGGTGAAACAGATGAAAGTAGTGTA                   CCAGAGCTCTATGGTTATGAAGTTCTGATCTCAAGTACTGGAAAAGATGGGAAATACA                   AAAGTGTATATGTAGGAGAAGAAACAAATATCACTTTAAATGATCTCAAGCCAGCCAT                   GGATTACCATGCAAAAGTCCAGGCAGAATATAATTCTATAAAGGGAACTCCTTCAGAG                   GCTGAAATCTTTACCACCTTGAGCTGTGAACCTGATATACCTAATCCACCAAGGATAG                   CCAATCGGACCAAAAATTCACTCACTTTGCAATGGAAGGCACCTAGTGACAATGGTTC                   TAAAATCCAAAACTTTGTATTAGAATGGGATGAAGGAAAAGGAAATGGAGAATTTTGT                   CAGTGTTACATGGGCTCACAGAAACAATTTAAAATTACTAAACTTTCACCAGCAATGG                   GCTGTAAATTCAGACTATCGGCCAGAAATGACTATGCTACAAGTGGTTTTAGTGAAGA                   AGTCTTATATTACACCTCAGGCTGTGCTCCTTCTATGCCAGCAAGTCCTGTATTAACC                   AAGGCTGGAATTACTTGGTTATCCTTACAATGGAGTAAGCCCTCAGGAACACCATCAG                   ATGAAGGAATTTCTTACATTTTAGAGATGGAGGAAGAAACTTCAGGATATGGTTTTAA                   GCCTAAATATGATGGAGAAGATCTTGCTTACACAGTGAAAAATCTCAGACGTAGTACT                   AAGTATAAATTTAAGGTTATTGCTTACAACTCAGAAGGTAAAAGTAATCCAAGTGAAG                   TAGTAGAATTTACTACTTGCCCTGATAAACCAGGCATACCTGTAAAGCCTTCAGTGAA                   AGGAAAGATACATTCACACAGTTTTAAAATAACCTGGGATCCACCAAAAGACAATGGC                   GGAGCAACCATCAATAATATGTAGTGGAGATGGCAGAAGGTTCTAAACGGAAACAAAT                   GGGAAATGATATACAGTGGTGCTACCAGGGAACATCTTTGTGATCGACTGAATCCAGG                   CTGTTTCTATCGTTTACGAGTTTACTGCATCAGTGATGGAGGACAGAGTGCGCTCTCT                   GAATCTTTACTTGTGCAGACTCCAGCTGTGCCTCCTGGCCCATGCCTCCCTCCCAGAT                   TACAGGGTAGACCCAAAGCAAAAGAAATACAGTTACGATGGGGACCCCCTCTGGTTGA                   TGGTGGATCACCCATTTCCTGTTACAGTGTGGAAATGTCTCCTATAGAAAAAGATGAA                   CCTAGAGAAGTTTACCAAGGTTCTGAAGTAGAATGTACAGTGAGCAGCCTTCTTCCTG                   GAAAGACATACAGCTTCAGACTACGTGCAGCTAACAAAATGGGGTTTGGACCATTTTC                   AGAAAAATGTGATATTACTACAGCCCCTGGGCCACCAGATCAGTGCAAGCCCCCTCAA                   GTGACATGTAGATCTGCAACTTGTGCACAAGTGAATTGGGAGGTTCCTTTGAGTAATG                   GAACAGATGTCACTGAATATCGACTGGAGTGGGGAGGAGTTGAAGGAAGTATGCAGAT                   ATGTTACTGTGGGCCTGGTCTCAGTTATGAAATAAAAGGACTTTCACCAGCAACTACC                   TATTATTGCAGGGTCCAGGCTCTGAGTGTTGTGGGTGCAGGCCCTTTCAGTGAAGTAG                   TAGCCTGTGTGACTCCACCATCAGTTCCTGGCATTGTGACCTGTCTTCAAGAAATAAG                   CGATGATGAGATAGAAAATCCCCATTATTCACCTTCTACATGCCTTGCAATAAGCTGG                   GAAAAGCCTTGTGATCATGGTTCGGAAATCCTTGCCTACAGCATAGACTTTGGAGATA                   AACAATCCCTAACAGTGGGAAAGGTTACAAGCTATATTATCAACAATTTGCAACCAGA                   TACAACATACAGAATACGAATTCAAGCCTTGAATAGCCTTGGAGCTGGTCCTTTCAGC                   CATATGATAAAATTAAAAACTAAGCCTCTCCCTCCTGATCCACCTCGTCTGGAATGTG                   TTGCCTTTAGCCACCAGAACCTTAAGCTGAAATGGGGAGAAGGAACTCCAAAGACATT                   GTCAACCGATTCTATTCAGTACCACCTTCAGATGGAGGATAAGAATGGACGGTTTGTA                   TCCCTATACAGAGGACCATGTCATACATACAAAGTACAAAGACTTAATGAGTCAACAT                   CCTATAAATTCTGTATTCAAGCTTGTAATGAAGCTCGGGAAGGTCCCCTCTCCCAAGA                   ATATATTTTCACTACTCCAAAATCTGTCCCAGCTGCCTTGAAAGCCCCCAAAATAGAG                   AAAGTAAATGATCACATTTGTGAAATTACATGGGAGTGTTTACAGCCAATGAAAGGTG                   ATCCAGTTATTTACAGTCTTCAAGTTATGTTGGGAAAAGATTCAGAATTCAAACAGAT                   TTACAAGGGTCCCGACTCTTCCTTCCGGTATTCCAGCCTTCAGCTGAACTGTGAATAT                   CGCTTCCGTGTATGTGCCATTCGCCAGTGCCAAGACTCTCTGGGACACCAGGACCTCG                   TAGGTCCCTACAGCACCACAGTGCTCTTCATCTCTCAGAGGACTGAACCACCAGCCAG                   CACCAACAGAGACACTGTGGAAAGCACAAGGACCCGACGGGCACTGAGTGACGAGCAG                   TGTGCTCCCCTCATCCTTGTGCTGTTTGCTTTCTTTTCCATTTTGATTGCCTTTATCA                   TTCAGTACTTTGTAATCAAG TGA   AAATATAACTTTATTTTTTAACTCTATTACATTTT                       ATTTTGTCATGTACTAAAATTATTTCTGTATTGCTTTTATAAAAAACAGTGGCATTTA                       GCACTGGCATTGAGACTATAGCACATCATTTTTGCCATTTTCAGTGCTTATATTGTTA                       GGTAGAGGCTGGCACTTTATTAGAATGCAAGCCACAAAAATATCAATTTTGTTTTTTT                       TTGTTAGGGTGGGTCTTCTTTTTTTCTTTCCCTCTCTCTTTTTTTAACAAATGCCTTC                       TTATAGAAAAACTTTCTAAGAGGCAACAATTTAGAATGGATATTTTGACGAATCGGCA                       TGAGTGTAACAGTGATAACCTGATCTGTTTGTTTTAAAGATTATTACCAAGTGAAAAA                       TTCAGAATGAATAGAATTTACACTAACATGCTATATAAAATGTTAAAGTCTGATGCTG                       TGAAAGCAATCTAGTGCTATATTTCTACCTCCTCATTTGTCTTAATTATTTGGTAAGT                       GGGATTATGATGAGTAACTGGAGGGGCTTAGAAACAAAAACTGGATGAAAGAGTATGC                       ATGAAGAAAAGCTTCTTTGATAAATGTGGAGTTCTTCATTATAAATATATATTCATGA                       ATTCACAGATAAGTACTTAAAGAACAGACAGTTTACTTGGCCTAAAAATATTTTGATG                       TTTACTCAAAAAGTACCTCTTCAGGTCTTGAGAACATGGAAAAGAATTGAGTGCTTTT                       AAATACTTTTTAGAAAGTAATCATAAAAGTAAATTGAATTTCAAACCTATTTGGCTTC                       TGTTTTGTGAACCTTTGAACTATATGTATGTGTATAAGGGTATACACATACATATATG                       GCATATAACAAGTGTACACATATACACATAACAAGTGTAGAAGTATATATTACATACA                       TACACTCACTCTGTCTGGTATAGGCTAATTTTGAAGAACTCCCATAAGTTTCTGCTGC                       TTCTCCCATAACTGCTGCCACCACCATCAGAATTCATAATCAAACCTAACCTTTTTGT                       TTGGGGCACCAAATCTGAAGACAAAATTAATTTGCACCAGTAAACTTCAAGCTGCTTT                       CTTTCTTGAAAACTAAACGTTTAACGTATAATGTCTGTTTGGATACTGTTCCAAATTG                       TTGATTGCATGTGGTTAATGTTGCATTAGAGCACTTTGCAATTGCATAATTCATTAAT                       GTTTTGTGAGCTTGCATTTGTGAGTTATTGGATGATCAGACTGAATTTTGTCAAGTAT                       CACATTGTACATCTTGCCTAGATGTCGATGACTGCAAGTAATAATACAGTTTATAATG                       AAACTATCTACAATTCTTGTTTTAGCACATCTGTTATCCGTAAAACACCTGTAACTAG                       CTTTTTTAATTTATTATTTGAATTTTAGGATAGCGAATCACTAATTTTTAGTTGCTGA                       GGTTGGCATTTTAGTGATTATTAAGCACTTCTGTCAGTCTTTGAAAAAAAGAACGTAT                       TTTTTGTGCTTTGAAGATCTCTGAAGAATTTCTTTTATAATAGAATGGGCATGTATTG                       TAACAGTTTTATGTCAAATGATCTGTGCTGTAGAAAAACATTAACCCTTGTTCAAAAA                       AGAAATGGATAAACTTGGCCTTTCTAAGTGGTAAGAATGACCTGTCACTATAATATAC                       TGTATGTTTACATTTTATTTAAATTTAATCTCTTATGTATAGGGTGATAACCTTCCCC                       AGAAACAACAGTGATTGCGATTGTTTTCTAGAAACTTCTTTAAAGTGCCACATTTGGC                       AGTACAAATGAGTCTGAGTGTAATAGCCCAGAGATTTATATATAGTTGAATGTCTAAA                       ATGGTAAAATGTGCCACTGTGTCAAGTTACAGTGGCTTATGTTTTTCATAGTAATTCA                       AATGAACTTCCTATTTTTGATAGTAAATGTCATTTkATAGTATACTTGCCATTTGAGC                       CTCACTGCAAAATTAGTGCAGAGGAGAAAACAATTTTTAATGTAATCTTGATTTTACC                       TCATATACTGTACATTCCAAAAACTCTAAACTTTTTAAAGATTATAGATACACTACCA                       GTTGTATCATTCTTTTTGAGATACGTTTATTGTATTCATATATATTCATTATTTGCTA                       CCTGTTTAAGAAAGTGAAATGTTATGGTCTCCCCTCTTCCAATGAGCTTAAAACATTT                       GTTGTATCATTCTTTTTGAGATACGTTTATTGTATTCATATATATTCATTATTTGCTA                       CCTGTTTAAGAAAGTGAAATGTTATGGTCTCCCCTCTTCCAATGAGCTTAAAACATTT                       TTCCCAACAGTATATAAATCTTCAACATGAGAGGATGTATATTTATTATATAAAGCCC                       AGTAAAGAATAAAATTAGAAGTTTTATCCTAGG                                           ORF Start: ATG at 81   ORF Stop: TGA at 3675                                         SEQ ID NO 26   1198 aa   MW at 131840.2 kD                             NOV10a,   MAEHPPLLDTTQILSSDISLLSAPIVSADGTQQVILVQVNPGEAFTTRREDGQFQCIT           CG126600-01       Protein Sequence   GPAQVPMMSPNGSVPPIYVPPGYAPQVIEDNGVRRVVVVPQAPEFHPGSHTVLHRSPH                   PPLPGFISVPTMMPPPPRHMYSPVTGAGDMTTQYMPQYQSSQVYGDVDAHSTHGRSNF                   IRDERSSKTYERLQKKLKDRQGTQKDKMSSPPSSPQKCPSPINEHNGLIKGQIAGGINT                   GSAKIKSGKGKGGTQVDTEIEEKDEETKJXFEALLSNIVKPVASDIQARTVVLTWSPPS                   SLINGETDESSVPELYGYEVLISSTGKDGKYKSVYXTGEETNITLNDLKPAMDYHAKVQ                   AEYNSIKGTPSEAEIFTTLSCEPDIPNPPRIANRTKNSLTLQWKAPSDNCSKIQNFVL                   EWDEGKGNGEFCQCYMGSQKQFKITKLSPAMGCKFRLSARNDYGTSGFSEEVLYYTSG                   CAPSMPASPVLTKAGITWLSLQWSKPSGTPSDEGISYILEMEEETSGYGFKPKYDGED                   LAYTVKNLRRSTKYKFKVIAYNSEGKSNPSEVVEFTTCPDKPGIPVKPSVKGKIHSHS                   FKITWDPPKDNGGATINKYVVEMAEGSNGNKWEMIYSGATREHLCDRLNPGCFYRLRV                   YCISDGCQSAVSESLLVQTPAVPPGPCLPPRLQCRPKAKEIQLRWGPPLVDGGSPISC                   YSVEMSPIEKDEPREVYQGSEVECTVSSLLPGKTYSFRLRAANKMGFGPFSEKCDITT                   APGPPDQCKPPQVTCRSATCAQVNWEVPLSNGTDVTEYRLEWGGVEGSMQICYCGPGL                   SYEIKGLSPATTYYCRVQALSVVGAGPFSEVVACVTPPSVPGIVTCLQEISDDEIENP                   HYSPSTCLAISWEKPCDHGSEILAYSIDFGDKQSLTVGKVTSYIINNLQPDTTYRIRI                   QALNSLGAGPFSHMIKLKTKPLPPDPPRLECVAFSHQNLKLKWGEGTPKTLSTDSIQY                   HLQMEDKNGRFVSLYRGPCHTYKVQRLNESTSYKFCIQACNEAGEGPLSQEYIFTTPK                   SVPAALKAPKIEKVNDHICEITWECLQPMKGDPVIYSLQVMLGKDSEFKQIYKGPDSS                   FRYSSLQLNCEYRFRVCAIRQCQDSLGHQDLVGPYSTTVLFISQRTEPPASTNRDTVE                   STRTRRALSDEQCAAVILVLFAFFSILIAFIIQYFVIK                  
 
     [0383] Further analysis of the NOV10a protein yielded the following properties shown in Table 10B.  
               TABLE 10B                       Protein Sequence Properties NOV10a                                        PSort   0.8500 probability located in endoplasmic reticulum       analysis:   (membrane); 0.6640 probability located in plasma membrane;           0.1000 probability located in mitochondrial inner           membrane; 0.1000 probability located in Golgi body       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0384] A search of the NOV10a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 10C.  
               TABLE 10C                          Geneseq Results for NOV10a                                         NOV10a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABG34076   Human Pro peptide #47 -  Homo     351 . . . 1198    459/850 (54%)   0.0             sapiens , 847 aa. [WO200224888-   2 . . . 847   607/850 (71%)           A2, 28 MAR. 2002]       AAM93625   Human polypeptide, SEQ ID NO:   437 . . . 1198    405/764 (53%)   0.0           3462 -  Homo sapiens , 760 aa.   1 . . . 760   540/764 (70%)           [EP1130094-A2, 05 SEP. 2001]       AAU18383   Human endocrine polypeptide SEQ   486 . . . 1198    373/715 (52%)   0.0           ID No 338 -  Homo sapiens , 717 aa.   7 . . . 717   501/715 (69%)           [WO200155364-A2, 02 AUG.           2001]       AAM43571   Human polypeptide SEQ ID NO   487 . . . 1198    372/714 (52%)   0.0           249 -  Homo sapiens , 710 aa.   1 . . . 710   499/714 (69%)           [WO200155308-A2, 02 AUG.           2001]       AAU12206   Human PRO4979 polypeptide   8 . . . 608   313/614 (50%)   e−168           sequence -  Homo sapiens , 625 aa.   9 . . . 612   409/614 (65%)           [WO200140466-A2, 07 JUN. 2001]                  
 
     [0385] In a BLAST search of public sequence datbases, the NOV10a protein was found to have homology to the proteins shown in the BLASTP data in Table 10D.  
               TABLE 10D                          Public BLASTP Results for NOV10a                                         NOV10a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q9Y2H6   KIAA0970 protein -  Homo     57 . . . 1198    1139/1142 (99%)    0.0             sapiens  (Human), 1151 aa   10 . . . 1151    1141/1142 (99%)            (fragment).       Q9H1W1   BA203I16.1 (KIAA0970   422 . . . 1198    733/777 (94%)   0.0           protein) -  Homo sapiens     1 . . . 733    733/777 (94%)           (Human), 733 aa.       Q96N25   CDNA FLJ31509 fis, clone   1 . . . 326    324/326 (99%)   0.0           NT2RI1000016 -  Homo     1 . . . 326    325/326 (99%)             sapiens  (Human), 326 aa.       Q9H517   CDNA: FLJ23399 fis,   706 . . . 1198    256/494 (51%)   e−151           clone HEP 18254 -  Homo     5 . . . 495    350/494 (70%)             sapiens  (Human), 495 aa.       Q9NSQ8   Hypothetical 52.6 kDa   720 . . . 1198    249/480 (51%)   e−147           protein -  Homo sapiens     1 . . . 477    341/480 (70%)           (Human), 477 aa           (fragment).                  
 
     [0386] PFam analysis indicates that the NOV10a protein contains the domains shown in the Table 10E.  
               TABLE 10E                          Domain Analysis of NOV10a                                             Identities/                   NOV10a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                       fn3   266 . . . 359   24/97 (25%)   1.6e−05                   65/97 (67%)           fn3   371 . . . 455   19/88 (22%)   3.2e−06                   62/88 (70%)           fn3   467 . . . 552   22/87 (25%)   9.7e−07                   59/87 (68%)           fn3   564 . . . 650   25/88 (28%)   0.00012                   60/88 (68%)           fn3   661 . . . 747   25/90 (28%)   4.1e−09                   59/90 (66%)           fn3   759 . . . 841   24/86 (28%)   1.6e−08                   59/86 (69%)           fn3   863 . . . 940   28/87 (32%)   3.2e−09                   63/87 (72%)           fn3    952 . . . 1035   23/88 (26%)   0.032                   52/88 (59%)                      
 
     Example 11  
     [0387] The NOV11 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 11A.  
               TABLE 11A                       NOV11 Sequence Analysis                                                    SEQ ID NO: 27   1175 bp                             NOV11a,     ATG GCCACTGCCCAGTTGCAGAGGACTTCCATGACTGCACTGGTATTTCTCAATAAGA           CG127888-01       DNA Sequence   TACCACCTGAACACCAGTCTTTGGTGTTAGTGAAGAGTTTCCTCACAGTTTCAGTATC                   CTGTATCATGTATTTGAGAGGAATATTTCCAGCATGTGCTTATGGAACCAGATATCTA                   GATGATCTTTGTGTCAAAATACTGAGAGAAGATAAAAATTGCCCAGGATCTACACAGT                   TAGTGAAATGGATACTAGGATGTTACGATGCTTTACAGAAAAAAATATACACAAACCC                   AGAAGATCCTCAGACAATTTCAGAATGTTACCAATTCAAATTCAAATACACCAATAAT                   GGACCACTTATGGACTTCATAAGTGAAAGCCPAAGCAATGAGTCTAGCATGTTATGTA                   CTGACACCGAGAAAGCAAGCACTCTCCTAATTCGCAAGATTTATACCCTAATGCAAAA                   TCTGGGGCCTTTACCTAATGTTTGTTTGAGCATGAAACGTTTTTACTATGATGAAGTT                   ACACCCCCAGATTACCAGCCTCCTGGTTTTAAGGATGGTGATTGTGAAGGACTTATAT                   TTGAAGGGGAACTTATGTATTTATCTGGGCGAAGTCTCAAAACACCTTTTCCCACCTT                   CAAAGTAAGTGACCACTGAGAGAGAACGAATGGAAAATATTTATTCAAACTATACTAA                   TCACTAAAACAAATAAAPACAACTTCACAAAATCCTGAGGGACAAAGATGCAGAAAAG                   ATGACCACGCGCATTATACAAGTGATGATTTGGACATTGAAACTAAAATGGAAGAGCA                   GGAAAAAAACCCTCGATTTTCTGAACTTGGAGAACCAAGTTTAGTTTGTGAGGATGAT                   GAAATTGTGAGGTATAAAPAAAGTTCAGATCTTTCCATTTCTCATTCTCAGGTTGAGC                   AGTTAGTCAATAAAACATCGGAACTTGATATGTCTGAAAGCAAAACAAGAAGTGGAAA                   GTCTTTCAGAATAATGGCAAATGGAAATCAACCAGTAACATCTTCCAAAGAAATTCGG                   AAGAGAAGTCAACATGAATCTGGGAGAATAGTGCTCCATCACTCGCATTCTTCTAGTC                   AAGAGTCAGTACCAAAAAGGAGAAAGTTTAGTGAACCAAAGGACATATA TAA   AAAATT                       ATTTTTCTTCTGTAT                                           ORF Start: ATG at 1   ORF Stop: TAA at 1153                                         SEQ ID NO: 28   384 aa   MW at 43970.6 kD                             NOV11a,   MATAQLQRTSMTALVFLNKIPPEHQSLVLVKSFLTVSVSCIMYLRGIFPACAYGTRYL           CG127888-01       Protein Sequence   DDLCVKILREDKNCPGSTQLVKWILGCYDALQKKIYTNPEDPQTISECYQFKFKYTNN                   GPLMDFISESQSNESSMLCTDTEKASTLLIRKTYTLMQNLGRLPNVCLSMKRFYYDEV                   TPPDYQPPGFKDGDCEGVIFEGELMYLNVGEVSTPFPTFKVKVTTERERMENIYSTIL                   SLKQIKTKLHKILRDKDAEDDQAHYTSDDLDIETKMEEQEKNPRFSELGEPSLVCEDD                   EIVRYKKSSDLSISHSQVEQLVNKTSELDMSESKTRSGKSFRIMANGNQPVTSSKEIR                   KRSQHESGRIVLHHSHSSSQESVPKRRKFSEPKEHI                  
 
     [0388] Further analysis of the NOV11a protein yielded the following properties shown in Table 11B.  
               TABLE 11B                       Protein Sequence Properties NOV11a                                        PSort   0.6186 probability located in outside; 0.1900 probability       analysis:   located in lysosome (lumen); 0.1000 probability located           in endoplasmic reticulum (membrane); 0.1000 probability           located in endoplasmic reticulum (lumen)       SignalP   Cleavage site between residues 53 and 54       analysis:                  
 
     [0389] A search of the NOV11a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 11C.  
               TABLE 11C                          Geneseq Results for NOV11a                                         NOV11a   Identities/                   Residues/   Similarities for       Genescq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAG89139   Human secreted protein, SEQ ID   1 . . . 384   339/394 (86%)   0.0           NO: 259 -  Homo sapiens , 394 aa.   1 . . . 394   350/394 (88%)           [WO200142451-A2, 14 JUN. 2001]       AAB63451   Human breast cancer associated   36 . . . 259    196/233 (84%)   e−109           antigen protein sequence SEQ ID   2 . . . 234   203/233 (87%)           NO: 813 -  Homo sapiens , 235 aa.           [WO200073801-A2, 07 DEC. 2000]       AAB63280   Human breast cancer associated   36 . . . 259    196/233 (84%)   e−109           antigen protein sequence SEQ ID   2 . . . 234   203/233 (87%)           NO: 642 -  Homo sapiens , 235 aa.           [WO200073801-A2, 07 DEC. 2000]       AAU07870   Polypeptidc sequence for   1 . . . 112    93/121 (76%)   5e−46            mammalian Spg27 - Mammalia, 121 aa.   1 . . . 121   100/121 (81%)           [WO200166752-A2, 13 SEP. 2001]       AAG76687   Human colon cancer antigen protein   248 . . . 359     88/113 (77%)   6e−41            SEQ ID NO: 7451 -  Homo sapiens ,   22 . . . 134     94/113 (82%)           155 aa. [WO200122920-A2, 05           APR. 2001]                  
 
     [0390] In a BLAST search of public sequence datbases, the NOV11a protein was found to have homology to the proteins shown in the BLASTP data in Table 11D.  
               TABLE 11D                          Public BLASTP Results for NOV11a                                         NOV11a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value                                         Q9H0K8   Hypothetical 44.4 kDa protein -   1 . . . 384   338/387 (87%)   0.0             Homo sapiens  (Human), 387 aa.   1 . . . 387   350/387 (90%)       Q9D5T7   4921522K05Rik protein -  Mus     1 . . . 383   272/395 (68%)   e−146             musculus  (Mouse), 392 aa.   1 . . . 391   315/395 (78%)       Q9D473   4921522K05Rik protein -  Mus     1 . . . 351   255/363 (70%)   e−138             musculus  (Mouse), 374 aa.   1 . . . 360   294/363 (80%)       Q95JZ3   Hypothetical 30.7 kDa protein -   120 . . . 384    228/267 (85%)   e−123             Macaca fascicularis  (Crab eating   1 . . . 267   239/267 (89%)           macaque) (Cynomolgus monkey),           267 aa.       Q9CUF3   4921522K05Rik protein -  Mus     1 . . . 288   212/298 (71%)   e−116             musculus  (Mouse), 295 aa   1 . . . 295   242/298 (81%)           (fragment).                  
 
     [0391] PFam analysis indicates that the NOV11a protein contains the domains shown in the Table 11E.  
               TABLE 11E                          Domain Analysis of NOV11a                                             Identities/                   NOV11a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                                                 HORMA   22 . . . 225   54/254 (21%)   0.00013                   134/254 (53%)                       
 
     Example 12  
     [0392] The NOV12 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 12A.  
               TABLE 12A                       NOV12 Sequence Analysis                                                    SEQ ID NO: 29   513 bp                             NOV12a,     GCCAGACCAAACCGGACCTCGGGGCCG   ATG CGGCTGCTGCCCCTGCTGCGGACTGTCC           CG128249-02       DNA Sequence   TCTGGGCCGCGTTCGTCGGCTCCCCTCTGCGCGGGGGCTCCAGCCTCCGCCACGTAGT                   CTACTGGAACTCCAGTAACCCCAGGTTGCTTCGAGGAGACGCCGTGGTGGAGGTGGCC                   CTCAACGATTACCTAGACATTGTCTGCCCCCACTACGAAGGCCCAGGGCCCCCTGAGG                   GCCCCGAGACGTTTGCTTTGTACATGGTGGACTGGCCAGGGTATGAGTCCTGCCAGGC                   AGAGGGCCCCCGGGCCTACAAGCGCTGGGTGTCCTCCCTGCCCTTTGGCCATGTTCAA                   TTCTCAGAGAAGATTCAGCGCTTCACACCCTTCTCCCTCGGCTTTGAGTTCTTACCTG                   GAGAGAGTGGCACATCAGGGTGGCGAGGGGGGGACACTCCCAGCCCCCTCTCTCTCTT                   GCTATTACTGCTGCTTCTGATTCTTCGTCTTCTGCGAATTCTG TGA   CCC                                           ORF Start: ATG at 28   ORF Stop: TGA at 508                                         SEQ ID NO: 30   160 aa   MW at 17901.6 kD                             NOV12a   MRLLPLLRTVLWAAFVGSPLRGGSSLRHVVYWNSSNPRLLRGDAVVEVGLNDYLDIVC           CG128249-02       Protein Sequence   PHYEGPGPPEGPETFALYMVDWPGYESCQAEGPRAYKRWVCSLPFGHVQFSEKIQRFT                   PFSLGFEFLPGESGTSGWRGGDTPSPLCLLLLLLLLILRLLRIL                  
 
     [0393] Further analysis of the NOV 12a protein yielded the following properties shown in Table 12B.  
               TABLE 12B                       Protein Sequence Properties NOV12a                                        PSort   0.9190 probability located in plasma membrane; 0.3000       analysis:   probability located in lysosome (membrane); 0.2133           probability located in microbody (peroxisome); 0.1000           probability located in endoplasmic reticulum (membrane)       SignalP   Cleavage site between residues 23 and 24       analysis:                  
 
     [0394] A search of the NOV12a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 12C.  
               TABLE 12C                          Geneseq Results for NOV12a                                         NOV12a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAR71482   Human hek-L protein -  Homo     1 . . . 160   158/201 (78%)    4e−87             sapiens , 201 aa. [WO9506065-A,   1 . . . 201   160/201 (78%)            02 MAR. 1995]       ABG27837   Novel human diagnostic protein   1 . . . 127   63/131 (48%)   1e−28           #27828 -  Homo sapiens , 335 aa.   111 . . . 240    82/131 (62%)           [WO200175067-A2, 11 OCT.           2001]       ABG27837   Novel human diagnostic protein   1 . . . 127   63/131 (48%)   1e−28           #27828 -  Homo sapiens , 335 aa.   111 . . . 240    82/131 (62%)           [WO200175067-A2, 11 OCT.           2001]       AAW00035   HEK4 binding protein -  Homo     1 . . . 127   63/131 (48%)   1e−28             sapiens , 228 aa. [WO9623000-A1,   4 . . . 133   82/131 (62%)           01 AUG. 1996]       AAW02586   Lerk-7 protein -  Homo sapiens ,   1 . . . 127   63/131 (48%)   1e−28           228 aa. [WO9617925-A1, 13 JUN.   4 . . . 133   82/131 (62%)           1996]                  
 
     [0395]               TABLE 12D                          Public BLASTP Results for NOV12a                                         NOV12a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               P52798   Ephrin-A4 precursor (EPH-related   1 . . . 160   158/201 (78%)   1e−86           receptor tyrosine kinase ligand 4)   1 . . . 201   160/201 (78%)           (LERK-4) -  Homo sapiens  (Human),           201 aa.       008542   Ephrin-A4 precursor (EPH-related   1 . . . 160   131/206 (63%)   2e−67           receptor tyrosine kinase ligand 4)   1 . . . 206   141/206 (67%)           (LERK-4) -  Mus musculus  (Mouse),           206 aa.       Q9CZS8   10 days embryo cDNA, RIKEN full-   1 . . . 160   129/206 (62%)   1e−66           length enriched library,   1 . . . 206   141/206 (67%)           clone: 2610529M21, full insert           sequence -  Mus musculus  (Mouse),           206 aa.       Q98TZ1   Ephrin-A6 -  Gallus gallus  (Chicken),   6 . . . 129    69/127 (54%)   2e−31           202 aa (fragment).   1 . . . 124    84/127 (65%)       P97605   Ephrin-A5 precursor (EPH-related   1 . . . 127    64/131 (48%)   3e−28           receptor tyrosine kinase ligand 7)   4 . . . 133    82/131 (61%)           (LERK-7) (AL-1) -  Rattus               norvegicus  (Rat), 228 aa.                    
     [0396] PFam analysis indicates that the NOV12a protein contains the domains shown in the Table 12E.  
               TABLE 12E                          Domain Analysis of NOV12a                                             Identities/                   NOV12a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                       Ephrin   22 . . . 129   63/114 (55%)   1.2e−54                   94/114 (82%)                      
 
     Example 13  
     [0397] The NOV13 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 13A.  
               TABLE 13A                       NOV13 Sequence Analysis                                                    SEQ ID NO: 31   240 bp                             NOV13a,     ATG GTGGGCCCCGCGCCGCGGCGGCGGCTGCGGCCGCTGGCAGCGCTGGCCCTGGTCC           CG128785-01       DNA Sequence   TGGCGCTGGCCCCGGGGCTGCCCACAGCCCGGGCCGGGCAGACACCGCGCCCTGCCGA                   GCGGGGGCCCCCAGTGCGGCTTTTCACCGAGGAGGAGCTGGCCCGCTATGGCGGGGAG                   GAGCTTCTCCCCTGCTTTCTAGGAAGATCACCCCATCTACTTGGCAGTGAACGGAGTG                   GTGTT TGA                                           ORF Start: ATG at 1   ORF Stop: TGA at 238                                         SEQ ID NO: 32   79 aa   MW at 8309.6 kD                             NOV13a,   MVGPAPRRRLRPLAALALVLALAPGLPTARAGQTPRPAERGPPVRLFTEEELARYGGE           CG128785-01       Protein Sequence   ELLPCFLGRSAHLLGSEGSGV                  
 
     [0398] Further analysis of the NOV13a protein yielded the following properties shown in Table 13B.  
               TABLE 13B                       Protein Sequence Properties NOV13a                                        PSort   0.6854 probability located in outside; 0.1000 probability       analysis:   located in endoplasmic reticulum (membrane); 0.1000           probability located in endoplasmic reticulum (lumen);           0.1000 probability located in microbody (peroxisome)       SignalP   Cleavage site between residues 32 and 33       analysis:                  
 
     [0399] A search of the NOV13a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 13C.  
               TABLE 13C                          Geneseq Results for NOV13a                                         NOV13a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAB98325   Human ortholog of r0v0-176.7A   1 . . . 59    59/59 (100%)   1e−27           (PA27) protein sequence -  Homo     1 . . . 59    59/59 (100%)             sapiens , 120 aa. [WO200132926-A2,           10 MAY 2001]       AAY94866   Human protein clone HP 10557 -   1 . . . 59    59/59 (100%)   1e−27             Homo sapiens , 172 aa.   1 . . . 59    59/59 (100%)           [WO200005367-A2, 03 FEB. 2000]       AAB98322   Human PA27 protein (r0v0-176.7A)   1 . . . 59   58/59 (98%)   1e−25           SEQ ID NO: 72 -  Homo sapiens , 171 aa.   1 . . . 58   58/59 (98%)           [WO200132926-A2, 10 MAY           2001]       ABB72158   Rat protein isolated from skin cells   1 . . . 59   46/59 (77%)   4e−17           SEQ ID NO: 197 - Rattus sp, 171 aa.   1 . . . 58   48/59 (80%)           [WO200190357-A1, 29 NOV. 2001]       AAB55958   Skin cell protein, SEQ ID NO: 197 -   1 . . . 59   46/59 (77%)   4e−17           Rattus sp, 171 aa. [WO200069884-   1 . . . 58   48/59 (80%)           A2, 23 NOV. 2000]                  
 
     [0400] In a BLAST search of public sequence datbases, the NOV13a protein was found to have homology to the proteins shown in the BLASTP data in Table 13D.  
               TABLE 13D                          Public BLASTP Results for NOV13a                                         NOV13a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q9UMX5   Secreted protein of unknown   1 . . . 59    59/59 (100%)   2e−27           function -  Homo sapiens     1 . . . 59    59/59 (100%)           (Human), 172 aa.       Q9CQ45   1110060M21Rik protein -  Mus     1 . . . 59   47/59 (79%)   1e−17             musculus  (Mouse), 171 aa.   1 . . . 58   49/59 (82%)       Q9I6U2   Probable TonB-dependent   6 . . . 44   21/42 (50%)   1.6           receptor -  Pseudomonas     8 . . . 48   23/42 (54%)             aeruginosa , 790 aa.       Q9AJPO   ORF5 -  Streptomyces griseus ,   4 . . . 42   18/42 (42%)   2.0           524 aa.   421 . . . 462    25/42 (58%)       AAA42060   Ornithine aminotransferase -   10 . . . 62    20/56 (35%)   6.0             Rattus norvegicus  (Rat), 97 aa   2 . . . 57   27/56 (47%)           (fragment).                  
 
     [0401] PFam analysis indicates that the NOV13a protein contains the domains shown in the Table 13E.  
               TABLE 13E                          Domain Analysis of NOV13a                                             Identities/                   NOV13a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                             No Significant Matches Found                  
 
     Example 14  
     [0402] The NOV14 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 14A.  
               TABLE 14A                       NOV14 Sequence Analysis                                                    SEQ ID NO: 33   751 bp                             NOV14a,   CGAGCGTCGCGGCTATGGCTTATCACTCGGGCTACGGAGCCCACGGCTCCAAGCACAG           CG129005-01       DNA Sequence   GGCCCGGGCAGCCCCGGATCCCCCTCCCCTCTTCGATGACACAAGCGGTGGTTATTCC                   AGCCAGCCCGGGGGATACCCAGCCACAGGAGCAGACGTGGCCTTCAGTGTCAACCACT                   TGCTTGGGGACCCAATGGCCAATGTGGCTATGGCCTATGGCAGCTCCATCGCATCCCA                   TGGGAAGGACATGGTGCACAAGGAGCTGCACCGTTTTGTGTCTGTGAGCAAACTCAAG                   TATTTTTTTGCTGTGGACACAGCCTACGTGCCCAAGAAGCTAGGGCTGCTGGTCTTCC                   CCTACACACACCAGAACTGGGAAGTGCAGTACAGTCGTGATGCTCCTCTGCCCCCCCG                   GCAAGACCTCAACGCCCCTGACCTCTATATCCCCACGATGGCCTTCATTACTTACGTG                   CTCCTGGCTCGGATGGCACTGGGCATTCAGAAAATGATCCTCAGTGTGCTCACGGGGC                   TGCTGTTCGGCAGCGATGGCTACTACGTGGCGCTGGCCTGGACCTCATCGGCGCTCAT                   GTACTTCATTGTGCGCTCTTTGCGGACAGCAGCCCTGGGCCCCGACAGCATGGGCGGC                   CCCGTCCCCCGGCAGCGTCTCCAGCTCTACCTGACTCTGGGAGCTGCAGCCTTCCAGC                   CCCTCATCATATACTGGCTGACTTTCCACCTGGTCCCG TGA   CCCCCTGGCCCCAG                                           ORF Start: ATG at 15   ORF Stop: TGA at 735                                         SEQ ID NO: 34   240 aa   MW at 26221.0 kD                             NOV14a,   MAYHSGYGAHGSKHRARAAPDPPPLFDDTSGGYSSQPGGYPATGADVAFSVNHLLGDP           CG129005-01       Protein Sequence   MANVAMAYGSSIASHGKDMVHKELHRFVSVSKLKYFFAVDTAYVAKKLGLLVFPYTHQ                   NWEVQYSRDAPLPPRQDLNAPDLYIPTMAFITYVLLAGMALGIQKMILSVLTGLLFGS                   DGYYVALAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGaAAFQPLIiy                   WLTFHLVR                  
 
     [0403] Further analysis of the NOV14a protein yielded the following properties shown in Table 14B.  
               TABLE 14B                       Protein Sequence Properties NOV14a                                        PSort   0.7480 probability located in microbody (peroxisome); 0.7000       analysis:   probability located in plasma membrane; 0.2000 probability           located in endoplasmic reticulum (membrane); 0.1000           probability located in mitochondrial inner membrane       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0404] A search of the NOV14a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 14C.  
               TABLE 14C                          Geneseq Results for NOV14a                                         NOV14a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABB12032   Human SIGP 2328134 homologue,    1 . . . 240   240/293 (81%)    e−132           SEQ ID NO: 2402 -  Homo sapiens ,   53 . . . 345   240/293 (81%)           345 aa. [WO200157188-A2, 09           AUG. 2001]       AAY21851   Human signal peptide-contianing    1 . . . 240   240/293 (81%)    e−132           protein (SIGP) (clone ID 2328134) -   54 . . . 346   240/293 (81%)             Homo sapiens , 346 aa.           [WO9933981-A2, 08 JUL. 1999]       AAM41111   Human polypeptide SEQ ID NO   11 . . . 240   133/294 (45%)   7e−59           6042 -  Homo sapiens , 351 aa.   61 . . . 351   171/294 (57%)           [WO200153312-A1, 26 JUL. 2001]       AAO17463   Human liver cancer expressed   21 . . . 240   128/284 (45%)   7e−57           protein PP4519 -  Homo sapiens ,    3 . . . 283   165/284 (58%)           283 aa. [CN1329064-A, 02 JAN.           2002]       AAU83613   Human PRO protein, Seq ID No 44 -   21 . . . 240   128/284 (45%)   7e−57             Homo sapiens , 283 aa.    3 . . . 283   165/284 (58%)           [WO200208288-A2, 31 JAN. 2002]                  
 
     [0405] In a BLAST search of public sequence datbases, the NOV14a protein was found to have homology to the proteins shown in the BLASTP data in Table 14D.  
               TABLE 14D                          Public BLASTP Results for NOV14a                                         NOV14a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q9BVD0   Putative transmembrane protein -   1 . . . 240   240/293 (81%)   e−131             Homo sapiens  (Human), 293 aa.   1 . . . 293   240/293 (81%)       O95070   54TMp -  Homo sapiens  (Human),   1 . . . 240   239/293 (81%)   e−131           293 aa.   1 . . . 293   239/293 (81%)       Q91XB7   Similar to putative transmembrane   1 . . . 240   220/293 (75%)   e−120           protein, homolog of yeast golgi   1 . . . 293   230/293 (78%)           membrane protein Yif1p (Yip1p-           interacting factor) -  Mus musculus             (Mouse), 293 aa.       O35946   Hypothetical 14.9 kDa protein -   1 . . . 132   112/132 (84%)   2e−63              Rattus norvegicus  (Rat), 137 aa.   1 . . . 132   123/132 (92%)       O00606   Putative Rab5-interacting protein -   10 . . . 115     99/107 (92%)   8e−52              Homo sapiens  (Human), 123 aa   1 . . . 107   101/107 (93%)           (fragment).                  
 
     [0406] PFam analysis indicates that the NOV14a protein contains the domains shown in the Table 14E.  
               TABLE 14E                          Domain Analysis of NOV14a                                             Identities/                   NOV14a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                             No Significant Matches Found                  
 
     Example 15  
     [0407] The NOV15 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 15A.  
               TABLE 15A                       NOV15 Sequence Analysis                                                    SEQ ID NO: 35   9508 bp                             NOV15a,   TACTGCCACCATTGGAACTTTTGATGTTGATGGGGAAGAGTTGCAACACCTCCAGGGT           CG132086-01       DNA Sequence   TGTCCTGCTGATGGTGGCTGCGAAGATTTGCCTTGACAATAGCTGAAAAACCACCAT                   CTGCAACACGTGGGAGTAAGACTTCTCCTGCTCTTTGCCAGTGGTCTGACGTGATGAA                   CCACCCTGGCTTGGTGTGCTGTGTCCAGCAAACTACAGGGGTGCCGCTGGTAGTTATG                   GTGAAACCAGACACTTTTCTTATCCACGAGATTAAGACTCTTCCTGCTAAAGCGAAGA                   TCCAAGACATGGTTGCTATTAGGCACACGGCCTGCAATGAGCAGCAGCGGACAACAAT                   GATTCTGCTGTGTGAGGATGGCAGCCTGCGCATTTACATGGCCAACGTGGAGAACACC                   TCCTACTGGCTGCAGCCATCCCTGCAGCCCAGCAGTGTCATCAGCATCATGAAGCCTG                   TTCGAAAGCGCAAAACAGCTACAATCACAACCCGCACGTCTAGCCAGGTGACTTTCCC                   CATTGACTTTTTTOAACACAACCAGCAGCTGACAGATGTGGAGTTTGGTGGTAACGAC                   CTCCTACAGGTCTATAATGCACAACAGATAAAACACCGGCTGAATTCCACTGGCATGT                   ATGTGGCCAACACCAAGCCCGGAGGCTTCACCATTGAGATTAGTAACAACAATAGCAC                   TATGGTGATGACAGGCATGCGGATCCAGATTGGGACTQAAGCAATAGAACCGGCCCCG                   TCATATATCGAGATCTTCGGCACAACTATGCAGCTCAACCTGAGTCGCTCACGCTGGT                   TTGACTTCCCCTTCACCAGAGAAGAAGCCCTGCAGGCTGATAAGAAGCTGAACCTCTT                   CATTGGGGCCTCGGTGGATCCAGCAGGTGTCGCCATGATAGATGCTGTAAAAATTTAT                   GGCAAGACTAAGGACCAGTTTGGCTGGCCTGATGAGCCCCCAGAAGAATTCCCTTCTG                   CCTCTGTCAGCAACATCTOCCCTTCAAATCTGAACCAGAGCAACGGCACTGGAGATAG                   CGACTCAGCTGCCCCCACTACGACCAGTGOAACTGTCCTGGAGAGGCTGGTTGTGAGT                   TCTTTAGAGCCCTGGAAAGCTGCTTTGCCGTTGGCCCAATCATCGAGAAAGGAGAGAA                   ACAAGAATGCTGCTCAGGAGCTGGCCACTTTGCTGTTGTCCCTGCCAGCACCTGCCAG                   TGTCCAGCAGCAGTCCAAGAGCCTTCTGGCCAGCCTGCACACCAGCCGCTCGGCCTAC                   CACAGCCACAAGGATCAGGCCTTGCTGAGCAAAGCTGTGCAGTGTCTCAACACATCTA                   GCAAAGAGGGCAAGGATTTGGACCCTGAGGTGTTCCAGAGGCTAGTGATCACAGCTCG                   CTCCATTGCCATCATGCGCCCCAACAACCTTGTCCACTTTACGGAGTCAAAGCTGCCC                   CAGATGGAAACAGACTGTTTTTTTCCTAGATGTGCCTGCTGGAGTCTAGGGATAGTTG                   GCATATTGATTGGGGCCCCACTTGAAACTCCCTCCCCAGAAGGAATGGATGAAGGGAA                   GGAACCGCAGAAGCAGTTGGAAGGAGATTGCTGTAGTTTCATCACCCAGCTTGTGAAC                   CACTTCTGGAACTCCATGCATCCAAACCGAAAGAATGCCTTCTTGGCACCTGCCTGCC                   TTCCAGGACTAACTCATATTGAAGCTACTGTCAATGCTCTGGTGGACATCATCCATGG                   CTACTGTACCTGTGAGCTGGATTGTATTAACACAGCATCCAAGATCTACATGCAGATG                   CTCTTGTGTCCTGATCCTGCTGTGAGCTTCTCTTGTAAAGAAGCTCTAATTCGAGTCC                   TAAGGCCCAGGAACAAACGGAGACATGTGACTTTACCCTCTTCCCCTCGAAGCAACAC                   TCCAATGGGAGACAAGGATGATGATGACGATGATGATGCAGATGACAAAAAGCAGTCA                   TCAGGGATCCCGAATGGTGGTCACATCCGTCAGGAAGCCAGGAAACAGAGTGAGGTGG                   ACCATCGAGATTTTCAGATGGTGTCTCAGTCCATGGTCCTGGAGACAGCTGAAAATGT                   CAACAATGGCAACCCCTCTCCCCTGGAGGCCCTGCTGGCAGGCGCAGAGGGCTTCCCC                   CCCATGCTGGACATCCCACCTGATGCAGATGACGAGACCATGGTTGAACTAGCCATTG                   CCCTGAGCCTGCAGCAGGACCAACAAGCTCCAGCCTCAGACGACGAGGGCAGTACAGC                   AGCGACAGATGGTTCTACCCTTCGCACCTCTCCTGCTGACCACGGTGGTAGTGTGGGC                   TCGGAGAGCGGGGGCAGTGCAGTGGACTCAGTGGCTGGCGAGCACAGTGTATCTGGCC                   GGAGCAGTGCTTATGGCGATGCTACAGCTGAGGGGCATCCGGCTGGACCAGGAAGTGT                   CAGCTCAAGCACTGGAGCCATCAGCACCACCACTGGGCACCAGGAGGGAGATGGCTCC                   GAGGGAGAAGGAGAAGGAGAAACTGAAGGAGATGTCCACACTAGCAACAGGCTGCACA                   TGGTCCGTCTAATGCTGTTGGAGAGATTACTGCAGACCCTGCCTCAAATTACGAACGT                   TGGCGGTGTCCGGGCCATCCCATACATGCAGGTCATTCTAATGCTCACTACAGATCTG                   GATGGAGAAGATGAGAAAGACAAGQGGGCCCTAGACACCTCCTCTCCCAACTTATTAA                   CTGAGTTGGGTATGGATAAAAAGGATGTCTCCAAGAAGAATGAGCGCAGCGCCTGAAA                   TGAAGTCCATCTGGTAGTAAATGAGACTCCTGAGTGTCTTCATGTCCCCCACCAATCT                   GGATCCAAGTCTTCCATATGTGAGTCATCTTCCCTCATCTCCAGTGCCACAGCAGCAG                   CTCTACTGAGCTCTGGGGCTGTGGACTACTGCCTGCACGTGCTCAAATCACTGCTCGA                   ATATTGGAAGAGCCAACAGAATGACGAGGAGCCTGTGGCTACCAGCCAGTTGCTGAAA                   CCACATACTACCTCCTCCCCACCTGACATGAGCCCATTCTTTCTCCCCCAGTATGTGA                   AGGGTCATGCTGCTGATGTGTTTGAGGCCTATACTCAGCTTCTAACAGAAATGGTACT                   GAGGCTTCCTTACCATCAAAGATTACTGACACCAATTCTCGAATCCCACCTCCGGAAA                   GTCTTTGACCACTCGTGGTTTTACTTTCTCTCCGAGTACCTCATGATCCAGCAGACTC                   CATTTGTGCGCCGTCAAGTCCCCAACTTCTGCTCTTCATCTGTGGATCCAAGAAAAAA                   GTACCGCCAGCTCCGGGATTTGCACACCCTGGACTCTCACGTGCGTGGGATCAACAAG                   CTGCTAGAAGAGCAGGGGATATTCCTCCGGGCAAGTGTGGTTACAGCCAGCTCAGGCT                   CCGCCTTGCAATATGACACACTCATCAGCCTGATGGAGCACCTGAAAGCCTGTGCAGA                   GATTGCCGCCCAGCGAACCATCAAACTGGCAGAAATTCTGCATCAAGATGACTCCGTC                   CTGTACTTCCTCCTCCAAGTCAGTTTCCTTGTGGATGAGGGCGTGTCCCCAGTGCTGC                   TGCAACTGCTCTCCTGTGCTCTGTGCGGCAGCAAGGTGCTCGCTGCACTGCCAGCCTC                   TTCGGGATCCTCCAGTGCTTCTTCCTCCTCAGCCCCTGTGGCTGCCAGTTCTGGACAA                   GCCACAACACAGTCCAAGTCTTCCACTAAAAAGAGCAAGAAAGAAGAAAAAGAAAAGG                   AGAAAGATGGTGAGACCTCTGGCAGCCAGGAGGACCAGCTGTGCACAGCTCTGGTGAA                   CCAGCTGAACAAATTTGCCGATAAGGAAACCCTGATCCAGTTCCTGCGTTGTTTCCTG                   TTAGAGTCCAATTCTTCCTCGGTGCGCTGGCAGGCCCACTGTCTGACACTGCACATCT                   ACAGAAATTCCAGCAAATCTCAACAGGAGCTCCTGCTAGATCTGATGTGGTCCATCTG                   GCCAGAACTCCCAGCCTATGGTCGTAAGGCTGCCCAGTTTGTGGACCTACTAGGATAT                   TTCTCCCTGAACTCCACAACAGAGAAGAAGTTGAAGGAAGTATTCACAGAAAAGCTAA                   TGGAGATTCTGCGGACTCAAAACCATATTCTTACCAACCACCCCAACTCGAACATTTA                   TAACACTTTGTCTGGCTTAGTGGAGTTTGATGGCTATTACCTGGAGAGCGATCCCTGC                   CTGCTGTGTAATAACCCGGAAGTACCGTTCTGTTATATCAAGCTGTCTTCCATTAAAG                   TGGACACGCGGTACACCACCACCCAGCAGGTTGTGAAGCTCATTGGCAGTCACACCAT                   CAGCAAAGTGACAGTGAAATCGGGGATCTGAAACGGACCAIkGATGGTGCGGACCATC                   AACCTGTATTATAACACCGPACCGTGCAGGCCATCGTGGAGTTGAAACAAAAGCCAG                   CTCCCTGCCACAAAGCCAAGAAGGTTCAGCTGACCCCTGGACACACAGAGGTGAAGAT                   TGACCTGCCGTTGCCCATTGTGGCCTCCAATCTGATGATTGAGTTTGCAGACTTCTAT                   GAAAACTACCAGGCCTCCACAOAGACCCTGCAGTGCCCTCGCTGTAGTOCCTCGGTCC                   CTGCCAACCCAGGAGTCTGTGGCAACTGTGGAGAGAATGTGTACCAGTGTCACAAATG                   CAGATCCATCAACTACGATGAAAAGGATCCCTTCCTCTGCAATGCCTGTGGCTTCTGT                   AAATATGCCCGCTTCGACTTCATGCTCTATCACCAGCCTTGCTGTGCAGTGGATCCCA                   TTGAGAATGAAGAGACCGGAAGACGCTGTATCCAACATCAATACACTTTTGGACAAAA                   AGCTGATCGAGTGTATCATCAGCTGATGGGACACCGGCCACAGCTGGAGAACCTGCTC                   TGCAAAGTGAATGAGGCAGCTCCAGAAAAGCCACAGGATGACTCAGGAACAGCAGGGG                   GCATCAGCTCCACTTCTGCCAGTGTGAATCGTTACATCCTGCAGTTGGCTCAGGAGTA                   TTGTGGAGACTCCAAGAACTCTTTTGATGAACTCTCCAAATCATCCAGAAAGTCATTT                   GCTTCGCGCAAAGAGTTGTTGGAATATGACCTACAGCAGAGGGAAGCAGCACTAAAAT                   CATCCCGGACCTCCGTGCAGCCCACATTCACTGCCAGCCAGTACCGTGCCTTATCCGT                   CCTGGGCTGTGGCCACACATCCTCCACCAAGTGCTATGGCTGCGCCTCGGCTGTCACA                   GAACATTGTATCACACTACTTCGGGCCCTGGCCACCAACCCAGCCTTGAGGCACATCC                   TTGTCTCCCAGGGCCTTATCCGGGAGCTCTTTGATTATAATCTTCGCCGAGGGGCTGC                   GGCCATGCGGGAGGAGGTCCGCCAGCTCATGTGCCTCCTAACTCGAGACAAACCCAGA                   GCCACCCAACAGATGAATGACCTGATTATTCGCAAGGTCTCCACACCCCTGAAGGGCC                   ACTGGCCCAACCCCGATCTGGCAGTAGCCTGCAGTATGAAAATGCTGCTGCTGACGGA                   TTCTATCTCCAAGGAGGACAGCTGCTGGGAGCTCCGGTTACGCTGTGCTCTCAGCCTT                   TTCCTCATGGCTGTGAACATTAAGACTCCTGTGGTGGTTGAAAACATTACCCTCATGT                   GCCTGAGGATCTTGCAGAAGCTGATAAAACCACCTGCTCCCACTAGCAAGAAGAACAA                   GGATGTCCCCGTTGAGGCCCTCACCACGGTGAAOCCATACTGCAATGAGATCCATGCC                   CAGGCTCAACTGTGGCTCPIAAGAGAGACCCCAGGCATCCTATCATGCCTGGAAGAAT                   GTCTTCCTATCAGAGGGATAGATGGCAATCGGAAAAGCCCCCAGCAATCAGAGCTCCG                   CCATCTCTATTTGACTGAGAAGTATGTGTGGAGGTGGAAACAGTTCCTGAGTCGTCGG                   GGGAAGAGGACCTCCCCCTTGGATCTCACTGGGGCATAACAACTGGCTGCGACAAAAC                   TGCTTTTCACTCCAGCAACGCAGGCCGCACGGCAGGCAGCCTGTACCATTGTGGAAGC                   TCTAGCCACCATTCCCAGCCGCAAGCAGCAGGTCCTGGACCTGCTTACCAGTTACCTG                   GATGAGCTGAGCATAGCTGGGGAGTGTGCACCTGAGTACCTGGCTCTCTACCAGAAGC                   TCATCACTTCTGCGCACTGGAAAGTCTACTTGGCAGCTCGGGGAGTCCTACCCTATGT                   GGGCAACCTCATCACCAAGGAAATAGCTCGTCTGCTGGCCCTGGAGGAGGCTACCCTG                   AGTACCGATCTGCAGCAGCGTTATGCCCTTAAAGTCTCACAGGCCTTCTCTCCTCCTA                   TTGTTGAGGTGGAATCCATCAAAAAGACATTTTAAAGTCGCTTGGTGGGTACTGTGCT                   GAATGGATACCTGTGCTTGCGGAAGCTGGTGGTGCAGAGGACCAAGCTGATCGATGAG                   ACGCAGGACATGCTGCTGGACATGCTGGAGGACATGACCACAGGTACAGAAAAATCAG                   CCAAGGCCTTCATGGCTGTGTGCATTGAGACAGCCAAGCGCTACAAATCTGGATGACT                   CCGGACCCCGGTGTTCATCTTCGAGAGGCTCTGCAGCATCATTTATCCTGAGGAGAAT                   GAAGTCACTGAGTTCTTTGTGACCCTGGAGAAGGATCCCCAACAAGAAGACTTCTTAC                   AGGGCAGGATGCCTGGGAACCCGTATAGCAGCAATGAGCCAGGCATCGGGCCGCTGAT                   GAGGGATATAAAGAACAAGATTTGCCAGGACTGTGACTTAGTGGCCCTCCTGGAAGAT                   GACAGTGGCATGGAGCTTCTAGTGAZkCAATAAAATCATTAGTTTGGACCTTCCTGTG                   CTGAAGTTTACAAGAAAGTCTGGTGTACCACGAATGAGGGAGAGCCCATGAGGATTGT                   TTATCGTATGCGGGGGCTGCTGGGCGATGCCACAGAGGAGTTCATTGAGTCCCTGGAC                   TCTACTACAGATGAAGAAGAAGATGAAGAAGAAGTGTATAAAAATGGCTGGTGTGATG                   CCCAGTGTGGGGGCCTGGAATGCATGCTTAACAGACTCGCAGGGATCAGAGATTTCAA                   GCAGGGACGCCACCTTCTAACAGTGCTACTGAAATTGTTCAGTTACTGCGTGAAGGTG                   AAAGTCAACCGGCAGCAACTGGTCAAACTGGAAATGAACACCTTGAACGTCATGCTGG                   GGACCCTAACCTGGCCCTTGTAGCTGAACAAGAAAGCAAGGACAGTGGGGGTGCACCA                   TGTGGCTGAGCAGGTGCTTAGCATCATGGAGATCATTCTAGATGAGTCCAATGCTGAG                   CCCCTGAGTGAGGACAAGGGCAACCTCCTCCTGACAGGTGACAAGGATCAACTGGTGA                   TGCTCTTGGACCAGATCAACAGCACCTTTGTTCGCTCCAACCCCAGTGTGCTCCAGGG                   CCTGCTTCGCATCATCCCGTACCTTTCCTTTGGAGAGGTGGAGAAAATGCAGATCTTG                   GTGGAGCGATTCAAACCATACTGCAACTTTGATAAATATGATGAAGATCACAGTGGTG                   ATGATAAAGTCTTCCTGGACTGCTTCTGTAAATAGCTGCTGGCATCAAGAACAACAAG                   CAATGGGCACCAGCTGAAGGATCTGATTCTCCAGAAGGGGATCACCCAGATGCAACTT                   GACTACATGAAAAAGCACATCCCTAGCGCCAAGAATTTGGATGCCGACATCTGGAAAA                   AGTTTTTGTCTCGCCCAGCCTTGCCATTTATCCTAAGGCTGCTTCGGGGCCTGGCCAT                   CCAGCACCCTGGCACCCAGGTTCTGATTGGACTGATTCCATCCCGAACCTGCATAAAA                   CTGGACCAGGTGTCCAGTGATGAGGGCATTGGGACCTTGGCAGAGAACCTGCTGGAAA                   CCCTGCGGCAACACCCTGACGTAAACAAGAAGATTGACGCAGCCCGCAGGGAGACCCG                   GGCAGAGAAGAAGCGCATGGCCATGGCAATGAGGCAGAAGGCCCTGGGCACCCTGGGC                   ATGACGACAATGAAAAGCGCCACGTCGTGACCAAGACAGCACTCCTGAAAGCAGATGG                   AAGAGCTCATCGAGGAGCCTGGCCTCACGTGCTGCATCTGCAGGGAGGGATACAAGTT                   CCAGCCCACAAAGGTCCTGGGCATTTATACCTTCACGAAGCGGGTAGCCTTCGAGGAG                   ATGGAGAATAAGCCCCGGAAACAGCAGGGCTACAGCACCGTGTCCCACTTCAACATTG                   TGCACTACGACTGCCATCTGGCTGCCGTCAGGTTGGCTCGAGGCCGGGAAGAGTGGGA                   GAGTGCCGCCCTGCACAATGCCACACCTTAGTGCAACGGGCTCCTTCCGGTCTGGGGA                   CCTCATGTCCCTGAATCAGCTTTTGCCACTTGCTTGGCAAGACACAACACTTACCTCC                   AAAGCAATGTACAGGCCAGCGGGAGCCCACGTATCAGCTCACATCCATGACATCAACT                   GCTCTTCCTGCGCTTCGCCATGGAGCAGTCGTTCAGCGCAGACACTGGCGGGGGCGGC                   CGGGAGAGCAACATCCACCTGATCCCGTACATCATTCACACTGTGCTTTACGTCCTGA                   ACACACCCGAGCAACTTCCCGAGAAGAGAAGAACCTCCAAGGCTTTCTGGAAACAGCC                   CAAGGAGAAGTGGGTGGAGAGTGCCTTTGAAGTGGACGGGCCCTACTATTTCACAGTC                   TTGGCCCTTCACATCCTGCCCCCTGAGCAGTGGAGAGCCACACGTGTGGAAATCTTGC                   GCAGCCTGTTGGTGACCTCGCAGGCTCGGGCAGTGGCTCCAGGTGGAGCCACCAGGCT                   GACAGATAAGGCAGTGAAGGACTATTCCGCTTACCGTTCTTCCCTTCTCTTTTGGGCC                   CTCGTCGATCTCATTTACAACATGTTTAACAAGGTGCCTACCAGTAACACAGAGGGAG                   GCTGGTCCTGCTCTCTCGCTGAGTACATCCGCCACAACGACATGCCCATCTACGAAGC                   TGCCGACAAAGCCCTGAAAACCTTCCAGGAGGAGTTCATGCCAGTGGAGACCTTCTCA                   GAGTTCCTCGATGTGGCCGGTCTTTTATCAGAAATCACCGATCCAGAGAGCTTCCTGA                   AGGACCTGTTGAACTCAGTCCCC TGA   CCACCACACAGCAGCTGCGGCGGCGAAGACGA                       AGCTGGCTTGCCTTCCACCCTCTGTTCTCCCTCCTTGTGCATTAAGTTCCCTCCGCGG                       GATGCTGCATTGTTACCCCGCCCTCCCCTCTCTCATTTTTCTTGGTGTGGCTTGGGGT                       TTTTAGGCTTCCTGTTTTATCTCGTGTGTGTGGTGCACCAGCTATGAGGTTGTCTGTA                       ACCCAAGCCATCAAAGGGCCTGTACATACCTAGGAGCCATGAGTTGTCCCGGCCAGCT                       TCATACTTGAGTGTGCACATCTTGAGAAATAAACAAGTGACTTAACACACATTG                                           ORF Start: ATG at 170   ORF Stop: TGA at 9188                                         SEQ ID NO: 36   3006 aa   MW at 334825.2 kD                             NOV15a,   MNHPGLVCCVQQTTGVPLVVMVKPDTFLIHEIKTLPAKAKIQDMVAIRHTACNEQQRT           CG132086-01       Protein Sequence   TMILLCEDGSLRIYMANVENTSYWLQPSLQPSSVISIMKPVRKRKTATITTRTSSQVT                   FPIDFFEHNQQLTDVEFGGNDLLQVYNAQQIKHRLNSTGMYVANTKPGGFTIEISNNN                   STMVMTGMRIQIGTQAIERAPSYTIEIFGRTMQLNLSRSRWFDFPFTREALQADKKLN                   LFIGASVDPAGVAMIDAVKIYGKTKEQFGWPDEPPEEFPSASVSNICPSNLNQSNGTG                   DSDSAAPTTTSGTVLERLVVSSLEALESCFAVGPIIEKERNKNAAQELATLLLSLPAP                   ASVQQQSKSLLASLHTSRSAYHSHKDQALLSKAVQCLNTSSKEGKDLDPEVFQRLVIT                   ARSIAIMRPNNLVHFTESKLPQMETDCFFPRCACWSLGIVGILIGAPLETPSPEGMDE                   GKEPQKQLEGDCCSFITQLVNHFWKLHASKPKNAFLAPACLPGLTHIEATVNALVDII                   HGYCTCELDCINTASKIYMQMLLCPDPAVSFSCKQALIRVLRPRNKRRHVTLPSSPRS                   NTPMGDKDDDDDDDADEKMQSSGIPNGGHIRQESQEQSEVDHGDFEMVSESMVLETAE                   NVNNGNPSPLEALLAGAEGFPPMLDIPPDADDETMVELAIALSLQQDQQAPASDDEGS                   TAATDGSTLRTSPADHGGSVGSESGGSAVDSVAGEHSVSGRSSAYGDATAEGHPAGRG                   SVSSSTGAISTTTGHQEGDGSEGEGEGETEGDVHTSNRLHMVRLMLLERLLQTLPQLR                   NVGGVRAIPYMQVILMLTTDLDGEDEKDKGALDNLLSQLIAELGMDKKDVSKKNERSA                   LNEVHLVVMRLLSVFMSRTKSGSKSSICESSSLISSATAAALLSSGAVDYCLHVLKSL                   LEYWKSQQNDEEPVATSQLLKPHTTSSPPDMSPFFLRQYVKGHAADVFEAYTQLLTEM                   VLRLPYQIKKITDTNSRIPPPVFDHSWFYFLSEYLMIQQTPFVRRQVRKLLLFICGSK                   EKYRQLRDLHTLDSHVRGIKKLLEEQGIFLRASVATASSGSALQYDTLISLMEHLKAC                   AEIAAQRTINWQKFCIKDDSVLYFLLQVSFLVDEGVSPVLLQLLSCALCOSKVLAALA                   ASSGSSSASSSSAPVAASSGQATTQSKSSTKKSKKEEKEKEKDGETSGSQEDQLCTAL                   VNQLNKFADKETLIQFLRCFLLESNSSSVRWQAHCLTLHIYRNSSKSQQELLLDLMWS                   IWPELPAYGRKAAQFVDLLGYFSLKTPQTEKKLKEYSQKAVEILRTQNHILTNHPNSN                   IYNTLSGLVEFDGYYLESDPCLVCNNPEVPFCYIKLSSIKVDTRYTTTQQVVKLIGSH                   TI SKVTVKIGDLKRTKMVRTINLYYNNRTVQAIVELKNKPARWHKAKVQLTPGQTEV                   KIDLPLPIVASNLMIEFADFYENYQASTETLQCPRCSASVPANPGVCGNCGENVYQCH                   KCRSINYDEKDPFLCNACGFCKYARFDFMLYAKPCCAVDPIENEEDRKKAVSNINTLL                   DKADRVYHQLMGHRPQLENLLCKVNEAAPEKPQDDSGTAGGISSTSASVNRYILQLAQ                   EYCGDCKNSFDELSKIIQKVFASRKELLEYDLQQREAATKSSRTSVQPTFTASQYRAL                   SVLGCGHTSSTKCYGCASAVTEHCITLLRALATNPALRHILVSQCLIRELFDYNLRRG                   AAAMREEVRQLMCLLTRDNPEATQQMNDLIIGKVSTALKGHWANPDLASSLQYEMLLL                   TDSISKEDSCWELRLRCALSLFLMAVNIKTPVVVENITLMCLRILQKLIKPPAPTSKK                   NKDVPVEALTTVKPYCNEIHAQAQLWLKRDPKASYDAWKKCLPIRGIDGNGKAPSKSE                   LRHLYLTEKYVWRWKQFLSRRGKRTSPLDLKLGHNNWLRQVLFTPATQAARQAACTIV                   EALATIPSRKQQVLDLLTSYLDELSIAGECAAEYLALYQKLITSAHWKVYLAARGVLP                   YVGNLITKEIARLLALEEATLSTDLQQGYALKSLTGLLSSFVEVESIKRHFKSRLVGT                   VLNGYLCLRKLVVQRTKLIDETQDMLLEMLEDMTTGTESETKAFMAVCIETAKRYNLD                   DYRTPVFIFERLCSIIYPEENEVTEFFVTLEKDPQQEDFLQGRMPGNPYSSNEPCICP                   LMRDIKNKICQDCDLVALLEDDSGMELLVNNKIISLDLPVAEVYKKVWCTTNEGEPMR                   IVYRMRGLLCDATEEFIESLDSTTDEDEEEVYKAVIAGVMAQCGGLECMLNRLAGIRD                   FKQGRHLLTVLLKLFSYCVKVKVNRQQLVKLEMNTLNTMLGTLNLALVAEQESKDSCG                   AAVAEQVLSIMEIILDESNAEPLSEDKGNLLLTGDKDQLVMLLDQINSTFVRSNPSVL                   QGLLRIIPYLSFGEVEKMQILVERFKPYCNFDKYDEDHSGDDKVFLDCFCKLAAGIKN                   NSNGHQLKDLILQKGITQNLDYMKKHIPSAKNLDADIWKKFLSRPALPFIYLRLLRGL                   ATQHPGTQVLIGTDSIPNLHKLEQVSSDEGIGTLAENLLEALREHPDVNKKIDAARRE                   TRAEKKRMAMRQKALGTLGMTTNEKGQVATKTALLKQMEELIEEPGLTCCICREGYAA                   KFQPTKVLGIYTFTKRVALEEMENKPRKQQGYSTVSHFNIVHYDCHLAAVRLARGREE                   WESAALQNANTKCNGLLPVWGPHVPESAFATCLARHNTYLQECTGQREPTYQLNIHDI                   QPKEKWVESAFEVDGPYYFTVLALHILPPEQWRATRVEILRRLLVTSQARAVPGGATA                   RLTDKAVKDYSAYRSSLLFWALVDLIYNMFKKVPTSNTEGGWSCSLAEYIRHNDMPIY                   IEAADKALKTFQEEFMPVETFSEFLDVAGLLSEITDPESFLKDLLNSVP                  
 
     [0408] Further analysis of the NOV15a protein yielded the following properties shown in Table 15B.  
               TABLE 15B                       Protein Sequence Properties NOV15a                                        PSort   0.6850 probability located in endoplasmic reticulum       analysis:   (membrane); 0.6400 probability located in plasma membrane;           0.4600 probability located in Golgi body; 0.1800           probability located in nucleus       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0409] A search of the NOV15a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 15C.  
               TABLE 15C                          Geneseq Results for NOV15a                                         NOV15a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value                                         AAY53675   Mechanical stress induced protein   1 . . . 2938   2834/2974 (95%)   0.0           274 amino acid sequence - Rattus   318 . . . 3262    2881/2974 (96%)           sp, 3262 aa. [WO9960164-A1, 25           NOV. 1999]       AAU28088   Novel human secretory protein,   584 . . . 3006    2423/2458 (98%)   0.0           Seq ID No 257 -  Homo sapiens ,   1 . . . 2458   2423/2458 (98%)           2458 aa. [WO200166689-A2, 13           SEP. 2001]       AAM39071   Human polypeptide SEQ ID NO   584 . . . 3006    2421/2458 (98%)   0.0           2216 -  Homo sapiens , 2458 aa.   1 . . . 2458   2423/2458 (98%)           [WO200153312-A1, 26 JUL.           2001]       AAY53677   Sequence   731 . . . 3006    2276/2278 (99%)   0.0           gi/3413886/dbj/BAA323071 from   1 . . . 2278   2276/2278 (99%)           an alignment with protein 274 -           Unidentified, 2278 aa.           [WO9960164-A1, 25 NOV. 1999]       AAM40857   Human polypeptide SEQ ID NO 5788 -   731 . . . 3006    2246/2281 (98%)   0.0             Homo sapiens , 2281 aa.   1 . . . 2281   2253/2281 (98%)           [WO200153312-A1, 26 JUL.           2001]                  
 
     [0410] In a BLAST search of public sequence datbases, the NOV15a protein was found to have homology to the proteins shown in the BLASTP data in Table 15D.  
               TABLE 15D                          Public BLASTP Results for NOV15a                                         NOV15a   Identities/           Protein   Protein/   Residues/   Similarities for       Accession   Organism/   Match   the Matched   Expect       Number   Length   Residues   Portion   Value                                         Q8TDN5   Retinoblastoma-associated   1 . . . 3006   2974/3041 (97%)   0.0           factor 600 -  Homo sapiens     2171 . . . 5183     2975/3041 (97%)           (Human), 5183 aa.       O75050   KIAA0462 protein -  Homo     731 . . . 3006     2276/2276 (100%)   0.0             sapiens  (Human), 2276 aa   1 . . . 2276    2276/2276 (100%)           (fragment).       Q9XYD2   PUSHOVER -  Drosophila     3 . . . 3006   1330/3157 (42%)   0.0             melanogaster  (Fruit fly), 5322   2303 . . . 5316     1891/3157 (59%)           aa.       Q9VLT5   CG14472 protein -  Drosophila     3 . . . 3006   1329/3157 (42%)   0.0             melanogaster  (Fruit fly), 5322   2303 . . . 5316     1892/3157 (59%)           aa.       O96958   CALO protein -  Drosophila     3 . . . 3006   1327/3155 (42%)   0.0             melanogaster  (Fruit fly), 4116   1097 . . . 4110     1890/3155 (59%)           aa (fragment).                  
 
     [0411] PFam analysis indicates that the NOV15a protein contains the domains shown in the Table 15E.  
               TABLE 15E                          Domain Analysis of NOV15a                                             Identities/                   NOV15a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                                                 Tub   1417 . . . 1437    8/21 (38%)   0.13                   17/21 (81%)                      
 
     Example 16  
     [0412] The NOV16 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 16A.  
               TABLE 16A                       NOV16 Sequence Analysis                                                    SEQ ID NO: 37   2178 bp                             NOV16a,     TTGACTGTATCGCCGGAATTC   ATG GCGGGTCTGACGGCGGCGGCCCCGCGGCCCGGAG           CG132297-01       DNA Sequence   TCCTCCTGCTCCTGCTGTCCATCCTCCACCCCTCTCGGCCTGGAGGGGTCCCTGGGGC                   CATTCCTGGTGGAGTTCCTGGAGGAGTCTTTTATCCAGGGGCTGGTCTCGGAGCCCTT                   GGAGGAGGAGCGCTGGGGCCTGGAGGCAAACCTCTTAAGCCAGTTCCCGGAGGGCTTG                   CGGGTGCTGGCCTTGGGGCAGGGCTCGGCGCCTTCCCCGCAGTTACCTTTCCGGGGGC                   TCTGGTGCCTGGTGGAGTGGCTGACGCTGCTGCAGCCTATAAAGCTGCTAAGGCTGGC                   GCTGGGCTTGGTGGTGTCCCAGGAGTTGGTGGCTTAGGAGTGTCTGCAGCCCCTTCTG                   TGCCAGGTGCGGTGGTTCCTCAGCCTGGAGCCGGAGTGAAGCCCGGGAAAGTGCCGGG                   TGTGGGGCTGCCAGGTGTATACCCAGGTGGCGTGCTCCCAGGAGCTCGGTTCCCCGGT                   GTGGGGGTGCTCCCTGGAGTTCCCACTGGAGCAGGAGTTAAGCCCAAGGCTCCAGGTG                   TAGGTGGAGCTTTTGCTGGAATCCCAGGAGTTGGACCCTTTGGGGGACCGCAACCTGG                   AGTCCCACTCGGGTATCCCATCAAGGCCCCCAAGCTGCCTGGTGGCTATGGACTGCCC                   TACACCACAGGGAAACTGCCCTATGGCTATGGGCCCGGAGGAGTGGCTGGTGCAGCGG                   GCAAGGCTGGTTACCCAACAGGGACAGGGGTTGCCCCCCAGGCAGCAGCAGCACCGGC                   AGCTAAAGCAGCAGCAAAGTTCGGTGCTGGAGCAGCCCGAGTCCTCCCTGGTCTTGGA                   GGGGCTGGTGTTCCTGGCGTGCCTGGGGCAATTCCTGGAATTGGACGCATCGCAGCCG                   TTGGGACTCCAGCTGCAGCTGCAGCTGCAGCAGCGGCCGCTAAGGCAGCCAAGTATGG                   AGCTGCTGCAGGCTTAGTGCCTGGTGGGCCAGGCTTTGGCCCGGGAGTAGTTGGTGTC                   CCAGGAGCTGGCGTTCCAGGTGTTGGTGTCCCAGGAGCTGGGATTCCAGTTGTCCCAG                   GTGCTGGGATCCCAGGTGCTGCGGTTCCAGGGGTTGTGTCACCAGAAGCAGCTGCTAA                   GGCAGCTGCAAAGGCAGCCAAATACGGGGCCAGGCCCGGAGTCGGAGTTGGAGGCATT                   CCTACTTACGGGGTTGGAGCTGGGGGCTTTCCCGGCTTTGGTGTCGGAGTCGGAGGTA                   TCCCTGGAGTCGCAGGTGTCCCTAGTGTCGGAGGTGTTCCCGGAGTCGGAGGTGTCCC                   GGGAGTTGGCATTTCCCCCGAAGCTCAGGCAGCAGCTGCCGCCAAGGCTGCCAAGTAC                   GGAGTGGGGACCCCAGCAGCTGCAGCTGCTAAAGCAGCCGCCAAAGCCGCCCAGTTTG                   GGTTAGTTCCTGGTGTCGGCGTGGCTCCTGGAGTTGGCGTGGCTCCTGGTGTCGGTGT                   GGCTCCTGGAGTTGGCTTGGCTCCTGGAGTTGGCGTGGCTCCTGGAGTTGGTGTGGCT                   CCTGGCGTTGGCGTGGCTCCCGGCATTGGCCCTGGTGGAGTTGCAGCTGCAGCAAAAT                   CCGCTGCCAAGGTGGCTGCCAAAGCCCAGCTCCGAGCTGCAGCTGGGCTTGGTGCTGG                   CATCCCTGGACTTGGAGTTGGTGTCGGCGTCCCTGGACTTGGAGTTGGTGCTGGTGTT                   CCTGGACTTGGAGTTGGTGCTGGTGTTCCTGCCTTCGGGGCAGTACCTGGAGCCCTGG                   CTGCCCCTAGAGCAGCCAAATATGGAGCAGCAGTGCCTGGGGTCCTTGGAGGGCTCGG                   GGCTCTCGGTCCACTAGGCATCCCAGGCGGTGTGGTGGGAGCCGGACCCGCCGCCGCC                   GCTGCCGCAGCCAAAGCTGCTGCCAAAGCCGCCCAGTTTGGCCTAGTGGGAGCCGCTG                   GGCTCGGAGGACTCGCAGTCGGAGGGCTTGGAGTTCCAGGTGTTGGGGGCCTTGGAGG                   TATACCTCCAGCTGCAGCCGCTAAAGCAGCTAAATACGGAGTGGCAGCAAGACCTGGC                   TTCGGATTGTCTCCCATTTTCCCAGGTGGGGCCTGCCTGGGCAAAGCTTGTGGCCGGA                   AGAGAAAATGACTGCAGCCAAGCTAATTCCGG                                         ORF Start: ATG at 22   ORF Stop: TGA at 2155                                         SEQ ID NO: 38   711 bp   MW at 61662.7 kD                             NOV16a,   MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGP           CG132297-01       Protein Sequence   GCKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAYKAAAKAGAGLGCVP                   GVGGLGVSAAPSVPGAVVPQPGAGVKPGKVPCVGLPGVYPCCVLPGARFRGVGVLPGV                   PTGAGVKPKAPGVGCGFAGIPGVGPFGGPQPGVPLGYPIKAPKLPGGYGLPYTTGKLP                   YGYGPGGVAGAAGKAGYPTGTGVCPQAAAAAAAKAAAKFGAGAAGVLPGVGGAGVPGV                   PGAIPGIGGIAGVGTAAAAAAAAAAKAAKYGAAAGLVPGGPCFGPGVVGVPGAGVPGA                   VGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKMAKAAKYGARRGVGVGCIPTYGVGAA                   GGFPGFGVGVGGIPGVAGVPSVGGVPGVCGVPGVGISPEAQAAAAAKAAKYGVGTPAA                   AAAKAAAKAAQFGLVPGVGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAP                   GIGPGGVkAAAKSAAKVAAKAQLRAAAGLGAGIPGLGVGVGVPGLGVCAGVPGLGVGA                   GVPGFGAVPGALAAARAAKYGAAVPGVLGGLCALGGVGIPGGVVGAGPAAAAAYAAAA                   AKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAAAAKAAKYGVAARPGFGLSPIF                   PGGACLGKACGRKRK                                         SEQ ID NO: 39   2100 bp                             NOV16b,     TTGACTGTATCGCCGGAATTC   ATG GCGGGTCTGACGGCGGCGGCCCCGCGGCCCGGAG           CG132297-02       DNA Sequence   TCCTCCTGCTCCTGCTGTCCATCCTCCACCCCTCTCGGCCTGGAGGGGTCCCTCGGGC                   CATTCCTGCTGGAGTTCCTGGAGGAGTCTTTTATCCAGGCGCTGGTCTCGGAGCCCTT                   GGAGCAGGAGCGCTGGGGCCTGGAGGCAAACCTCTTAAGCCAGTTCCCGGAGGGCTTG                   CGGGTGCTGGCCTTCGGGCAGGGCTCGGCGCCTTCCCCGCAGTTACCTTTCCCGGGGC                   TCTGGTGCCTGGTGGAGTCCCTGACGCTGCTGCAGCCTATAAAGCTGCTAAGGCTGGC                   GCTCGGCTTGGTGGTGTCCCAGGAGTTGGTGGCTTAGGAGTGTCTGCAGGTGCCGTGG                   TTCCTCAGCCTGGAGCCGGAGTGAAGCCTGGGAAAGTGCCGGGTGTACGTGGAGCTTT                   TGCTGCAATCCCAGGAGTTGGACCCTTTGGGGGACCGCAACCTGGAGTCCCACTGGGG                   TATCCCATCAAGGCCCCCAAGCTGCCTGGTGGCTATGGACTGCCCTACACCACAGGGA                   AACTGCCCTATGGCTATGGGCCCGGAGGAGTGGCTGGTGCAGCGGGCAAGGCTGGTTA                   CCCAACAGGGACAGGGGTTGGCCCCCAGGCAGCAGCAGCAGCGGCAGCTAAGCACCAA                   GCAAAGTTCGGTGCTGGAGCAGCCGGAGTCCTCCCTGGTGTTGGAGGGGCTGGTGTTC                   CTGGCGTGCCTGGGGCAATTCCTGGAATTGGAGGCATCGCAGGCGTTGGGACTCCAGC                   TGCAGCTGCAGCTGCAGCAGCAGCCGCTAAGGCAGCCAAGTATCGAGCTGCTGCAGGC                   TTAGTGCCTGGTGGCCCAGGCTTTGGCCCGGGAGTAGTTGGTGTCCCAGGAGCTGGCG                   TTCCAGGTGTTGGTGTCCCAGGAGCTGGGATTCCAGTTGTCCCAGGTGCTGGGATCCC                   AGGTGCTGCGGTTCCAGGGGTTGTGTCACCAGAAGCAGCTGCTAAGGCAGCTGCAAAG                   GCAGCCAAATACGGGGCCAGGCCCGCAGTCGGAGTTGGAGGCATTCCTACTTACGGGG                   TTGGAGCTGGGGGCTTTCCCGGCTTTGGTGTCGGAGTCGGAGGTATCCCTGGAGTCGC                   AGGTGTCCCTAGTGTCGGAGGTGTTCCCGGAGTCGGAGGTGTCCCGGGAGTTGGCATT                   TCCCCCGAAGCTCAGGCAGCAGCTGCCGCCAAGGCTGCCAAGTACGGAGTGGGGACCC                   CAGCAGCTGCAGCTGCTAAAGCAGCCGCCAAAGCCGCCCAGTTTGCTCTTCTCAATCT                   TCCAGGGTTAGTTCCTGGTGTCGGCGTGGCTCCTGGAGTTGGCGTGGCTCCTGGTGTC                   GGTGTGGCTCCTGGAGTTGGCTTGGCTCCTGGAGTTGGCGTGGCTCCTGGAGTTGGTG                   TGGCTCCTGGCGTTGGCGTGGCTCCCGGCATTGGCCCTGGTGGAGTTGCAGCTGCAGC                   AAAATCCGCTGCCAAGGTGGCTGCCAAAGCCCAGCTCCGAGCTGCAGCTGGGCTTGGT                   GCTGGCATCCCTGGACTTGGAGTTCGTGTCGGCGTCCCTGGACTTGGAGTTGGTGCTG                   GTGTTCCTGGACTTGGACTTGGTGCTGGTGTTCCTGGCTTCGGGGCAGTACCTGGAGC                   CCTGGCTGCCGCTAAAGCAGCCAAATATGGAGCAGCAGTGCCTGGGGTCCTTGGAGGG                   CTCGGGGCTCTCGGTGGAGTAGGCATCCCAGGCGGTGTGGTGGGAGCCGGACCCGCCG                   CCGCCGCTGCCGCAGCCAAAGCTGCTGCCAAAGCCGCCCAGTTTGCCCTAGTGGGAGC                   CGCTGGGCTCGGAGGACTCGGAGTCCGAGGGCTTGGAGTTCCAGGTGTTGGGGGCCTT                   GGAGGTATACCTCCAGCTGCAGCCGCTAAAGCAGCTAAATACGGTGCTGCTGGCCTTG                   GAGGTGTCCTAGGGGGTGCCGGGCAGTTCCCACTTGGAGGAGTGGCAGCAGAACCTGG                   CTTCGGATTGTCTCCCATTTTCCCAGGTGGGGCCTGCCTGGGGAAAGCTTGTGGCCGG                   AAGAGAAAATGA                                         ORF Start: ATG at 22   ORF Stop: TGA at 2098                                         SEQ ID NO: 40   692 aa   MW at 59784.4 kD                             NOV16b,   MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGP           CG132297-02       Protein Sequence   GGKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAKAAAAYAGAGLGGVP                   GVGGLGVSAGAVVPQPGAGVKPGKVPGVGGAFAGIPGVGPFGGPQPGVPLGYPIKAPK                   LPGGYGLRYTTGKLPYGYGPGGVAGAAGKAGYPTGTGVGPQAAAAAAAKAAAKFGAGA                   AGVLPGVGGAGVPGVPGAIPGIGGIAGVGTRAAAAAAAAAAAKAAKYGAAAGLVRGGP                   FGPGVVGVPGAGVPGVGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKAAAKAAKYGAR                   PGVGVGGIPTYGVGAGGFPGFCVGVGGIPGVAGVPSVGGVPGVGGVPGVGISPEAQAA                   AAAKAAKYGVGTPAAAAAKAAAKAAQFALLNLAGLVPGVGVAPGVGVAPGVGVAPGVG                   LAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAAKSAAKVAAKAQLRAAAGLCAGIPGLG                   VGVGVPGLGVGAGVPGLGVGAGVPGFGAvPGALAAAKAAKYGAAVPGVLGGLGALGGV                   GIPGGVVGAGPAAAAAAAKAAAKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAA                   AAKAAKYGAAGLGGVLGGAGQFPLGGVAARPGFGLSPTFPGGACLGKACGRKRK                  
 
     [0413] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 16B  
               TABLE 16B                          Comparison of NOVl6a against NOV16b.                                 Identities/               Similarities       Protein   NOV16a Residues/   for the       Sequence   Match Residues   Matched Region               NOV16b   686 . . . 711   26/26 (100%)           667 . . . 692   26/26 (100%)                  
 
     [0414] Further analysis of the NOV16a protein yielded the following properties shown in Table 16C.  
               TABLE 16C                       Protein Sequence Properties NOV16a                                        PSort   0.4323 probability located in outside; 0.1376 probability       analysis:   located in microbody (peroxisome); 0.1000 probability located           in endoplasmic reticulum (membrane); 0.1000 probability           located in endoplasmic reticulum (lumen)       SignalP   Cleavage site between residues 27 and 28       analysis:                  
 
     [0415] A search of the NOV16a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 16D.  
               TABLE 16D                          Geneseq Results for NOV16a                                         NOV16a   Identities/                   Residues/   Similarities for       Geneseq   Protcin/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value                                         AAB08630   Amino acid sequence of a human   1 . . . 711   704/717 (98%)   0.0           elastin polypeptide -  Homo sapiens ,   1 . . . 712   705/717 (98%)           712 aa. [WO200050068-A2, 31           AUG. 2000]       AAB08631   Fusion protein comprising human   2 . . . 711   703/716 (98%)   0.0           elastin and c-myc - Synthetic, 730   11 . . . 721    704/716 (98%)           aa. [WO200050068-A2, 31 AUG.           2000]       AAY69069   Amino acid sequence of a human   27 . . . 711    679/703 (96%)   0.0           reduced tropoelastin derivative -   1 . . . 698   680/703 (96%)           Synthetic, 698 aa. [WO200004043-           A1, 27 JAN. 2000]       AAY01302   Human tropoelastin variant   27 . . . 711    679/703 (96%)   0.0           SHELdelta26A -  Homo sapiens ,   1 . . . 698   680/703 (96%)           698 aa. [WO9903886-A1, 28 JAN.           1999]       AAW46315   Human elastin containing non-   27 . . . 711    679/735 (92%)   0.0           natural polypeptide MFU-1   1 . . . 730   680/735 (92%)           sequence -  Homo sapiens , 730 aa.           [WO9805685-A2, 12 FEB. 1998]                  
 
     [0416] In a BLAST search of public sequence datbases, the NOV16a protein was found to have homology to the proteins shown in the BLASTP data in Table 16E.  
               TABLE 16E                          Public BLASTP Results for NOV16a                                             Identities/                   NOV16a   Similarities for       Protein       Residues/   the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value                                         P15502   Elastin precursor (Tropoelastin) -   1 . . . 711   705/735 (95%)   0.0             Homo sapiens  (Human), 730 aa.   1 . . . 730   706/735 (95%)       Q14234   Elastin -  Homo sapiens  (Human),   1 . . . 711   705/762 (92%)   0.0           757 aa.   1 . . . 757   706/762 (92%)       Q14235   Elastin -  Homo sapiens  (Human),   1 . . . 711   686/711 (96%)   0.0           687 aa.   1 . . . 687   687/711 (96%)       EAHU   elastin precursor, long splice   1 . . . 711   705/797 (88%)   0.0           form - human, 792 aa.   1 . . . 792   706/797 (88%)       O15337   Elastin -  Homo sapiens  (Human),   29 . . . 600    565/607 (93%)   0.0           602 aa (fragment).   1 . . . 602   566/607 (93%)                  
 
     [0417] PFam analysis indicates that the NOV16a protein contains the domains shown in the Table 16F.  
               TABLE 16F                          Domain Analysis of NOV16a                                             Identities/                   NOV16a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                             No Significant Matches Found                  
 
     Example 17  
     [0418] The NOV17 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 17A.  
               TABLE 17A                       NOV17 Sequence Analysis                                                    SEQ ID NO: 41   1072 bp                             NOV17a,     ATCCGAGTCACCTGCAGGACCGAA   ATG GAGGAGAGAGCACAGCACTGCCTGTCCAGAT           CG132343-01       DNA Sequence   TACTAGACAACTCTGCCCTGAAGCAGCAGCAGTTACCCATACACCGGCTATATTTCAC                   GGCCAGGAGAGTCCTCTTTGTCTTTTTCGCAACAGGAATATTCTGCCTTTGTATGGGC                   ATCATCCTTATATTGTCTGCAAGGAGCACTCAGGAAATAGAGGTTAATTACACAAGAA                   TATGTGCAAATTGTGCAAAACTGCGAGAAATGCCTCTIAATTTTGACAAGGAATGCAC                   CTGCTCTATTCCCTTTTACCTTTCAGGAAAAATGCAGGGTAATGTTTATATGTACTAC                   AAATTGTATGGCTTCTATCAGAACCTGTATCTATATATTCGATCCAGAAGTAATAGAC                   AACTGGTGGGCAAAGATGTAAAAGTAGTTGAGGATTGTGCCCCATTTAAAATGTCCGA                   CAATAAGACCCCCATCGTTCCTTGTGGTGCTATTGCCAACAGCATGTTCAATGACACC                   ATAATTCTTTCACACAACATTAATTCATCTGTACAAATCAAAGTGCCAATGTTAAAGA                   GTAGACTTACGTGGTGGACAGATAGTATGTCAAATTTCAGAAAATCTAAGTTTCAAGA                   TCTTGCTGATGATTTAGAGGTACCACAAAGCCCCCAACTGGCCCIAAAGCCTATCTAT                   AACTTGGATAAAAAGGATCCAAGAAACAATGGCTTCCTCAATGATGACTTCATTGTGT                   GGATGCGGGCAGCTGCCTTTCCCACTTTCAAAAAACTGTATGGTCGACTCAGTCGAAC                   ACACCATTTTATAGAAGGCTTGCCTGCTGGTAATTATAGTTTCAACATAACCTATAGT                   TTCCCAGTAACCAGGTTCCACGGAGAAAAATCAGTTGTTCTCTCCACCCTGACATGGT                   GTGGGGGTAATAGCCTTTTCTTAGGTCTTGCCTACACAGTGACAGGAGCTATGACATG                   GTTGGCCTCCTTTGCCATGATGGCAATTCACATCATGCTGAAAAAAACAAGAATGTCC                   TTCTTCCATCAA TAA   AGTCAAGCTTTA A                                         ORF Start: ATG at 25   ORF Stop: TAA at 1057                                         SEQ ID N0 42   344 aa   MW at 39698.8 kD                             NOV17a,   MEERAQHCLSRLLDNSALKQQELPIHRLYFTARRVLFVFFATGIFCLCMCIILILSARAA           CG132343-01       Protein Sequence   STQEIEVNYTRICANCAKLRENASNFDKECTCSIPFYLSGKMQGNVYMYYKLYGFYQNAA                   LYLYIRSRSNRQLVGKDVKVVEDCAPFKMSDNKTPIVPCGAIAASMFNDTIILSHNINAA                   SSVQIKVPMLKSRLTWWTDKYVKFQNLSFKNLADEFRGTTKPPNWPKPIYDLDKKDPR                   INNGFLNDDFIVWMRAAFPTFKKLYGRLSRTHHFIEGLPAGNYSFNITYSFPVTRFHG                   EKSVVLSTLTWCGGNSLFLGLAYTVTGAMTWLASFAMMAIHIMLKNKKAVISFFHQ                  
 
     [0419] Further analysis of the NOV17a protein yielded the following properties shown in Table 17B.  
               TABLE 17B                       Protein Sequence Properties NOV17a                                        PSort   0.7900 probability located in plasma membrane; 0.7294       analysis:   probability located in microbody (peroxisome); 0.3000           probability located in Golgi body; 0.2000 probability           located in endoplasmic reticulum (membrane)       SignalP   Cleavage site between residues 60 and 61       analysis:                  
 
     [0420] A search of the NOV17a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 17C.  
               TABLE 17C                          Geneseq Results for NOV17a                                         NOV17a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAB93258   Human protein sequence SEQ ID   10 . . . 336   147/336 (43%)   6e−74           NO: 12282 -  Homo sapiens , 361 aa.   25 . . . 352   206/336 (60%)           [EP1074617-A2, 07 FEB. 2001]       AAY28810   nn296_2 secreted protein -  Homo     10 . . . 336   147/336 (43%)   6e−74             sapiens , 361 aa. [WO9950405-A1,   25 . . . 352   206/336 (60%)           07 OCT. 1999]       ABB64777     Drosophila melanogaster     3 . . . 343   141/349 (40%)   3e−65           polypeptide SEQ ID NO 21123 -   9 . . . 349   203/349 (57%)             Drosophila melanogaster , 357 aa.           [WO200171042-A2, 27 SEP. 2001]       ABG20423   Novel human diagnostic protein   10 . . . 336   138/336 (41%)   5e−65           #20414 -  Homo sapiens , 430 aa.   94 . . . 421   194/336 (57%)           [WO200175067-A2, 11 OCT. 2001]       ABG20423   Novel human diagnostic protein   10 . . . 336   138/336 (41%)   5e−65           #20414 -  Homo sapiens , 430 aa.   94 . . . 421   194/336 (57%)           [WO200175067-A2, 11 OCT. 2001]                  
 
     [0421] In a BLAST search of public sequence datbases, the NOV17a protein was found to have homology to the proteins shown in the BLASTP data in Table 17D.  
               TABLE 17D                          Public BLASTP Results for NOV17a                                         NOV17a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q95JK4   Hypothetical 39.5 kDa protein -   1 . . . 344   324/344 (94%)   0.0             Macaca fascicularis  (Crab eating   1 . . . 344   330/344 (95%)           macaque) (Cynomolgus monkey),           344 aa.       Q95JU6   Hypothetical 33.9 kDa protein -   1 . . . 282   268/282 (95%)   e−160             Macaca fascicularis  (Crab eating   1 . . . 282   271/282 (96%)           macaque) (Cynomolgus monkey),           292 aa.       Q9D4D7   4933401B01Rik protein -  Mus     1 . . . 341   229/341 (67%)   e−135             musculus  (Mouse). 342 aa.   1 . . . 341   272/341 (79%)       Q9UGC2   DJ234P15.3 (novel protein similar   10 . . . 336    147/336 (43%)   2e−73            to (predicted) yeast and worm   23 . . . 350    206/336 (60%)           proteins) -  Homo sapiens             (Human), 359 aa.       Q9NV96   CDNA FLJ10856 fis, clone   10 . . . 336    147/336 (43%)   2e−73            NT2RP4001547 -  Homo sapiens     25 . . . 352    206/336 (60%)           (Human), 361 aa.                  
 
     [0422] PFam analysis indicates that the NOV17a protein contains the domains shown in the Table 17E.  
               TABLE 17E                          Domain Analysis of NOV17a                                             Identities/                       Similarities           Pfam   NOV17a Match   for the   Expect           Domain   Region   Matched Region   Value                             No Significant Matches Found                  
 
     Example 18  
     [0423] The NOV18 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 18A.  
               TABLE 18A                       NOV18 Sequence Analysis                                                    SEQ ID NO: 43   1084 bp                             NOV 18a,     GAAGCTTCTGGATCCTACGCTCATCTCTACAGAGGAGAA CATGCACGCAGCAGAGATC           CG132423-01       DNA Sequence   ATGGGGCCCCTCTCAGCCCCTCCCTGCACAGAGCACATCAAATGGAAGGGGCTCCTGC                   TCACAGCATTACTTTTAAACTTCTGGAACTTGCCTACCACTGCCCAAGTCATGATTGA                   AGCCCAGCCACCCAAAGTGTCCGAGGGGAAGGATGTTCTTCTACTTGTCCAAATCAGG                   GACCTCTACCATTACATTACATCATATGTAGTAGACGGTCAATAAATTATATATGGAC                   CGGCATACAGTGGACGAGAAACAGTATATTCCAATGCATCCCTGCTGATCCAGAATGT                   CACCCGGGAGGACGCAGGATCCTACACCTTACACATCATAAAGCGAGGTGATCGGACT                   AGAGGAGTAACTGGATATTTCACCTTCACCTTATACCTGGAGACTCCCAAGCCCTCCA                   TCTCCAGCAGCAACTTAACCCCAGGGAGGCCATGGAGACTGTGATCTTAACCTGTAAA                   TCCTGAGACTCCGGACGCAAGCTACCTGTGGTGGATGAATGGTCAGAGCCTCCCTATG                   ACTCATAGGATGCAGCTGTCTGAAACCAACAGGACCCTCTTTCTATTTAGTGTCACAA                   AGTATACTGCAGGACCCTATGAATGTGAAATATGGAACTCAGGGAGTGCCAGCCGCAG                   TGACCCAGTCACCCTGAATCTCCTCCATGGTCCAGACCTCCCCACAATTTTCCCTTCA                   GTCACCTCTTACTATTCAGCAGAGAACCTCGACTTGTCCTGCTTCGCAGACTCTAACC                   CACCAGCACAGTATTCTTGGACAATTAAATGGGAAAGTTTCAGCTATCAGGACAAACT                   CTTTATCCCTCAATTACTCCAAAGCATAATGGGCTCTATGCTTGCTCTGCTCGTAAAC                   TCAGCCACTGGCGAGGAAAGCTCCACATCCTTGACAATCAGAGTCATTGCTCCTCCAG                   GATTAGGAACTTTTGCTTTCAATAATCCAACGTAGCAGCCGTGATGTCATTTTTGTAT                   TTCAGGAAGACTGGCAGGAGATTTATGGAAAAGACTATGA                                         ORF Start: ATG at 41   ORF Stop: TAG at 1019                                         SEQ ID NO: 44   326 aa   MW at 36013.5 kD                             NOV18a,   MHAAEIMGPLSAPPCTEHIKWKGLLLTALLLNFWNLPTTAQVMIEAQPPKVSEGKDVL           CG132423-01       Protein Sequence   LLVQIRDLYHYITSYVVDGQIIIYGPAYSGRETVYSNASLLIQNTTREDAGSYTLHII                   KRGDGTRGVTCYFTFTLYLETPKPSISSSNLNPREANETVILTCNPETPDASYLWWMN                   GQSLPMTHRMQLSETNRTLFLFGVTKYTAGPYECEIWNSGSASRSDPVTLNLLHGPDL                   PRIFPSVTSYYSGENLDLSCFADSNPPAQYSWTINGKFQLSGQKLFIPQITPKHNGLY                   ACSARNSATGEESSTSLTIRVIAPPGLGTFAFNNPT                                         SEQ ID NO: 45   990 bp                             NOV18b,     AGA TCTATGCACGCAGCAGAGATCATGGGGCCCCTCTCAGCCCCTCCCTGCACAGAGC           225029377 DNA       Sequence   ACATCAAATGGAAGGGGCTCCTGCTCACAGCATTACTTTTAAACTTCTGGAACTTGCC                   TACCACTGCCCAAGTCATGATTGAAGCCCAGCCACCCAAAGTGTCCGAGGGGAAGCAT                   GTTCTTCTACTTGTCCAAATCAGGGACCTCTACCATTACATTACATCATATGTAGTAG                   ACGGTCAATAAATTATATATGGACCGGCATACAGTGGACGAAGAACAGTATATTCCAA                   TGCATCCCTGCTGATCCAGAATGTCACCCGGCAGGACGCAGGATCCTACACCTTACAC                   ATCATAAGCGAGGTGATGGGACTAGAGGAGTAAACTGGATATTTCACCTTCACCTTAT                   ACCTGGAGACTCCCAAGCCCTCCATCTCCAGCAGCAACTTAAACCCCAGGGAGGCCAT                   GGAGACTGTGATCTTAACCTGTAATCCTGAGACTCCGGACGCAAGCTACCTGTGGTGG                   ATGAATGGTCAGAGCCTCCCTATGACTCATAGGATGCAGCTGTCTGAAACCAACAGGA                   CCCTCTTTCTATTTGGTGTCACAAGTATACTGCGGGACCCTATGAAAAATGTGATATG                   GAACTCAGGCAAGTGCCAGCCGCAGTGACCCAGTCACCCTGATCTCCTCCATGGTCCA                   GACCTCCCCAGAATTTTCCCTTCAGTCACCTCTTACTATTCAGGAGAGkACCTCGACT                   TGTCCTGCTTCGCAGACTCTAAACCCACCAGCACAGTATTCTTGGACATTAAATGAAA                   GTTTCAGCTATCAGGACAAAGCTCTTTATCCCTCAGATTACTCCAAGCATAAAATGGG                   CTCTATGCTTGCTCTGCTCGTAACTCAGCCACTGGCGAGGAAAGCTCCACATCCTTGA                   CAATCGGAGTCATTGCTCCTCCAGGATTAGGAACTTTTGCTTTCAATAATCCAACGCT                   CGAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 46   330 aa   MW at 36399.9 kD                             NOV18b,   RSMHAAEIMGPLSAPPCTEHIKWKGLLLTALLLNFWNLPTTAQVMIEAQPPKVSEGKD           225029377       Protein Sequence   VLLLVQIRDLYHYITSYVVDGQIIIYGPAYSGRETVYSNASLLIQNVTREDAGSYTLH                   IIKRGDGTRGVTGYFTFTLYLETPKPSISSSNLNPREAMETVILTCNPETPDASYLWW                   MNGQSLPMTHRMQLSETNRTLFLFGVTKYTAGPYECEIWNSGSASRSDPVTLNLLHGP                   DLPRIFPSVTSYYSGENLDLSCFADSNPPAQYSWTINGKFQLSGQKLFIPQITPKHNG                   YACSARNSATGEESSTSLTIGVIAPPGLGTFAFNITPTLE                  
 
     [0424] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 18B.  
               TABLE 18B                          Comparison of NOV18a against NOV18b.                                         Identities/           Protein   NOV18a Residues/   Similarities for           Sequence   Match Residues   the Matched Region                       NOV18b   1 . . . 326   317/326 (97%)               3 . . . 328   317/326 (97%)                      
 
     [0425] Further analysis of the NOV18a protein yielded the following properties shown in Table 18C.  
               TABLE 18C                       Protein Sequence Properties NOV18a                                                PSort   0.4500 probability located in cytoplasm;           analysis:   0.2390 probability located in               lysosome (lumen); 0.2113 probability               located in microbody (peroxisome);               0.1000 probability located in               mitochondrial matrix space           SignalP   Cleavage site between residues 41 and 42           analysis:                      
 
     [0426] A search of the NOV18a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 18D.  
               TABLE 18D                          Geneseq Results for NOV18a                                         NOV18a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABG18511   Novel human diagnostic protein   1 . . . 322   321/337 (95%)   0.0           #18502 -  Homo sapiens , 355 aa.   18 . . . 354    321/337 (95%)           [WO200175067-A2, 11 OCT.           2001]       ABG18511   Novel human diagnostic protein   1 . . . 322   321/337 (95%)   0.0           #18502 -  Homo sapiens , 355 aa.   18 . . . 354    321/337 (95%)           [WO200175067-A2, 11 OCT.           2001]       AAY57912   Human transmembrane protein   7 . . . 325   260/334 (77%)   e−147           HTMPN-36 -  Homo sapiens , 335   1 . . . 334   278/334 (82%)           aa. [WO9961471-A2, 02 DEC.           1999]       AAM93561   Human polypeptide, SEQ ID NO:   7 . . . 311   223/320 (69%)   e−125           3333 -  Homo sapiens , 324 aa.   1 . . . 320   252/320 (78%)           [EP1130094-A2, 05 SEP. 2001]       AAM93510   Human polypeptide, SEQ ID NO:   7 . . . 311   223/320 (69%)   e−125           3229 -  Homo sapiens , 326 aa.   1 . . . 320   252/320 (78%)           [EP1130094-A2, 05 SEP. 2001]                  
 
     [0427] In a BLAST search of public sequence datbases, the NOV18a protein was found to have homology to the proteins shown in the BLASTP data in Table 18E.  
               TABLE 18E                          Public BLASTP Results for NOV18a                                         NOV18a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q15242   Pregnancy-specific beta-1-   7 . . . 322   315/331 (95%)   0.0           glycoprotein precursor -  Homo     1 . . . 331   315/331 (95%)             sapiens  (Human), 332 aa.       Q8TCD9   Pregnancy specific beta-1-   7 . . . 326   287/335 (85%)   e−165           glycoprotein 2 -  Homo sapiens     1 . . . 335   295/335 (87%)           (Human), 335 aa.       P11465   Pregnancy-specific beta-1-   7 . . . 326   285/335 (85%)   e−164           glycoprotein 2 precursor (PSBG-2)   1 . . . 335   295/335 (87%)           (Pregnancy-specific beta-1           glycoprotein E) (PS-beta-E) -  Homo               sapiens  (Human), 335 aa.       C27658   pregnancy-specific beta-1   7 . . . 326   285/336 (84%)   e−163           glycoprotein E precursor - human,   1 . . . 336   295/336 (86%)           336 aa.       O75237   PSGIIA-c -  Homo sapiens  (Human),   7 . . . 313   261/322 (81%)   e−147           335 aa.   1 . . . 322   274/322 (85%)                  
 
     [0428] PFam analysis indicates that the NOV18a protein contains the domains shown in the Table 18F.  
               TABLE 18F                          Domain Analysis of NOV18a                                             Identities/                       Similarities           Pfam   NOV18a Match   for the   Expect           Domain   Region   Matched Region   Value                       ig   245 . . . 294   16/53 (30%)   7.9e−08                   34/53 (64%)                      
 
     Example 19  
     [0429] The NOV19 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 19A.  
               TABLE 19A                       NOV19 Sequence Analysis                                                    SEQ ID NO: 47   7347 bp                             NOV19a,     ATG CAGAAGGAGCTGGGCATTGTGCCTTCCTGCCCTGCCATGAAGAGCCCCAGGCCCC           CG132541-01       DNA Sequence   ACCTCCTGCTACCATTGCTGCTGCTGCTGCTGCTGCTGCTGGGGGCTGGGGTGCCAGG                   TGCCTGGGGTCAGGCTGGGAGCCTGGACTTGCAGATTGATGAGGAGCAGCCAGCGGGT                   ACACTGATTGGCGACATCAGTGCGGCGCTTCCGGCAGGCAcGGCAGCTCCTCTCATGT                   ACTTCATCTCTGCCCAAGAGGGCAGCGGCGTGGGCACAGACCTGGCCATTGACGAACA                   CAGTGGGGTCGTCCGTACAGCCCGTGTCTTGGACCGTGAGCAGCGGGACCGCTACCGC                   TTCACTGCAGTCACTCCTGATGGTGCCACCGTAGAAGTTACAGTGCGAGTCGCTGACA                   TCAACGACCATGCTCCAGCCTTCCCACAGGCTCGGGCTGCCCTGCAGGTACCTGAGCA                   TACAGCTTTTGGCACCCGCTACCCACTGGAGCCTGCTCGTGATGCAGATGCTGGGCGT                   CTGGGAACCCAGGGCTATGCGCTATCTGGTGATGGGGCTGGAGAGACCTTCCGGCTGG                   AGACACGCCCCGGTCCAGATGGGACTCCAGTACCTGAGCTGGTAGTTACTGGGAAACT                   GGACCGAGAGAACCGCTCACACTATATGCTACAGCTGGAGGCCTATGATGGTGGTTCA                   CCCCCCCGGAGGGCCCAGGCCCTGCTGGACGTGACACTGCTGGACATCAATGACCATG                   CCCCGGCTTTCAATCAGAGCCGCTACCATGCTGTGGTGTCTGAGAGCCTGGCCCCTGG                   CAGTCCTGTCTTGCAGGTGTTCGCATCTGATGCCGATGCTGGTGTCAATGGGGCTGTG                   ACTTACGAGATCAACCGGAGGCAGAGCGAGGGTGATGGACCCTTCTCCATCGACGCAC                   ACACGGGGCTGCTGCAGTTAGAGCGGCCACTGGACTTTGAGCAGCGGCGGGTCCATGA                   ACTGGTGGTGCAAGCACGAGATGGTGGGGCTCACCCTGAGCTGGGCTCGGCCTTTGTG                   ACTGTGCATGTGCGAGATGCCAATGACAATCAGCCCTCCATGACTGTCATCTTTCTCA                   GTGCAGATGGCTCCCCCCAAGTGTCTGAGGCCGCCCCACCTGGACAGCTCGTTGCTCG                   CATCTCTGTGTCAGACCCAGATGATGGTGACTTTGCCCATGTCAATGTGTCCCTGGAA                   GGTGGAGAGGGCCACTTTGCCCTAAGCACCCAAGACAGCGTCATCTATCTGGTGTGTG                   GCTCGGCGGCTGGATCGAGAGGAGAGGGATGCCTATAACTTGAGGGTTACAGCCAC                   AGACTCAGGCTCACCTCCACTGCGGGCTGAGGCTGCCTTTGTGCTGCACGTCACTGAT                   GTCAACGACAATGCACCTGCCTTTGACCGCCAGCTCTACCGACCTGAGCCCCTGCCTG                   AGGTTGCGCTGCCTGGCAGCTTTGTAGTGCGGGTGACTGCTCGGGATCCTGACCAAGG                   CACCAATGGTCAGGTCACTTATAGCCTAGCCCCTGGCGCCCACACCCACTCGTTCTCC                   ATTGACCCCACCTCAGGCATTATCACTACGGCTGCCTCACTGGACTATGAGTTGGAAC                   CTCAGCCACAGCTGATTGTGGTGGCCACAGATGGTCGCCTGCCCCCTCTAGCCTCCTC                   TGCCACAGTTAGCGTGGCCCTGCAAGATGTGAATGATAATGAGCCCCAATTCCAGAGG                   ACTTTCTACAATGCCTCACTGCCTGAGGGCACCCAGCCTGGAACTTGCTTCCTGCAGG                   TGACAGCCACAGACGCGGATAGTGGCCCATTTGGCCTCCTCTCCTATTCCTTGGGTGC                   TGGACTTGGGTCCTCCGGATCTCCCCCATTCCGCATTGATGCCCACAGCGGTGATGTG                   TGCACAACCCGGACCCTGGACCGTGACCAGGGGCCCTCAAGCTTTGACTTCACAGTGA                   CAGCTGTGGATGGGGGAGGCCTCAAGTCCATCGTATATGTGAAGGTGTTTCTGTCAGA                   CGAGAATGACAACCCTCCTCAGTTTTATCCACGGGAGTATGCTGCCAGTATPAGTGCC                   CAGAGTCCACCAGGCACAGCTGTGCTGAGGTTGCGTGCCCATGACCCTGACCAGGGAT                   CCCATGGGCGACTCTCCTACCATATCCTGGCTGGCAACAGCCCCCCACTTTTTACCTT                   GGATGAGCAATCAGGTCTGTTGACAGTAGCCTGGCCCTTGGCCAGACGGGCCAATTCT                   GTGGTGCAGCTGGAGATCGGGGCTGAGGACGGAGGTGGCCTACAGGCAGAACCCAGTG                   CCCGAGTGGACATCAGCATTGTGCCTGGAACCCCCACACCACCCATATTTGAGCAACT                   ACAGTATGTTTTTTCTGTGCCAGAGGATGTGGCACCAGGCACCAGTGTGGGCATAGTC                   CAGGCACACAACCCACCAGGTCGCTTGGCACCTGTGACCCTTTCCCTATCAGGTCGGG                   AAATCCCCGAGGACTCTTCTCCCTAGATGCGGTATCAGGACTGTTGCAACACTTCCCC                   TCTGGACCGGGAGCTACTGGGACCAGTGTTGGAGCTGGAGGTGCGAGCAGGCAGTGGA                   GTGCCCCCAGCTTTCGCTGTAGCTCGCGTGCGTGTGCTGCTGGATGATGTGAATGACA                   ACTCCCCTGCCTTTCCTGCACCTGAAGACACGGTATTGCTACCACCAAACACTGCCCC                   AGGGACTCCCATCTATACACTGCGGGCTCTTGACCCCGACTCAGGTGTTAACAGTCGA                   GTCACCTTTACCCTGCTTGCTGGGGGTGGTGGAGCCTTCACCGTGGACCCCACCACAG                   GCCATGTACGGCTTATGAGGCCTCTGGGGCCCTCAGGAGGGCCAGCCCATGAGCTGGA                   GCTGGAGGCCCGGGATGGGGGCTCCCCACCACGCACCAGCCACTTTCGACTACGGGTG                   GTGGTACAGGATGTGGGAACCCGTCGGCTGGCTCCCCGATTCAACAGCCCTACCTACC                   GTGTGGACCTGCCCTCAGGCACCACTGCTGGAACTCAGGTCCTGCAAGTGCAGGCCCA                   AGCACCAGATGGGGGCCCTATCACCTATCACCTTGCAGCAGAGGGAGCAAGTAGCCCC                   TTTGGCCTGGAGCCACAGAGTGGGTGGCTATGGGTGCGGGCAGCACTACACCGTGAGG                   CCCAGGAATTGTACATACTGAAGGTAATGGCAGTGTCTGGGTCCAAAGCTGAGTTGGG                   GCAGCAGACAGGCACAGCCACCGTGAGGGTCAGCATCCTCAACCAGAATGAACACAGT                   CCCCGCTTGTCTGAGGATCCCACCTTCCTGGCTGTGGCTGAGAACCAGCCCCCAGGGA                   CCAGCGTGGGCCGAGTCTTTGCCACTGACCGAGACTCAGGACCCAATGGACGTCTGAC                   CTACAGCCTGCAACAGCTGTCTGAAGACAGCAAGGCCTTCCGCATCCACCCCCAGACT                   GGTGAGGTGACCACACTCCAAACCCTGGACCGTGAGCAGCAGAGCAGCTATCAGCTCC                   TGGTGCAGGTGCAGGATGGAGGGAGCCCACCCCGCAGCACCACAGGCACTGTCCATGT                   TGCAGTGCTTGACCTCAACGACAACAGCCCCACGTTCCTGCAGGCTTCAGGAGCTGCT                   GGTGGGGGCCTCCCTATACAGGTACCAGACCGCGTGCCTCCAGGAACACTGGTGACGA                   CTCTGCAGGCGAAGGATCCAGATGAGGGGGAGAATGGGACCATCTTCTACACGCTAAC                   TGGTCCTGGCTCAGAGCTTTTCTCTCTGCACCCTCACTCAGGGGAGCTGCTCACTGCA                   GCTCCCCTGATCCGAGCAGAGCGGCCCCACTATGTGCTGACACTGAGTGCTCATGACC                   AAGGCAGCCCTCCTCGAAGTCCCAGCCTCCAGCTGCTGGTGCAGGTACTTCCCTCAGC                   TCGCTTGGCCGAGCCGCCCCCAGATCTCGCAGAGCGGGACCCAGCGGCACCAGTGCCT                   GTCGTGCTGACGGTGACAGCAGCTGAGGGACTGCGGCCCGGCTCTCTGTTGGGCTCGG                   TGGCAGCGCCAGAGCCCGCGGGTCTGCGTGCACTCACCTACACACTGGTGGGCGGTGC                   CGATCCCGAGGGCACCTTCGCGCTGGATGCGGCCTCAGGGCGCTTGTACCTGGCGCCG                   CCCCTGGACTTCGAAGCTGGCCCGCCGTGGCGCGCGCTCACGGTACGCGCTGAGGGGC                   CGGGAGGCGCGGGCGCGCGGCTGCTGCGAGTGCAGGTGCAAGTGCAGCACGACAATGA                   GCATGCGCCCGCCTTTGCGCGCGACCCGCTGGCGCTGGCGCTGCCAGAGAACCCGGAG                   CCCGGCGCAGCGCTGTACACTTTCCGCGCGTCGGACGCCGACGGCCCCGGCCCCAATA                   GCGACGTGCGCTACCGCCTGCTGCGCCAGGAGCCGCCCGTGCCGGCGCTTCGCCTGGA                   CGCGCGCACCGGGGCGCTCAGCGCTCCGCGCGGCCTGGACCGAGAGACCACTCCCGCG                   CTGCTGCTGCTGGTGGAAGCCACCGACCGGCCCGCCAACGCCAGCCGCCGTCGTGCAG                   CGCGCGTTTCAGCGCGCCTCTTCGTCACGGATGAGAATGACAACGCGCCTGTCTTCGC                   CTCGCCGTCACGCGTGCGCCTCCCAGAGGACCAGCCGCCTGGGCCCGCGGCCCTGCAC                   GTGGTAGCCCGGGACCCGGATCTGGGCGAGGCTGCACGCGTGTCCTATCGGCTGGCAT                   CTGGCGGGGACGGCCACTTCCCGCTGCACTCAAGCACTCGTGCGCTGTCCGTGGTGCG                   GCCGTTCGACCGCGAACAACGAGCTGAGCACGTACTGACAGTGGTGGCCTCAGACCAC                   GGCTCCCCGCCGCGCTCGACCACGCAGGTCCTGACCGTCAGTGTCGCTGACGTCAACG                   ACGAGGCGCCTACTTTCCAGCAGCAGGAGTACAGCGTCCTCTTGCGTGAGAACAACCC                   TCCTGCCACATCTCTGCTCACCCTGCGAGCAACCGACCCCCACGTGGGTGCCAACGGG                   CAAGTGACTTATGGAGGCGTCTCTAGCGAAAGCTTTTCTCTGGATCCTGACACTCGTG                   TTCTCACGACTCTTCGGGCCCTGGATCGAGAGGAACAGGAGGAGATCAACCTGACAGT                   GTATGCCCAGGACAGGGGCTCACCTCCTCAGTTAACGCATGTCACTGTTCGAGTGGCT                   GTGGAGGATGAGAATGACCATGCACCAACCTTTGGGAGTGCCCATCTCTCTCTGGAGG                   TGCCTGAGGGCCAGGACCCCCAGACCCTTACCATGCTTCGGQCCTCTGATCCAGATGT                   GGGAGCCAATGGGCAGTTGCAGTACCGCATCCTAGATGGGGACCCATCAGGAGCCTTT                   GTCCTAGACCTTGCTTCTGGAGAGTTTGGCACCATGCGGCCACTAGACAGAGAACTGG                   AGCCAGCTTTCCAGCTGAGGATAGAGGCCCGGGATGGAGGCCAGCCAGCTCTCAGTGC                   AACACGCTGCTTTTGACAGTGACAGTGCTGGATGCCAATGACCATGCTCCAGCCTCCT                   GTGCCTGCCTACTCGTGGAGGTGCCGGAGGATGTGCCTGCAGGGACCCTGCTGCTCAC                   AGCTACAGGCTCATGACCCTGATGCTGGAGCTAATGGCCATGTGACCTACTACCTGGC                   CGCCGGTACAGCAGGAGCCTTCCTGCTGGAGCCCAGCTCTGGAGAACTGCGCACAGCT                   CCAGCCTTGGACAGAGAACAGTGTCCCAGCTACACCTTTTCTGTGAGTGCAGTGGATG                   GTGCAGCTGCTGGGCCCCTAAGCACCACAGTGTCTGTCACCATCACGGTGCGCGATGT                   CAATGACCATGCACCCACCTTCCCCACCAGTCCTCTGCGCCTACGTCTGCCCCGCCCA                   GGCCCCAGCTTCAGTACCCCAACCCTGGCTCTGGCCACACTGAGAGCTGAAGATCGTC                   ATGCTGGTGCCAATGCTTCCATTCTGTACCGGCTGGCAGGCACACCACCTCCTGGCAC                   TACTGTGGACTCTTACACTGGTGAAATCCGCGTGGCCCGCTCTCCTGTAGCTCTAGGC                   CCCCGAGATCGTGTCCTCTTCATTGTGGCCACTGATCTTGGCCGTCCAGCTCGCTCTG                   CCACTGGTGTCATCATTGTTGGACTGCAGGGGGAAGCTGAGCGTGGACCCCGCTTTCC                   CCGGGCTAGCAGTGAGGCTACGATTCGTGAGAATGCGCCCCCAGGTACTCCTATTGTC                   TCCCCCAGGGCCGTCCATGCAGGAGGCACAAATGGACCCATCACCTACAGCATTCTCA                   GTGGGAATGAGAAAGGGACATTCTCCATCCAGCCTAGTACAGGTGCCATCACAGTTCG                   CTCAGCAGAGGGGCTAGACTTCGAGGTGAGTCCACGGCTGCGACTGGTGCTGCAGGCA                   CTTGGAGGGGCCCCTGCTGCAGGTGGAGGCGGATGACCTGGATCAAGGCTCTGGAGGA                   ACAATGCTCCCCGTTTCCTGCGGCCCCATTATGTGGCCTTCCTTCCTGAGTCCCGGCC                   CTTGGAGGGGCCCCTGCTGCAGGTGGAGGCGGATGACCTGGATCAAGGCTCTGGAGGA                   CAGATTTCCTACAGTCTGGCTGCATCCCAGCCGGCACGTGGATTGTTCCACGTAGACC                   CACCACAGGCACTATCACTACCACAGCCATCCTGGACCGTGAGATCTGGGCTGAAAAC                   ACGGTTGGTGCTGATGGCCACAGACAGAGGGAGCCCAGCCCTGGTGGGCTCAGCTACC                   TTGACGGTGATGGTCATCGACACCAATGACAATCGCCCCACCATCCCCCAACCCTGGG                   AGCTCCGAGTGTCAGAAGATGGCAIGCCATGTGTGGCAGGTGCGCTGACAGCCATTGT                   GGCCGGCGAGCAGGAGCTCCGTGGCAGCTATAACTGGGACTACCTGCTGAGCTGGTGC                   CATCAGCACCAACCACTGGCCAGTGTCTTCACAGAGATCGCTCGGCTCAAGGATGAAG                   CTCGGCCATGTCCCCCAGCTCCCCGTATCGACCCACCACCCCTCATCACTGCCGTGGC                   CCACCCAGGAGCCAAGTCTGTGCCCCCCAAGCCAGCAAACACAGCTGCAGCCCGGGCC                   ATCTTCCCACCAGCTTCTCACCGCTCCCCCATCAGCCGTGAAGGCTCCCTGTCCTCAG                   CTGCCATGTCCCCCAGCTTCTCACCCTCTCTGTCTCCTCTGGCTGCTCGCTCACCCGT                   TGTCTCACCAATTGGGGTGGCCCAGGGTCCCTCAGCCTCAGCACTCAGCGCAGAGTCT                   GGCCTGGAGCCACCTGATGACACGGAGCTGCACATCTAG                                         ORF Start: ATG at 1   ORF Stop: TAG at 7345                                         SEQ ID NO: 48   2448 aa   MW at 258115.8 kD                             NOV19a,   MQKELGIVPSCPGMKSPRPHLLLPLLLLLLLLLGAGVPGAWGQAGSLDLQIDEEQPAG           CG132541-01       Protein Sequence   TLIGDISAGLPAGTAAPLMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDREQRDRYR                   PTAVTPDGATVEVTVRVADINDHAPAFPQARAALQVPEHTAFGTRYPLEPARDADAGR                   LGTQGYALSGDGAGETFRLETRPGPDGTPVPELVVTGELDRENRSHYMLQLEAYDGGS                   PPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLAPGSPVLQVFASDADAGVNGAV                   TYEINRRQSEGDGPFSIDAHTCLLQLERPLDFEQRRVHELVVQARDGGAHPELGSAFV                   TVHVRDANDNQPSMTVIFLSADGSPQVSEAAPPGQLVARISVSDPDDGDFAHVNVSLE                   GGEGHFALSTQDSVIYLVCVARRLDREERDAYNLRVTATDSGSPPLRAEAAFVLHVTD                   VNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQVTYSLAPGAHTHWFS                   IDPTSGIITTAASLDYELEPQPQLIVVATDGGLPPLASSATVSVALQDVNDNEPQFQR                   TFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGSSGSPPFRIDAHSGDV                   CTTRTLDRDQGPSSFDFTVTAVDGGGLKSMVYVKVFLSDENDNPPQFYPREYAASISA                   QSPRGTAVLRLRAHDPDQGSHGRLSYHILAGNSPPLFTLDEQSCLLTVAWPLARRANS                   VVQLEIGAEDGGGLQAEPSARVDISIVRGTPTPPIFEQLQYVFSVPEDVAPGTSVGIV                   QAHNPPGRLAPVTLSLSGGDPRGLFSLDAVSGLLQTLRPLDRELLGPVLELEVRAGSG                   VPPAFAVARVRVLLDDVNDNSPAFPAPEDTVLLPPNTAPGTPIYTLRALDPDSGVNSR                   VTETLLAGGGGAFTVDPTTGHVRLMRPLGPSGGRAHELELEARDGGSPPRTSHFRLRV                   VVQDVGTRGLAPRFNSPTYRVDLPSGTTAGTQVLQVQAQAPDGGPITYHLAAEGASSP                   FGLEPQSGWLNTRAALDREAQELYILKVMAVSGSKAELGQQTGTATVRVSILNQNEHS                   PRLSEDPTFLAVAENQPPGTSVGRVFATDRDSGPNGRLTYSLQQLSEDSKAFRIHPQT                   GEVTTLQTLDREQQSSYQLLVQVQDGGSPPRSTTGTVHVAVLDLNDNSPTFLQASGAA                   GGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGPGSELFSLHPHSGELLTA                   APLIRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSARLAEPPPDLAERDPAAPVP                   VVLTVTAAEGLRPGSLLGSVAAPEPAGVGALTYTLVGGADPEGTFALDAASCRLYLAR                   PLDFEAGPPWRALTVRAEGPGGAGARLLRVQVQVQDENEHAPAFARDPLALALPENPE                   PGAALYTFRASDADGPGPNSDVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPA                   LLLLVEATDRPANASRRRAARVSARVFVTDENDNAPVFASPSRVRLPEDQPPGPAALH                   VVARDPDLGEAARVSYRLASGGDGHFRLHSSTGALSVVRPLDREQRAEHVLTVVASDH                   GSPPRSATQVLTVSVADVNDEApTFQQQEYSVLLRENNPPGTSLLTLRATDPDVGAGI                   AQVTYGGVSSESFSLDPDTGVLTTLRALDREEQEEINLTVYAQDRGSPPQLTHVTVRV                   VEDENDHAPTFGSAHLSLEVPEGQDPQTLTMLRASDPDVGANGQLQYRILDGDPSCAF                   VLDLASGEFGTMRPLDREVEPAFQLRIERDGGQPALSATLLLTVTVLDANDHIAPAFP                   VPAYSVEVPEDVPAGTLLLQLQAHDPDAGANGIVTYYLGAGTAGAFLLEPSSGELRTA                   AALDREQCPSYTPSVSAVDGAAAGPLSTTVSVTITVRDVNDHAPTFPTSPLRLRLPRP                   GPSFSTPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPVALG                   PRDRVLFIVATDLGRPARSATGVIIVGLQGEAERGPRFPPASSEATIRENAPPGTPIV                   SPPAVHAGGTNGPITYSILSGNEKGTFSIQPSTGAITVRSAEGLDFEVSPRLRLVLQA                   ESGGAFAFTVLTLTLQDANDNAPRFLRPHYVAFLPESRPLEGPLLQVEAADLDQGSGG                   QISYSLAASQPARGLFHVDPTTGTITTTAILDREIWAETRLVLAATDRGSPALVGSAT                   LTVMVIDTNDNRPTIPQPWELRVSEDGKPCVAGALTAIVAGEEELRGSYNWDYLLSW                   HQHQPLASVFTEIARLKDEARPCPPAPRIDPPPLITAVAPGAKSVPPKPANTAAARA                   IFPPASHRSPISREGSLSSVASPSFSPSLSPLAARSPVVSPIGVAQGPSASALSAES                   GLEPPDDTELHI                                         SEQ ID NO: 49   10759 bp                             NOV19b,   GCGGGGGGAGGGGAGGGGAGGGGAGGGGGCGCGGGGCCGCGGCAGCGGACCTCGCATC           CG132541-02       DNA Sequence   CTCGGCGGGGCGGCTGTGCAGGAGGCGGCGCCCGGGCGTCAGCGGACGGACCGATCGA                   CGGCCAAGGGCGCGCGGACCGACGGCGGCTGCCCGGAGGGGATCGCGGGCCTCCGAGA                   CAGCCACTGCGGACGATGCGCGGCCCCAGGCCCCGCGCGAGCGGGCGCTGCCCGGGGG                   GCTGACCGCGGCCCGACGGCGCCCCAGCACCGGGCGAGGGAGCCCGCGTCGCGCGGAG                   GTCAGGGAGCCTGAGCTGGAGCCAGGGCCCCAGTGGGACCTGACCCAAAGTCTGAGGT                   CAAGCTCGGCCCAGAGCCTGGCCTGGAGCTGGAGCCCACAGCACAGCTGGACTACCCT                   TGTCATGCAGAAGGAGCTGGGCATTGTGCCTTCCTGCCCTGGCATGAAGAGCCCCAGG                   CCCCACCTCCTGCTACCATTGCTGCTGCTGCTGCTGCTGCTGCTGGGGGCTGGGGTGC                   CAGGTGCCTGGGGTCAGGCTGGGAGCCTGCACTTGCACATTGATGAGGAGCAGCCAGC                   GGGTACACTGATTGGCGACATCAGTGCGGGGCTTCCGGCAGGCACCGCAGCTCCTCTC                   ATGTACTTCATCTCTGCCCAAGAGCGCAGCGGCGTGGGCACAGACCTGGCCATTGACG                   AACACAGTGGGGTCGTCCGTACAGCCCGTGTCTTGGACCGTGAGCAGCGGGACCGCTA                   CCGCTTCACTCCAGTCACTCCTGATGGTGCCACCGTAGAAGTTACAGTGCGAGTGGCT                   GACATCAACGACCATGCTCCAGCCTTCCCACAGOCTCGGGCTGCCCTGCAGGTACCTG                   AGCATACAGCTTTTGGCACCCGCTACCCACTGGAGCCTGCTCGTGATGCAGATGCTCG                   GCGTCTGGGAACCCAGGGCTATGCGCTATCTGGTGATGGGGCTGGAGAGACCTTCCGG                   CTGGAGACACGCCCCGGTCCAGATGGGACTCCAGTACCTGAGCTGGTAGTTACTGGGG                   AACTGGACCGAGAGAACCGCTCACACTATATGCTACAGCTGGAGGCCTATGATGGTGG                   TTCACCCCCCCGCACGGCCCAGGCCCTGCTGGACGTGACACTGCTGGACATCAATGAC                   CATGCCCCGGCTTTCAATCAGAGCCGCTACCATGCTGTGGTGTCTGAGAGCCTGGCCC                   CTGGCAGTCCTGTCTTGCAGGTGTTCGCATCTGATGCCGATGCTGGTGTCAATGGGGC                   TGTGACTTACGAGATCAACCGCAAGGCAGAGCGAGGGTGATGGACCCTTCTCCATCGAC                   GCACACACGGCGCTGCTGCAGTTAGAGCGGCCACTGGACTTTGAGCAGCGGCGGGTCC                   ATGAACTGGTGGTGCAAGCACGAGATGGTGGGGCTCACCCTGAGCTGGGCTCGGCCTT                   TGTGACTGTGCATGTGCGAGATGCCAATGACAATCAGCCCTCCATGACTGTCATCTTT                   CTCAGTGCAGATGGCTCCCCCCAAGTGTCTGAGGCCGCCCCACCTGGACAGCTCGTTG                   CTCGCATCTCTGTGTCAGACCCAGATGATGGTGACTTTGCCCATGTCAATGTGTCCCT                   GGAAGGTGGAGAGGGCCACTTTGCCCTAAGCACCCAAGACAGCGTCATCTATCTGGTG                   TGTGTGGCTCGGCGGCTGGATCGAGAGGAGAGGGATGCCTATAACTTGAGGCTTACAG                   CCACAGACTCAGGCTCACCTCCACTGCGGGCTGAGGCTGCCTTTGTGCTGCACGTCAC                   TGATGTCAACGACAATGCACCTGCCTTTGACCGCCAGCTCTACCGACCTGAGCCCCTG                   CCTGAGGTTGCGCTGCCTGGCAGCTTTGTAGTGCGGGTGACTGCTCGGGATCCTGACC                   AAGGCACCAATGGTCAGGTCACTTATAGCCTAGCCCCTGGCGCCCACACCCACTGGTT                   CTCCATTGACCCCACCTCAGGCATTATCACTACGGCTGCCTCACTGGACTATGAGTTG                   GAACCTCAGCCACAGCTGATTGTGGTGGCCACAGATGGTGGCCTGCCCCCTCTAGCCT                   CCTCTGCCACAGTTAGCGTGGCCCTGCAAGATGTGATGAATAATGAGCCCCAATTCCA                   GAGGACTTTCTACAATGCCTCACTGCCTGAGGGCACCCAGCCTGGIACTTGCTTCCTG                   CAGGTGACAGCCACAGACGCGGATAGTGCCCCATTTGGCCTCCTCTCCTATTCCTTGG                   GTGCTGGACTTGGGTCCTCCGGATCTCCCCCATTCCGCATTGATGCCCATAGCGCTGA                   TGTGTGCACAACCCGGACCCTGGACCCTGACCAGGGGCCCTCAAGCTTTGACTTCACA                   GTGACAGCTGTGGATGGGGGAGGCCTCAAGTCCATGGTATATGTGAAGGTGTTTCTGT                   CAGACGAGAATGACAACCCTCCTCAGTTTTATCCACGGGAGTATGCTGCCAGTATAAG                   TGCCCAGAGTCCACCAGGCACAGCTGTGCTGAGGTTGCGTGCCCATGACCCTCACCAG                   GGATCCCATGGGCGACTCTCCTACCATATCCTGGCTGGCAACAGCCCCCCACTTTTTA                   CCTTGGATGAGCAATCAGGGCTGTTGACAGTAGCCTGGCCCTTGGCCAGACGGGCAAA                   TTCTGTGGTGCAGCTGGAGATCGGGGCTGAGGACGGAGGTGGCCTACAGGCAGAACCC                   AGTGCCCGAGTGGACATCAGCATTGTGCCTGGAACCCCCACACCACCCATATTTGAGC                   ACTACAGTATGTTTTTTCTGTGCCAGAGGATGTGGCACCAGGCACCAGTGTGGCACAT                   AGTCCAGGCACACAACCCACCAGGTCGCTTGGCACCTGTGACCCTTTCCCTATCAGGT                   GGGGATCCCCGAGGACTCTTCTCCCTAGATGCGGTATCAGGACTGTTGCAAACACTTC                   GCCCTCTGGACCCGGAGCTACTGGGACCAGTGTTGGAGCTGGAGGTGCGAGCAGGCAG                   TGGAGTGCCCCCAGCTTTCGCTGTAGCTCGGGTGCGTGTGCTGCTGGATGATGTGAAT                   GACAACTCCCCTGCCTTTCCTGCACCTGAAGACACGGTATTGCTACCACCAAACACTG                   CCCCAGGGACTCCCATCTATACACTGCGGGCTCTTGACCCCGACTCAGGTGTTAACAG                   TCGAGTCACCTTTACCCTGCTTGCTGGGGGTGGTGGAGCCTTCACCGTGGACCCCACC                   ACAGGCCATGTACGGCTTATGAGGCCTCTGGGGCCTCAGGACAGGCCAGCCCATGAGC                   TGGAGCTGGAGGCCCGGGATGGGGGCTCCCCACCACGCACCAGCCACTTTCGACTACG                   GGTGGTGGTACAGGATGTGGGAACCCGTGGGCTGGCTCCCCGATTCAACAGCCCTACC                   TACCGTCTGGACCTGCCCTCAGGCACCACTGCTGGAACTCAGGTCCTGCAAGTGCAGG                   CCCAAGCACCAGATGGGGGCCCTATCACCTATCACCTTGCACCAGAGGGAGCAAGTAG                   CCCCTTTGGCCTGGAGCCACAGAGTGGGTGGCTATGGGTGCGGGCAGCACTAGACCGT                   GAGGCCCAGGAATTGTACATACTGAAGGTAZTGGCAGTGTCTGGGTCCAAAGCTGAGT                   TGGGGCAGCAGACAGGCACAGCCACCGTGAGGGTCAGCATCCTCAACCAGAATGAACA                   CAGTCCCCGCTTGTCTGAGGATCCCACCTTCCTGGCTGTGGCTGAGAACCAGCCCCCA                   GGGACCAGCGTGGGCCGAGTCTTTGCCACTGACCGAGACTCAGGACCCAATGGACGTC                   TGACCTACAGCCTGCAACAGCTGTCTGAA\GACAGCAAGGCCTTCCGCATCCACCCCCA                   GACTGGAGAAGTGACCACACTCCAAACCCTGGACCGTGAGCAGCAGAGCAGCTATCAG                   CTCCTGGTGCAGGTGCAGGATGGAGGGAGCCCACCCCGCAGCACCACAGGCACTGTGC                   ATGTTGCAGTGCTTGACCTCAACGACAACAGCCCCACGTTCCTGCAGGCTTCAGGAGC                   TGCTGGTGGGGGCCTCCCTATACAGGTACCAGACCGCGTGCCTCCAGGAACACTGGTG                   ACGACTCTGCAGGCGAAGGATCCAGATGAGGGGCAGAATGGGACCATCTTGTACACGC                   TAACTGGTCCTGGCTCAGAGCTTTTCTCTCTGCACCCTCACTCAGGGGAGCTGCTCAC                   TGCAGCTCCCCTGATCCGAGCACAGCGGCCCCACTATGTGCTGACACTGAGTGCTCAT                   GACCAAGGCAGCCCTCCTCGAAGTGCCAGCCTCCAGCTGCTGGTGCAGGTGCTTCCCT                   CAGCTCGCTTGGCCGAGCCGCCCCCAGATCTCGCAGAGCGGGACCCAGCGGCACCAGT                   GCCTGTCGTGCTGACGGTGACAGCAGCTGAGGGACTGCGGCCCGGCTCTCTGTTGGGC                   TCGGTGGCAGCGCCAGAGCCCGCGCGTGTGGGTGCACTCACCTACACACTGGTGGGCG                   GTGCCGATCCCGAGGGCACCTTCGCGCTGGATGCGGCCTCAGGGCGCTTGTACCTGGC                   GCGGCCCCTGGACTTCGAAGCTGGCCCGCCGTGGCGCGCGCTCACGGTACGCGCTGAG                   GGGCCGGGAGGCGCCGGCGCGCGGCTGCTGCGAGTGCAGGTGCAAGTGCAGGACGAGA                   ATGAGCATGCGCCCGCCTTTGCGCGCGACCCGCTGGCGCTGGCGCTGCCAGAGAACCC                   GGAGCCCGGCGCAGCGCTGTACACTTTCCGCGCGTCGGACGCCGACGGCCCCGGCCCC                   AATAGCGACGTGCGCTACCGCCTGCTGCGCCACGAGCCGCCCGTGCCGGCGCTTCGCC                   TGGACGCGCGCACCGGGGCGCTCAGCGCTCCGCGCGGCCTGGACCGAGAGACCACTCC                   CGCGCTGCTGCTGCTGGTGGAAGCCACCGACCGGCCCGCCAACGCCAGCCQCCGTCGT                   GCAGCGCGCGTTTCAGCGCGCGTCTTCGTCACGGATGAGAATGACAACGCGCCTGTCT                   TCGCCTCGCCGTCACGCGTGCGCCTCCCAGAGGACCAGCCGCCTGGGCCCGCGGCCCT                   GCACGTGGTAGCCCGGGACCCGGATCTGGGCGAGGCTGCACGCGTGTCCTATCCGCTG                   GCATCTGGCGGGGACGGCCACTTCCGGCTGCACTCAAGCACTGGAGCGCTGTCCGTGG                   TGCGGCCGTTGGACCGCGAACAACGAGCTGAGCACGTACTGACAGTGGTGGCCTCAGA                   CCACGGCTCCCCGCCGCGCTCGGCCACGCAGGTCCTGACCGTCAGTGTCGCTGACGTC                   AACGACGAGGCGCCTACTTTCCAGCAGCAGGAGTACAGCGTCCTCTTGCGTGAGAACA                   ACCCTCCTGGCACATCTCTGCTCACCCTGCGAGCAACCGACCCCGACGTGGGGGCCAA                   CGGGCAAGTGACTTATGGAGGCGTCTCTAGCGAAAGCTTTTCTCTGGATCCTGACACT                   GGTGTTCTCACGACTCTTCGGGCCCTGGATCGAGAGGAACAGGAGGAGATCAACCTGA                   CAGTGTATGCCCAGGACAGGGGCTCACCTCCTCAGTTAACGCATGTCACTGTTCGAGT                   GGCTGTGGAGGATGAGAATGACCATGCACCAACCTTTGGGAGTGCCCATCTCTCTCTG                   GAGGTGCCTGAGGGCCAGGACCCCCAGACCCTTACCATGCTTCGGGCCTCTGATCCAG                   ATGTGGGAGCCAATGGGCAGTTGCAGTACCGCATCCTAGATGGGGACCCATCAGGAGC                   CTTTGTCCTAGACCTTGCTTCTGGAGACTTTGGCACCATGCGGCCACTAGACAGAGAA                   GTGGAGCCAGCTTTCCAGCTGAGGATAGACCCCCGGGATGGAGGCCAGCCAGCTCTCA                   GTGCCACGCTGCTTTTGACAGTGACAGTGCTGGATGCCAATGACCATGCTCCACCCTT                   TCCTGTGCCTGCCTACTCGGTGGAGGTGCCGGAGGATGTGCCTGCAGGGACCCTGCTG                   CTGCAGCTACAGGCTCATGACCCTGATGCTGGAGCTAATGGCCATGTGACCTACTACC                   TGGGCGCCGGTACACCAGGAGCCTTCCTGCTGGAGCCCAGCTCTGGAGAACTGCGCAC                   AGCTGCAGCCTTGGACAGAGAACAGTGTCCCAGCTACACCTTTTCTGTGAGTGCAGTG                   GATGGTGCAGCTGCTGGGCCCCTAAGCACCACAGTGTCTGTCACCATCACGGTGCGCG                   ATGTCAATGACCATGCACCCACCTTCCCACCAGTCCTCTGCGCCTACGTCTGCCCCGA                   CCCAGGCCCCAGCTTCAGTACCCCAACCCTGGCTCTGGCCACACTGAGAGCTGAAGAT                   CGTGATGCTGGTGCCAATGCTTCCATTCTGTACCGGCTGGCAGGCACACCACCTCCTG                   GCACTACTGTGGACTCTTACACTGGTGAAATCCGCGTGGCCCGCTCTCCTGTAGCTCT                   AGGCCCCCGAGATCGTGTCCTCTTCATTGTGGCCACTGATCTTGGCCGTCCAGCTCGC                   TCTGCCACTGGTGTGATCATTGTTGGACTGCAGGGGGAAGCTGAGCGTGGACCCCGCT                   TTCCCCGGCCTAGCAGTGAGOCTACGATTCGTGAGAATGCGCCCCCAGGGACTCCTAT                   TGTCTCCCCCAGGGCCGTCCATGCAGGAGGCACAAATGGACCCATCACCTACAGCATT                   CTCAGTGGGAATGAGAAAGGGACATTCTCCATCCAGCCTAGTACAGGTGCCATCACAG                   TTCGCTCAGCAGAGGGGCTAGACTTCGAGGTGAGTCCACGCCTGCGACTGGTGCTGCA                   GGCAGAGAGTGGAGGAGCCTTTGCCTTCACTGTGCTGACCCTGACCCTGCAAGATGCC                   AACGACAATGCTCCCCGTTTCCTGCGGCCCCATTATGTGGCCTTCCTTCCTGAGTCCC                   GGCCCTTGGAGGGGCCCCTGCTGCAGGTGGAGGCGGATGACCTGGATCAAGGCTCTGG                   AGGACAGATTTCCTACAGTCTGCCTGCATCCCAGCCGGCACGTGGATTGTTCCACGTA                   GACCCAACCACAGGCACTATCACTACCACAGCCATCCTGGACCGTOAGATCTGGGCTG                   AAACACGGTTGGTGCTGATGGCCACAGACAGAGGGAGCCCAGCCCTGGTGGGCTCAGC                   TACCTTGACGGTGATGGTCATCGACACCAATGACAATCGCCCCACCATCCCCCAACCC                   TGGGAGCTCCGAGTGTCAGAAGATGCGTTATTGGGCTCAGAGATTGCACAGGTAACAG                   GGkATGATGTGGACTCAGGACCCGTGCTGTGGTATGTGCTAAGCCCATCTGGGCCCCA                   GGATCCCTTCAGTGTTGGCCGCTATGGAGGCCGTGTCTCCCTCACGGGGCCCCTGGAC                   TTTGAGCAGTGTGACCGCTACCAGCTGCAGCTGCTGGCACATGATGGGCCTCATGAGG                   GCCGTGCCAACCTCACAGTCCTTGTGGAGGATGTCAATCACAATGCACCTGCCTTCTC                   ACAGAGCCTCTACCAGGTAATGCTGCTTGAGCACACACCCCCAGGCAGTGCCATTCTC                   TCCGTCTCTGCCACTGATCGGGACTCAGGTGCCAACGGTCACATTTCCTACCACCTGG                   CTTCCCCTGCCGATGGCTTCAGTGTTGACCCCAACAATGGGACCCTGTTCACAATAGT                   GGGAACAGTGGCCTTGGGCCATGACGGGTCAGGAGCAGTGGATGTGGTGCTGGAAGCA                   CGAGACCACGGGGCTCCAGGCCGGGCAGCACGAGCCACAGTGCACGTGCAGCTGCAGG                   ACCAGAACGACCACGCCCCGAGCTTCACATTGTCACACTACCGTGTGGCTGTGACTGA                   AGACCTGCCCCCTGGCTCCACTCTGCTCACCCTGGAGGCTACAGATGCTGATCGAAGC                   CGCAGCCATGCCGCTGTGGACTACAGCATCATCAGTGGCAACTGGGGCCGAGTCTTCC                   AGCTGGAACCCAGGCTGGCTGAGGCTGGGGAGAGTGCTGGACCAGGCCCCCGGGCACT                   GGGCTGCCTGGTGTTGCTTGAACCTCTAGACTTTGAAAGCCTGACACAGTACAATCTA                   ACAGTGGCTGCAGCTGACCGTGGGCAGCCACCCCAAAGCTCAGTCGTGCCAGTCACTG                   TCACTGTACTAGATGTCAATGACAACCCACCTGTCTTTACCCGAGCATCCTACCGTGT                   GACAGTACCTGAGGACACACCTGTTGGAGCTGAGCTGCTGCATGTAGAGGCCTCTGAC                   GCTGACCCTGGCCCTCATGGCCTCGTGCGTTTCACTGTCAGCTCAGGCGACCCATCAG                   GGCTCTTTGAGCTGGATGAGAGCTCAGGCACCTTGCGACTGGCCCATGCCCTGGACTG                   TGAGACCCAGGCTCGACATCAGCTTGTAGTACAGGCTGCTGACCCTGCTGGTGCACAC                   TTTGCTTTGGCACCAGTGACAATTGAGGTCCAGGATGTGAATGATCATGGCCCAGCCT                   TCCCACTGAACTTACTCAGCACCAGCGTGGCCGAGAATCAGCCTCCAGGCACTCTCGT                   GACCACTCTGCATGCAATCGACGGGGATGCTGGGGCTTTTGGGAGGCTCCGTTACAGC                   CTGTTGGAGGCTGGGCCAGGACCTGAGGGCCGTGAGGCATTTGCACTGAACAGCTCAA                   CAGGGGAGTTGCGTGCGCGAGTGCCCTTTGACTATGAGCACACAGAAAGCTTCCGGCT                   GCTGGTGGGTGCTGCTGATGCTGGGAATCTCTCAGCCTCTGTCACTGTGTCGGTGCTA                   GTGACTGGAGAGGATGAGTATGACCCTGTATTTCTGGCACCAGCTTTCCACTTCCAAG                   TGCCCGAAGGTGCCCGGCGTGGCCACAGCTTGGGTCACGTCCAGGCCACAGATGAGGA                   TGGGGGTGCCGATGGCCTGGTTCTGTATTCCCTTGCCACCTCTTCCCCCTATTTTGGT                   ATTAACCAGACTACAGGAGCCCTGTACCTGCGGGTGGACAGTCGGGCACCAGGCAGCG                   GAACAGCCACCTCTGGGGGTGGGGGCCGGACCCGGCGGGAAGCACCACGGGAGCTGAG                   GCTGGAGGTGATAGCACCGGGCCCTCTGCCTGGTTCCCGGAGTGCCACAGTGCCTGTG                   ACCGTGGATATCACCCACACCGCACTGGGCCTGGCACCTGACCTCAACCTGCTATTAG                   TAGGGGCCGTGGCAGCCTCCTTGGGAGTTGTGGTGGTGCTTGCACTGGCACCCCTGGT                   CCTAGGACTTGTTCGCGCCCGTAGCCGCAAGGCTGAGGCAGCCCCTGGCCCAATGTCA                   CAGGCAGCACCCCTAGCCAGTGACTCACTGCAGkAZCTGGGCCGGGAGCCACCTAGTC                   CACCACCCTCTGAGCACCTCTATCACCAGACTCTTCCCAGCTATGGTGGGCCAGGAGC                   TGGAGGACCCTACCCCCCTGGTGGCTCCTTGGACCCTTCACATTCAAGTGGCCGAGGA                   TCAGCAGAGGCTGCAGAGGATGATGAGATCCGCATGATCAATGAGTTCCCCCGTGTGG                   CCAGTGTGGCCTCCTCTCTGGCTCCCCGTGGCCCTGACTCAGGCATCCAGCAGGATGC                   AGATGGTCTGAGTGACACATCCTGCGAACCACCTGCCCCTGACACCTGGTATAAGGCC                   CGAAAGGCAGGGCTGCTGCTGCCAGGTGCAGGAGCCACTCTCTACAGAGAGGAGGGGC                   CCCCAGCCACTGCCACAGCCTTCCTGGGGGGCTGTGGCCTGAGCCCTGCACCCACTGG                   GGACTATGGCTTCCCAGCAGATGGCAAGCCATGTGTGGCAGGTGCGCTGACAGCCATT                   GTGGCCGGCGAGGAGGAGCTCCGTGGCAOCTATAACTGGGACTACCTGCTGAGCTGGT                   CCCCTCAGTTCCAACCACTGGCCAGTGTCTTCACAGAGATCGCTCGGCTCAAGGATGA                   AGCTCGGCCATGTCCCCCAGCTCCCCGTATCGACCCACCACCCCTCATCACTGCCGTG                   GCCCACCCAGGAGCCAAGTCTGTGCCCCCCAAGCCAGCAAACACAGCTGCAGCCCGGG                   CCATCTTCCCACCAGCTTCTCACCGCTCCCCCATCAGCCATGAAGGCTCCCTGTCCTC                   AGCTGCCATGTCCCCCAGCTTCTCACCCTCTCTGTCTCCTCTGGCTGCTCGCTCACCC                   GTTGTCTCACCATTTGCGGTGGCCCAGGGTCCCTCAGCCTCAGCACTCAGCGCAGAGT                   CTGGCCTGGAGCCACCTGATGACACGGAGCTGCACATCTAGCTGTCAGCCCAGGCTGG                   CCCGACCTGGGATGCGCACAGTGTCCCCAACGCAGGCCCCACTCTCAAGCCTGCCCTG                   GGCAGCCTCGGACTATGACTGGCTACGGGGAGGCCACCACCAGGCCCCAGCTCTCCAC                   CCTGAACTCCCCAGCCCCCTCAGAGTACTAGGACCACAGAAGCCCTGTTGCTCACTGA                   CCTGTGACCAGGTCCAATGTGGGGAGAAATATGAAGGAGGTAGCAGCCCTGGGTTCTC                   CTCAGTGAGGGATCCCTGCCCTGCACCAGCACCCTGAGATCGACCTGAGACTTTATTT                   ATTGGGGGTAGGGGGATGGAGGAGGTCCCTCCAAkCATGTTTGGACCCAGCTCCTTTGG                   GTTCCACTGACACCCCTGCCCCTGCCCCTGCCCAGAACCAAGTGCCATTTCTCACTCT                   GGAGCCTTAATAAACTGCAATTTGTATCC                                         ORF Start: ATG at 411   ORF Stop: TAG at 10305                                         SEQ ID NO: 50   3298 aa   MW at 346176.3 kD                             NOV19b,   MQKELGIVPSCPGMKSPRPHLLLPLLLLLLLLLGAGVPGAWGQAGSLDLQIDEEQPAG           CG132541-02       Protein Sequence   TLIGDISAGLPAGTAAPLMYFISAQEGSGVGTDLAIDEHSGVVRTARVLDREQRDRYR                   FTAVTPDGATVEVTVRVADINDHAPAFPQARAALQVPEHTAFGTRYPLEPARDADAGR                   LGTQGYALSGDGAGETFRLETRPGPDGTPVPELVVTGELDRENRSHYMLQLEAYDGGS                   PPRRAQALLDVTLLDINDHAPAFNQSRYHAVVSESLARGSPVLQVFASDADAGVNGAV                   TYEINRRQSEGDGPFSIDAHTGLLQLERPLDFEQRRVHELVVQARDGGAHPELGSAFV                   TVHVRDANDNQPSMTVIFLSADGSPQVSEAAPRGQLVARISVSDPDDGDFAHVNTSLE                   GGEGHFALSTQDSVIYLVCVARRLDREERDAYNLRVTATDSGSPPLRAEAAFVLHVTD                   VNDNAPAFDRQLYRPEPLPEVALPGSFVVRVTARDPDQGTNGQVTYSLAPGAHTHWFS                   IDPTSGIITTAASLDYELEPQPQLITVATDGGLPPLASSATVSVALQDVNDNEPQFQR                   TFYNASLPEGTQPGTCFLQVTATDADSGPFGLLSYSLGAGLGSSGSPPFRIDAHSGDV                   CTTRTLDRDQGPSSFDFTVTAVDGGGLKSAVYVKVFLSDENDNPPQFYPREYAASISA                   QSPPGTAVLRLRAHDPDQGSHGRLSYHILAGNSPPLFTLDEQSGLLTVAWPLARRANS                   VVQLEIGAEDGGGLQAEPSARVDISIVPGTPTPPIFEQLQYVFSVPEDVAPGTSVGIV                   QAHNPPGRLAPVTLSLSGGDPRGLFSLDAVSGLLQTLRPLDRELLGPVLELEVRAGSG                   VPPAFAVARVRVLLDDVNDNSPAFPAPEDTVLLPPNTAPGTPIYTLRALDPDSGVNSR                   VTFTLLAGGGGAFTVDPTTGHVRLMRPLGPSGGPAHELELEARDGGSPPRTSHFRLRV                   VVQDVGThGLAPRFNSPTYRVDLPSGTTAGTQVLQVQAQAPDGGPITYHLAAEGASSP                   FGLEPQSGWLWVRAALDREAQELYILKVMAVSGSKAELGQQTGTATVRVSILNQNEHS                   PRLSEDPTFLAVAENQPPGTSVGRVFATDRDSGPNGRLTYSLQQLSEDSKAFRIHPQT                   GEVTTLQTLDREQQSSYQLLVQVQDGGSPPRSTTGTVHVAVLDLNDNSPTFLQASGAA                   GGGLPIQVPDRVPPGTLVTTLQAKDPDEGENGTILYTLTGPGSELFSLHPHSGELLTA                   APLIRAERPHYVLTLSAHDQGSPPRSASLQLLVQVLPSARLAEPPPDLAERDPAAPVP                   VVLTVTAAEGLRPCSLLGSVAAPEPAGVGALTYTLVGGADPEGTFALDAASGRLYLAR                   PLDFEAGPPWRALTVRAEGPGGAGARLLRVQVQVQDENEHAPAFARDPLALALPENPE                   PGAALYTFRASDADGPGPNSDVRYRLLRQEPPVPALRLDARTGALSAPRGLDRETTPA                   LLLLVEATDRPANASRRRAARVSARVFVTDENDNAPVFASPSRVRLPEDQPPGPAALH                   VVARDPDLGEAARVSYRLASGGDGHFRLHSSTGALSVVRPLDREQRAEHVLTVVASDH                   GSPPRSATQVLTVSVADVNIDEAPTFQQQEYSVLLRENPPGTSLLTLRATDPDVGANG                   QVTYGGVSSESFSLDPDTGVLTTLRALDREEQEEINLTVYAQDRGSPPQLTHVTVRVA                   VEDENDHAPTFGSAHLSLEVPEGQDPQTLTMLRASDPDVGANGQLQYRILDGDPSGAF                   VLDLASGEFGTMRPLDREVEPAFQLRIEARDGGQPALSATLLLTVTVLDANDHAPAFP                   VPAYSVEVPEDVPAGTLLLQLQAHDPDAGANGHVTYYLGAGTAGAFLLEPSSGELRTA                   AALDREQCPSYTFSVSAVDGAAAGPLSTTVSVTITVRDVNDHAPTFPTSPLRLRLPRP                   GPSFSTPTLALATLRAEDRDAGANASILYRLAGTPPPGTTVDSYTGEIRVARSPVALG                   IPRDRVLFIVATDLGRPARSATGVIIVGLQGEAERGPRFPRASSEATIRENAPPGTPV                   SPRAVHAGGTNGPITYSILSGNEKGTFSIQPSTGAITVRSAEGLDFEVSPRLRLVLQA                   ESGGAFAFTVLTLTLQDANDNAPRFLRPHYVAFLPESRPLEGPLLQVEADDLDQGSGG                   IQISYSLAASQPARGLFHVDPTTGTITTTAILDREIWAETRLVLMATDRGSPALVGST                   LTVMVIDTNDNRPTIPQPWELRVSEDALLGSEIAQVTGNDVDSGPVLWYVLSPSGPQD                   PFSVGRYGGRVSLTGPLDFEQCDRYQLQLLAHDGPHEGRANLTVLVEDvNDNAPAFSQ                   SLYQVMLLEHTPPGSAILSVSATDRDSGANGHISYHLASPADCFSVDPNNGTLFTIVG                   TVALGHDGSGAVDVVLEARDHGAPGRAARATVHVQLQDQNDHAPSFTLSHYRVAVTED                   LPPGSTLLTLEATDADGSRSHAAVDYSILSGNWGRVFQLEPRLAEAGESAGPGPRALG                   CLVLLEPLDFESLTQYNLTVAAADRGQPPQSSVVPVTVTVLDVNDNPPVFTRASYRVT                   VPEDTPVGAELLHVEASDADPCPHGLVRFTVSSGDPSGLFELDESSGTLRLAHALDCE                   TQARHQLVVQADPAGAHFALAPVTIEVQDVNIDHGPAFPLNLLSTSVAENQPPGTLVT                   TLHAIDGDAGAFGRLPYSLLEAGPGPEGREAFALNSSTGELRARVPFDYEHTESFRLL                   VGAADAGNLSASVTVSVLVTGEDEYDPVFLAPAFHFQVPEGARRGHSLGHTQATDEDG                   GADGLVLYSLATSSPYFGTNQTTGALYLRVDSRAPGSGTATSGGGGRTRREAPRELRL                   EVIARGPLPGSRSATVPVTVDITHTALGLAPDLNLLLVGAVAASLGVVVVLALAALVL                   GLVRARSRKAEAAPGPMSQAAPLASDSLQKLGREPPSPPPSEHLYHQTLPSYGGPGAG                   GPYPRGCSLDPSHSSGRGSAEAAEDDEIRMINEFPRVASVASSLAARGPDSGIQQDAD                   GLSDTSCEPPAPDTWYKGRKAGLLLRGAGATLYREEGPPATATAFLGCCGLSPAPTGD                   YGFPADGKPCVAGALTAIVAGEEELRGSYNWDYLLSWCPQFQPLASVFTEIARLKDEA                   RPCPPAPRIDPPPLITAVAHPGAKSVPPKPANTAAkARAIFPPASHRSPISHEGSLSS                   AMSPSFSPSLSPLAARSPVVSPFGVAQGPSASALSAESGLEPPDDTELHI                  
 
     [0430] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 19B.  
               TABLE 19B                          Comparison of NOV19a against NOV19b.                                         Identities/           Protein   NOV19a Residues/   Similarities for the           Sequence   Match Residues   Matched Region                       NOV19b   1 . . . 2318   2162/2318 (93%)               1 . . . 2314   2166/2318 (93%)                      
 
     [0431] Further analysis of the NOV19a protein yielded the following properties shown in Table 19C.  
               TABLE 19C                       Protein Sequence Properties NOV19a                                        PSort   0.7900 probability located in plasma membrane; 0.3000       analysis:   probability located in microbody (peroxisome); 0.3000           probability located in Golgi body; 0.2000           probability located in endoplasmic reticulum (membrane)       SignalP   Cleavage site between residues 43 and 44       analysis:                  
 
     [0432] A search of the NOV19a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 19D.  
               TABLE 19D                          Geneseq Results for NOV19a                                         NOV19a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABB05430   Human dachsous protein SEQ ID   1 . . . 2318   2297/2318 (99%)   0.0           NO: 2 -  Homo sapiens , 3298 aa.   1 . . . 2314   2301/2318 (99%)           [JP2001327295-A, 27 NOV. 2001]       AAU74825   Human REPTR 8 protein -  Homo     14 . . . 2318    2158/2305 (93%)   0.0             sapiens , 3217 aa. [WO200198354-   1 . . . 2233   2170/2305 (93%)           A2, 27 DEC. 2001]       ABB66499     Drosophila melanogaster     25 . . . 2304     875/2445 (35%)   0.0           polypeptide SEQ ID NO 26289 -   7 . . . 2400   1269/2445 (51%)             Drosophila melanogaster , 3503 aa.           [WO200171042-A2, 27 SEP.           2001]       AAU77406   Human NOV2 protein, homologue   14 . . . 611     590/598 (98%)   0.0           of cadherin proteins -  Homo     1 . . . 591     590/598 (98%)             sapiens , 602 aa.           [WO200206329-A2, 24 JAN.           2002]       ABB59831     Drosophila melanogaster     46 . . . 2302     728/2419 (30%)   0.0           polypeptide SEQ ID NO 6285 -   68 . . . 2410    1098/2419 (45%)             Drosophila melanogaster , 5147 aa.           [WO200171042-A2, 27 SEP.           2001]                  
 
     [0433] In a BLAST search of public sequence datbases, the NOV19a protein was found to have homology to the proteins shown in the BLASTP data in Table 19E.  
               TABLE 19E                          Public BLASTP Results for NOV19a                                         NOV19a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q96JQ0   Protocadherin 16 precursor    1 . . . 2318   2297/2318 (99%)   0.0           (Cadherin 19) (Cadherin fibroblast    1 . . . 2314   2301/2318 (99%)           1) -  Homo sapiens  (Human), 3298           aa.       Q24292   DACHSOUS protein precursor   25 . . . 2304    871/2445 (35%)   0.0           (ADHERIN) -  Drosophila      7 . . . 2400   1267/2445 (51%)             melanogaster  (Fruit fly), 3503 aa.       IJFFTM   cadherin-related tumor suppressor   46 . . . 2302    730/2419 (30%)   0.0           precursor - fruit fly ( Drosophila     68 . . . 2410   1097/2419 (45%)             melanogaster ), 5147 aa.       P33450   Cadherin-related tumor suppressor   46 . . . 2302    728/2419 (30%)   0.0           precursor (Fat protein) -   68 . . . 2410   1098/2419 (45%)             Drosophila melanogaster  (Fruit           fly), 5147 aa.       Q99PF4   Cadherin 23 precursor   150 . . . 2300     668/2243 (29%)   0.0           (Otocadherin) -  Mus musculus     40 . . . 2199   1007/2243 (44%)           (Mouse), 3354 aa.                  
 
     [0434] PFam analysis indicates that the NOV19a protein contains the domains shown in the Table 19F.  
               TABLE 19F                          Domain Analysis of NOV19a                                     Identities/                   Similarities       Pfam   NOV19a Match   for the   Expect       Domain   Region   Matched Region   Value               cadherin    47 . . . 134    24/110 (22%)   6.8e−05               61/110 (55%)       cadherin    148 . . . 246    35/111 (32%)   2.9e−09               69/111 (62%)       cadherin    260 . . . 353    39/109 (36%)   1.3e−22               69/109 (63%)       cadherin    371 . . . 463    33/107 (31%)   5.6e−14               71/107 (66%)       cadherin    478 . . . 569    39/107 (36%)   1.4e−23               72/107 (67%)       cadherin    583 . . . 676    38/110 (35%)   2.7e−16               71/110 (65%)       cadherin    690 . . . 781    32/107 (30%)   7.1e−16               67/107 (63%)       cadherin    795 . . . 885    33/107 (31%)   1.2e−11               69/107 (64%)       cadherin    899 . . . 989    32/107 (30%)     7e−16               70/107 (65%)       cadherin   1005 . . . 1096   30/107 (28%)   1.8e−14               67/107 (63%)       cadherin   1110 . . . 1202   44/108 (41%)   7.6e−33               78/108 (72%)       cadherin   1222 . . . 1312   36/107 (34%)   7.2e−21               71/107 (66%)       cadherin   1337 . . . 1427   22/108 (20%)   0.0045               62/108 (57%)       cadherin   1441 . . . 1537   34/108 (31%)   8.9e−08               66/108 (61%)       cadherin   1550 . . . 1640   39/107 (36%)   8.5e−31               78/107 (73%)       cadherin   1654 . . . 1742   42/107 (39%)   2.7e−27               76/107 (71%)       cadherin   1756 . . . 1846   38/107 (36%)   1.8e−19               71/107 (66%)       cadherin   1860 . . . 1951   39/107 (36%)   2.1e−28               77/107 (72%)       cadherin   1974 . . . 2059   27/110 (25%)   0.017                69/110 (63%)       cadherin   2073 . . . 2162   33/109 (30%)     3e−14               70/109 (64%)       cadherin   2176 . . . 2268   43/108 (40%)   2.7e−20               67/108 (62%)                  
 
     Example 20  
     [0435] The NOV20 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 20A.  
               TABLE 20A                       NOV20 Sequence Analysis                                                    SEQ ID NO:51   3400 bp                             NOV20a,     GAATTCTTAGTTGTTTTCTTTAGAAGAACATTTCTAGGGAATAATACAAGAAGATTTA             CC132888-02       DNA Sequence     GGAATCATTGAAGTTATAAATCTTTGGA   ATG AGCAAACTCAGAATGGTGCTACTTGAA                   CACTCTGGATCTGCTGACTTCAGAAGACATTTTGTCAACCTGAGTCCCTTCACCATTA                   CTGTGGTCTTACTTCTCAGTGCCTGTTTTGTCACCAGTTCTCTTGGAGGAACAGACAA                   GGAGCTGAGGCTAGTGGATGGTGAAAACAAGTGTAGCGGGAGAGTGGAAGTGAAAGTC                   CAGGAGGAGTGGGGAACGGTGTGTAATAATGGCTGGAGCATGGAAGCGGTCTCTGTGA                   TTTGTAACCAGCTGGGATGTCCAACTGCTATCAAAGCCCCTGGATGGGCTAATTCCAG                   TGCAGGTTCTGGACGCATTTGGATGGATCATGTTTCTTGTCGTGGGAATGAGTCAGCT                   CTTTGGGATTGCAAACATGATGGATGGGGAAAGCATAGTAACTGTACTCACCAACAAG                   ATGCTGGAGTGACCTGCTCAGATCGATCCAATTTGGAAATGAGGCTGACGCGTGGAGG                   GAATATGTGTTCTGGAAGAATAGAGATCAAATTCCAAGGACGGTGGGGAACAGTGTGT                   GATGATAACTTCAACATAGATCATGCATCTGTCATTTGTAGACAACTTGAATGTGGAA                   GTGCTGTCAGTTTCTCTGGTTCATCTAATTTTGGAGAAGGCTCTGGACCAATCTGGTT                   TGATGATCTTATATGCAACGGAAATGAGTCAGCTCTCTGGAACTGCAAACATCAAGGA                   TGGGGAAAGCATAACTGTGATCATGCTGAGGATGCTGGAGTGATTTGCTCAAAGGGAG                   CAGATCTGAGCCTGAGACTGGTAGATCGAGTCACTGAATGTTCAGGAAGATTAGAAGT                   GAGATTCCAAGGAGAATGGGGGACAATATGTGATGACGGCTGGGACAGTTACGATGCT                   GCTGTGGCATGCAAGCAACTGGGATGTCCkACTGCCGTCACAGCCATTGGTCGAGTTA                   ACGCCAGTAAGGGATTTGGACACATCTGGCTTGACAGCGTTTCTTGCCAGGGACATGA                   ACCTGCTGTCTGGCAATGTAAACACCATGAATGGGGAAAGCATTATTGCAATCACAAT                   GAAGATGCTGGCGTGACATGTTCTGATGGATCAGATCTGGAGCTAAGACTTAGAGGTG                   GAGGCAGCCGCTGTGCTGGGACAGTTGAGGTGGAGATTCAGAGACTGTTAGGGAACGT                   CTGTGACAGAGGCTGGGGACTGAAAGAAGCTGATGTGGTTTGCAGGCAGCTGGGATGT                   GGATCTGCACTCAAAACATCTTATCAAGTGTACTCCAAAATCCAGGCAACAAACACAT                   GGCTGTTTCTAAGTAGCTGTAACGGAAATGPAACTTCTCTTTGGGACTGCAAGAACTG                   GCAATGGGGTGGACTTACCTGTGATCACTATGAAGAAGCCAAAATTACCTGCTCAGCC                   CACAGGGAACCCAGACTGGTTGGAGGGGACATTCCCTGTTCTGGACGTGTTGAAGTGA                   AGCATGGTGACACGTGGGGCTCCATCTGTCATTCGGACTTCTCTCTGGAAGCTGCCAG                   CGTTCTATGCAGGGAATTACAGTGTGGCACAGTTGTCTCTATCCTGGGGGGAGCTCAC                   TTTGGAGAGGGAAATGGACAGATCTGGGCTGAAGAATTCCAGTGTGAGGGACATGAGT                   CCCATCTTTCACTCTGCCCAGTAGCACCCCGCCCAGAAGGAACTTGTAGCCACAGCAG                   GGATGTTGGAGTAGTCTGCTCAAGATACACAGAAATTCGCTTGGTGAATGGCAAGACC                   CCGTGTGAGGGCAGAGTGGAGCTCAAAACGCTTGGTGCCTGGGGATCCCTCTGTAACT                   CTCACTGGGACATAGAAGATGCCCATGTTCTTTGCCAGCAGCTTAAATGTGGAGTTGC                   CCTTTCTACCCCAGGAGGAGCACGTTTTGGAAAAGGAAATGGTCAGATCTGGAGGCAT                   ATGTTTCACTGCACTGGGACTGAGCAGCACATGGGAGATTGTCCTGTAACTGCTCTAG                   GTGCTTCATTATGTCCTTCAGAGCAAGTGGCCTCTGTAATCTGCTCAGGAAACCAGTC                   CCAAACACTGTCCTCGTGCAATTCATCGTCTTTGGGCCCAACAAGGCCTACCATTCCA                   GAAGAAAGTGCTGTGGCCTGCATAGAGAGTGGTCkACTTCGCCTGGTAAATGGAGGAG                   GTCGCTGTGCTGGGAGAGTAGACATCTATCATCAGCGCTCCTGGGGCACCATCTGTGA                   TGACAGCTGGGACCTGAGTGATGCCCACGTGGTTTGCAGACAGCTGGGCTGTGGAGAG                   GCCATTAATGCCACTGGTTCTGCTCATTTTGGGGAAGGAACAGGGCCCATCTGGCTGG                   ATGAGATGAAATGCAATGGAAAACAATCCCGCATTTGGCAGTGCCATTCACACGGCTG                   GGGGCAGCAAAATTGCAGGCACAAGGAGGATGCGGGAGTTATCTGCTCAGAATTCATG                   TCTCTGAGACTGACCAGTGAAGCCAGCAGAGAGGCCTGTGCAGGGCGTCTGGAAGTTT                   TTTACAATGGAGCTTGGGGCACTGTTGGCAAGAGTAGCATGTCTGAAACCACTGTGGG                   TGTGGTGTGCAGGCAGCTGGGCTGTGCAGACAAAGGGAAAATCAACCCTGCATCTTTA                   GACAAGGCCATGTCCATTCCCATGTGGGTGGACAATGTTCAGTGTCCAAAAGGACCTG                   ACACGCTGTGGCAGTGCCCATCATCTCCATGGGAGAAGAGACTGGCCAGCCCCTCGGA                   GGAGACCTGGATCACATGTGACAACAAGATAAGACTTCAGGAAGGACCCACTTCCTGT                   TCTGGACGTGTGGAGATCTGGCATGGAGGTTCCTGGGGGACAGTGTGTGATGACTCTT                   GGGACTTGGACGATGCTCAGGTGGTGTGTCAACAACTTGGCTGTGGTCCAGCTTTGAA                   AGCATTCAAAGAAGCAGAGTTTGGTCAGGGGACTGGACCGATATGGCTCAATGAAGTG                   AAGTCCAAAGGGAATGAGTCTTCCTTGTGGGATTGTCCTGCCAGACGCTGGGGCCATA                   GTGAGTGTGGGCACAAGGAAGACGCTGCAGTGAATTGCACAGATATTTCAGTGCAGAA                   AACCCCACAAAAAGCCACAACAGTTTCCTCAAGAGGAGAGAACTTAGTCCACCAAATT                   CAATACCGGGAGATGAATTCTTGCCTGAATGCAGATGATCTGGACCTAATGAATTCCT                   CAGGAGGCCATTCTGAGCCACACTGAAAAGGAAAATGGGAATTTATAACCCAGTGAGT                   TCAGCCTTTAAGATACCTTGATGAAGACCTGGAGTA                                         ORF Start: ATG at 87   ORF Stop: TGA at 3330                                         SEQ ID NO:52   1081 aa   MW at 117107.8 kD                             NOV20a,   MSKLRMVLLEDSGSADFRRHFVNLSPFTITVVLLLSACFVTSSLGGTDKELRLVDGEN           CG132888-02       CG132888-02   KCSGRVEVKVQEEWGTVCNNGWSMEAVSVICNQLGCPTAIKAPGWANSSAGSGRIWMD       Protein Sequence           HVSCRGNESALWDCKHDGWGKHSNCTHQQDAGVTCSDGSNLEMRLTRGGNMCSGRIEI                   KFQGRWGTVCDDNFNIDHASVICRQLECGSAVSPSGSSNFGEGSGPIWFDDLICNGNE                   SALWNCKHQGWGKHNCDHAEDAGVICSKGADLSLRLVDGVTECSGRLEVRFQGEWGTI                   CDDGWDSYDAAVACKQLGCPTAVTAIGRVNASKGFGHIWLDSVSCQGHEPAVWQCKHH                   EWGKHYCNHNEDAGVTCSDGSDLELRLRGGGSRCAGTVEVEIQRLLGKVCDRGWGLKE                   ADVVCRQLGCGSALKTSYQVYSKIQATNTWLFLSSCNGNETSLWDCKNWQWGGLTCDH                   YEEAKITCSAHREPRLVGGDIPCSGRVEVKHGDTWGSICDSDFSLEAASVLCRELQCG                   TVVSILGGAHFGEGNGQIWAEEFQCEGHESHLSLCPVAPRPEGTCSHSRDVGVVCSRY                   TEIRLVNGKTPCEGRVELKTLGAWGSLCNSHWDIEDAHVLCQQLKCGVALSTPGGARF                   GKGNGQIWRHMFHCTGTEQHMGDCPVTALGASLCPSEQVASVICSGNQSQTLSSCNSS                   SLGPTRPTIPEESAVACIESGQLRLVNCGGRCAGRVEIYHEGSWGTICDDSSDLSDAH                   VVCRQLGCGEAINATGSAHFGEGTGPIWLDEMKCNGKESRIWQCHSHGWGQQNCRHKE                   DAGVICSEFMSLRLTSEASREACAGRLEVFYNGAWGTVGKSSMSETTVGVVCRQLGCA                   DKGKINPASLDKANSIPMWVDNVQCPKGPDTLWQCPSSPWEKRLASPSEETWITCDNK                   IRLQEGPTSCSGRVEIWHGGSWGTVCDDSWDLDDAQVVCQQLGCGPALKAFKEAEFGQ                   GTGPIWLNEVKCKGNESSLWDCPARRWGHSECGHKEDAAVNCTDISVQKTPQKATTVS                   SRGENLVHQIQYREMNSCLNADDLDLMNSSGGHSEPH                  
 
     [0436] Further analysis of the NOV20a protein yielded the following properties shown in Table 20B.  
               TABLE 20B                       Protein Sequence Properties NOV20a                                        PSort   0.6500 probability located in plasma membrane; 0.5658 probability located in       analysis:   mitochondrial inner membrane; 0.3635 probability located in microbody           (peroxisome); 0.3000 probability located in Golgi body       SignalP   Cleavage site between residues 46 and 47       analysis:                  
 
     [0437] A search of the NOV20a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 20C.  
               TABLE 20C                          Geneseq Results for NOV20a                                         NOV20a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAM41280   Human polypeptide SEQ ID NO    1 . . . 1081   1081/1121 (96%)   0.0           6211 -  Homo sapiens , 1124 aa.    4 . . . 1124   1081/1121 (96%)           [WO200153312-A1, 26 JUL.           2001]       AAM41279   Human polypeptide SEQ ID NO    1 . . . 1081   1081/1121 (96%)   0.0           6210 -  Homo sapiens , 1124 aa.    4 . . . 1124   1081/1121 (96%)           [WO200153312-A1, 26 JUL.           2001]       AAM39493   Human polypeptide SEQ ID NO    1 . . . 1081   1081/1121 (96%)   0.0           2638 -  Homo sapiens , 1121 aa.    1 . . . 1121   1081/1121 (96%)           [WO200153312-A1, 26 JUL.           2001]       AAB66039   Human TANGO 234 mature    46 . . . 1067    586/1057 (55%)   0.0           protein -  Homo sapiens , 1413 aa.   324 . . . 1379    737/1057 (69%)           [WO200077239-A2, 21 DEC.           2000]       AAB66040   Human TANGO 234 extracellular    46 . . . 1034    575/989 (58%)   0.0           domain -  Homo sapiens , 1319 aa.   324 . . . 1311    722/989 (72%)           [WO200077239-A2, 21 DEC.           2000]                  
 
     [0438] In a BLAST search of public sequence datbases, the NOV20a protein was found to have homology to the proteins shown in the BLASTP data in Table 20D.  
               TABLE 20D                          Public BLASTP Results for NOV20a                                         NOV20a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q07898   M130 antigen precursor -  Homo      6 . . . 1081   1076/1116 (96%)   0.0             sapiens  (Human), 1116 aa.    1 . . . 1116   1076/1116 (96%)       Q07900   M130 antigen cytoplasmic variant    6 . . . 1075   1070/1110 (96%)   0.0           2 precursor -  Homo sapiens      1 . . . 1110   1070/1110 (96%)           (Human), 1156 aa.       Q07899   M130 antigen cytoplasmic variant    6 . . . 1079   1070/1114 (96%)   0.0           1 precursor -  Homo sapiens      1 . . . 1114   1070/1114 (96%)           (Human), 1151 aa.       Q99MX8   Macrophage hemoglobin    5 . . . 1075    804/1108 (72%)   0.0           scavenger receptor CD163    5 . . . 1108    911/1108 (81%)           precursor -  Mus musculus             (Mouse), 1121 aa.       Q9NR16   Scavenger receptor cysteine-rich    46 . . . 1067    585/1057 (55%)   0.0           type 1 protein M160 precursor -   364 . . . 1419    736/1057 (69%)             Homo sapiens  (Human), 1453 aa.                  
 
     [0439] PFam analysis indicates that the NOV20a protein contains the domains shown in the Table 20E.  
               TABLE 20E                          Domain Analysis of NOV20a                                             Identities/                       Similarities           Pfam   NOV20a Match   for the   Expect           Domain   Region   Matched Region   Value                       SRCR    54 . . . 152    43/115 (37%)   2.2e−30                   80/115 (70%)           SRCR   162 . . . 259    46/114 (40%)   9.6e−34                   79/114 (69%)           SRCR   269 . . . 366    47/114 (41%)   2.4e−35                   80/114 (70%)           SRCR   376 . . . 473    43/114 (38%)   7.4e−24                   73/114 (64%)           SRCR   481 . . . 578    52/114 (46%)     2e−39                   87/114 (76%)           SRCR   586 . . . 683    41/114 (36%)   2.4e−29                   78/114 (68%)           SRCR   722 . . . 819    53/114 (46%)   9.4e−45                   89/114 (78%)           SRCR   829 . . . 926    35/114 (31%)   3.2e−17                   69/114 (61%)           SRCR   932 . . . 1029   51/114 (45%)   2.1e−37                   80/114 (70%)                      
 
     Example 21  
     [0440] The NOV21 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 21A.  
               TABLE 21A                       NOV21 Sequence Analysis                                                    SEQ ID NO: 53   4308 bp                             NOV21a,   ATGGGGAAGAGAGGCATGATGAGAGATCTCTGTGGCTTGTGTGTGCCAAGGTCACCAC           CG133159-01       DNA Sequence   TGGAAACTCTCAAGGACAATACCTGTGTCTCCTCCAAGGCCCATCCCTCGTGCCTAAC                   ACAGTTCCTGGCAGAGACCAGAAACTCCTTTGACTGTTGTGAACCTGATGAGGTCCCT                   GATCACTGTCCAGGGCCGCCAGGCTCCAAGCACAGGGCCCGGCCAGCCCCGGATCCCC                   CTCCCCTCTTCGATGACACAAGCGGTGGTTATTCCAGCCAGCCCGGGGGATACCCAGC                   CACAGGAGCAGACGTGGCCTTCAGTGTCAACCACTTGCTTGGGGACCCAATGCCCAAT                   GTGGCTATCGCCTATGGCAGCTCCATCGCATCCCATGGGAAGGACATGGTGCACAAGG                   AGCTGCACCGTTTTGTGTCTGTGAGCAAACTCAAGTATTTTTTTGCTGTGGACACAGC                   CTACGTGGCCAAGAAGCTAGGGCTGCTGGTCTTCCCCTACACACACCAGAACTGGGAA                   GTGCAGTACAGTCGTCATGCTCCTCTGCCCCCCCGGCAAGACCTCAACGCCCCTGACC                   TCTATATCCCCAGCGTGCTCTGTTATCCCTTCTTCCAAGAAGCCTTTCCTGACCCCCT                   GAGCAAGTGGTGGCTCCCTTCTGGGTTCCCACAACTGCCTGTCCACATGGCATTTTTC                   AGGCTGCCCACACATACAGCTGACTCTTCTCTGTCCTGTTGGCTGCACAGGGCCAGGC                   CCATCGTGGACACCCAGGCGATGGCCTTCATTACTTACGTGCTCCTGGCTGGGATGGC                   ACTGGGCATTCAGAAAAGGTTCTCCCCGGAGGTGCTGGGCCTGTGTGCAAGCACAGCG                   CTGGTGTGGGTGGTGATGGAGGTGCTGGCCCTGCTCCTGGGCCTCTACCTGGCCACCG                   TGCGCAGTGACCTGAGCACCTTTCACCTGCTGGCCTACAGTGGCTACAAATACGTGGG                   AATGATCCTCAGTGTGCTCACGGGGCTGCTGTTCGGCAGCGATGGCTACTACGTGGCG                   CTGGCCTGGACCTCATCGGCGCTCATGTACTTCATTGTGCGCTCTTTGCGGACAGCAG                   CCCTGGGCCCCGACAGCATGGGGGGCCCCGTCCCCCGGCAGCGTCTCCAGCTCTACCT                   GACTCTGGGAGCTGCAGCCTTCCAGCCCCTCATCATATACTGGCTGACTTTCCACCTG                   GTCCGGCAGCTGCTACCCTCACCTCCAGAGGTGGTAGAAGAGGAGGGGGATGTTGAGG                   CCCAGGGTCACCCACTCTGCTGCACACAGAAACATCAGACAGAAGACGCCGTGGATGC                   AGTATTCTGGGACCACCAGCTGGGGGATGACTACCTGTTTAAGCTGCTTTTGATTGGC                   GACTCAGGCGTGGGCAAGTCATGCCTGCTCCTGCGGTTTGCTGATGACACGTACACAG                   AGAGCTACATCAGCACCATCGGGGTGGACTTCAAGATCCGAACCATCGAGCTGGATGG                   CAAAACTATCAAACTTCAGATCTGGGACACAGCGGCCCAGGAACGGTTCCGGACCATC                   ACTTCCAGCTACTACCGGGGGGCTCATGGCATCATCGTGGTGTATGACGTCACTGACC                   AGATTCACAAGTGCCAGTTCCGGCCCGGCCATTGTTCkAGGCCCTTGAGATTTAACTG                   CGAACAAGGTGGGGGTGGCTCTGGCATTCTACTGACGGAAACAGACAATAAACTTGCA                   TACAGAACCACCGTGACTTTAGGAGTGATAAGGTCAATGCTTCCAATAGAGTTGGAGC                   AAGTGCGCCAQAAGCTGCTGCAGCTGCTCCGCACCTACTCACCCAGCGCCCAGGTCAA                   GCGGCTCCTGCAGGCCTGCAAGCTGCTCTACATGGCCCTGAGGACCCAGCAAGGGGAG                   GGCGCGGGTGCCGACGAGTTCCTGCCTCTGCTGAGCCTCGTCTTGGCCCACTGTGACC                   TTCCTGACCTGCTGCTGGAGGCCGAGTACATGTCGGAGCTGCTGGAGCCCAGCCTGCT                   TACTGGAGAGGGTCGCTACTACCTGACCAGCCTCTCTGCCAGCCTGGCCCTGCTGAGT                   GGCCTGGGTCAGGCCCACACCCTCCCACTGAGCCCCGTGCAGGAGCTACGGCGCTCCC                   TCAGCCTCTGGGAGCAGCGCCGCCTCCCTGCCACCCACTGCTTCCAGCACCTCCTCCG                   AGTAGCCTATCAGGATCCCAGCAGTGGCTGCACCTCCAAGACCCTGGCCGTGCCCCCA                   GAGGCCTCGATTGCCACCCTGAACCAGCTCTGTGCCACCAAGTTCCGAGTGACCCAGC                   CCAACACTTTTCGCCTCTTCCTGTACAAGGAGCAGGGCTACCACCGCCTGCCCCCTGG                   GGCCCTGGCCCACAGGCTGCCCACCACTGGCTACCTCGTCTACCGCCGGGCAGAGTGG                   CCTGAGACCCAGGGGGCTGTGACAGAGGAGGAGGGCAGTGGGCAGTCAGAGGCAAGAA                   GCAGAGGGGAGGAGCAAGGGTGCCAGGGAGATGGGGATCCTGGGGTCAAAGCCAGCCC                   CAGGGACATTCGGGAACAGTCTGAGACAACTGCTGAAGGGGGCCAGGAGTTTGAGTGG                   CTGCCCTTCGGCTCTGTGGCCGCTGTGCAGTGCCAGGCTGGCAGGGGAGCCTCTCTGC                   TCTGCGTGAAGCAGCCTGAGGGAGGTGTGGGCTGGTCACGGGCTGGGCCCCTGTGCCT                   GGGGACTGGCTGCAGCCCTGACAACGGGGGCTGCGAACACGAATGTGTGGAGGAGGTG                   GATGGTCACGTGTCCTGCCGCTGCACTGAGGGCTTCCGGCTGGCAGCAGACGGGCGCA                   GTTGCGAGGACCCCTGTCCCCAGGCTCCGTGCGAGCAGCAGTGTGAGCCCGGTGGGCC                   ACAAGGCTACAGCTGCCACTGTCGCCTGGGTTTCCGGCCAGCGGAGGATGATCCGCAC                   CGCTGTGTGGACACAGATGAGTGCCAGATTGCCGGTGTGTGCCAGCAGATGTGTGTCA                   ACTACGTTGGTGGCTTCGAGTGTTATTGTAGCGAGGGACATGAGCTGGAGGCTGATGG                   CATCAGCTGCAGCCCTGCAGGGGCCATGGGTGCCCAGGCTTCCCAGGACCTCGGAGAT                   GAGTTGCTGGATGACGGCGAGGATGAGGAAGATGAAGACGAGGCCTGGAACGCCTTCA                   ACGGTGGCTGGACGGAGATGCCTGGGATCCTGTGGATGGAGCCTACGCAGCCGCCTGA                   CTTTGCCCTGGCCTATAGACCGAGCTTCCCAGAGGACAGAGAGCCACAGATACCCTAC                   CCGGAGCCCACCTGGCCACCCCCGCTCAGTGCCCCCAGGGTCCCCTACCACTCCTCAG                   TGCTCTCCGTCACCCGGCCTGTGGTGGTCTCTGCCACGCATCCCACACTGCCTTCTGC                   CCACCAGCCTCCTGTGATCCCTGCCACACACCCAGCTTTGTCCCGTGACCACCAGATC                   CCCGTGATCGCAGCCAACTATCCACATCTGCCTTCTGCCTACCAACCCGGTATTCTCT                   CTGTCTCTCATTCAGCACAGCCTCCTGCCCACCAGCCCCCTATGATCTCAACCAAATA                   TCCGGAGCTCTTCCCTGCCCACCAGTCCCCCATGTTTCCAGACACCCGGGTCGCTGGC                   ACCCAGACCACCACTCATTTGCCTGGAATCCCACCTAACCATGCCCCTCTGGTCACCA                   CCCTCGGTGCCCAGCTACCCCCTCAAGCCCCAGATGCCCTTGTCCTCAGAACCCAGGC                   CACCCAGCTTCCCATTATCCCAACTGCCCAGCCCTCTCTGACCACCACCTCCAGGTCC                   CCTGTGTCTCCTGCCCATCAAATCTCTGTGCCTGCTGCCACCCAGCCCGCAGCCCTCC                   CCACCCTCCTGCCCTCTCAGAGCCCCACTAACCAGACCTCACCCATCAGCCCTACACA                   TCCCCATTCCAAAGCCCCCCAAATCCCAAGGGAAGATGGCCCCAGTCCCAAGTTGGCC                   CTGTGGCTGCCCTCACCAGCTCCCACAGCAGCCCCAACAGCCCTGGGGGAGGCTGGTC                   TTGCCGAGCACAGCCAGAGGGATGACCGGTGGCTGCTGGTGGCACTCCTGGTGCCAAC                   GTGTGTCTTTTTGGTGGTCCTGCTTGCACTGGGCATCGTGTACTGCACCCGCTGTGGC                   CCCCATGCACCCAACAAGCGCATCACTGACTGCTATCGCTGGGTCATCCATGCTGGGA                   GCAAGAGCCCAACAGAACCCATGCCCCCCAGGGGCAGCCTCACAGGGGTGCAGACCTG                   CAGAACCAGCGTGTGA                                         ORF Start: ATG at 1   ORF Stop: TGA at 4306                                         SEQ ID NO:54   1435 aa   MW at 156118.8 kD                             NOV21a,   MGKRGMMRDLCGLCVPRSPVETLKDNTCVSSKAHPSCLTQFLAETRNSFDCCEPDEVP           CG133159-01       Protein Sequence   DHCPGPPGSKHRARAAPDPPPLFDDTSCGYSSQPGGYPATGADVAFSVNHLLGDPMAN                   VAMAYGSSIASHGKDMVHKELHRFVSVSKLKYFFAVDTAYVAKKLGLLVFPYTHQNWE                   VQYSRDAPLPPRQDLNAPDLYIPSVLCYPFFQEAFPDPLSKWWLPSGFPQLPVHMAFF                   RLPTHTADSSLSCWLHRARPIVDTQAMAFITYVLLAGMALGIQKRFSPEVLGLCASTA                   LVWVVMEVLALLLGLYLATVRSDLSTFHLLAYSGYKYVGMILSVLTGLLFCSDGYYVA                   LAWTSSALMYFIVRSLRTAALGPDSMGGPVPRQRLQLYLTLGAAAFQPLIIYWLTFHL                   VRQLLPSPPEVVEEEGDVEAQGHPLCCTQKHQTEEAVDGVFWDHQLGDDYLFKLLLIG                   DSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTI                   TSSYYRGAHGIIVVYDVTDQTHKCQFRPGHCSRPLRFNCEQGGGGSGILVTETDNKLA                   YRTTVTLGVIRSMLPIELEQVRQKLLQLLRTYSPSAQVKRLLQACKLLYMALRTQEGE                   GAGADEFLPLLSLVLAHCDLPELLLEAEYMSELLEPSLLTGEGGYYLTSLSASLALLS                   GLGQAHTLPLSPVQELRRSLSLWEQRRLPATHCFQHLLRVAYQDPSSGCTSKTLAVPP                   EASIATLNQLCATKFRVTQPNTFGLFLYKEQGYHRLPPGALAHRLPTTGYLVYRRAEW                   PETQGAVTEEEGSGQSEARSRGEEQGCQGDGDAGVKASPRDIREQSETTAEOGQEFEW                   LPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLGTGCSPDNGGCEHECVEEV                   DGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGFRPAEDDPH                   RCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQASQDLGD                   ELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDFALAYRPSFPEDREPQIPY                   PEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPALSRDHQI                   PVIAANYPDLPSAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAG                   TQTTTHLPGIPPNHAPLVTTLGAQLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRS                   PVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPREDGPSPKLA                   LWLPSPAPTAAPTALGEAGLAEHSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCG                   PHAPNKRITDCYRWVIHAGSKSPTEPMPPRGSLTGVQTCRTSV                  
 
     [0441] Further analysis of the NOV21a protein yielded the following properties shown in Table 21B.  
               TABLE 21B                       Protein Sequence Properties NOV21a                                        PSort   0.6000 probability located in plasma membrane; 0.4000 probability located in       analysis:   Golgi body; 0.3000 probability located in endoplasmic reticulum (membrane);           0.3000 probability located in microbody (peroxisome)       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0442] A search of the NOV21a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 21C.  
               TABLE 21C                          Geneseq Results for NOV21a                                         NOV21a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABB90732   Human Tumour Endothelial    867 . . . 1435    569/569 (100%)   0.0           Marker polypeptide SEQ ID NO    189 . . . 757     569/569 (100%)           196 -  Homo sapiens , 757 aa.           [WO200210217-A2, 07 FEB.           2002]       ABB90721   Human Tumour Endothelial    867 . . . 1435    569/569 (100%)   0.0           Marker polypeptide SEQ ID NO    189 . . . 757     569/569 (100%)           177 -  Homo sapiens , 757 aa.           [WO200210217-A2, 07 FEB.           2002]       AAM25557   Human protein sequence SEQ ID    941 . . . 1435   489/495 (98%)   0.0           NO: 1072 -  Homo sapiens , 494 aa.     2 . . . 494    489/495 (98%)           [WO200153455-A2, 26 JUL.           2001]       AAB93749   Human protein sequence SEQ ID   1003 . . . 1435   432/433 (99%)   0.0           NO: 13411 -  Homo sapiens , 433     1 . . . 433    432/433 (99%)           aa. [EP1074617-A2, 07 FEB           2001]       AAM93967   Human stomach cancer expressed   1003 . . . 1435   432/433 (99%)   0.0           polypeptide SEQ ID NO 2 -  Homo       1 . . . 433    432/433 (99%)             sapiens , 433 aa. [WO200109317-           A1, 08 FEB. 2001]                  
 
     [0443] In a BLAST search of public sequence datbases, the NOV21a protein was found to have homology to the proteins shown in the BLASTP data in Table 21D.  
               TABLE 21D                          Public BLASTP Results for NOV21a                                         NOV21a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q9HCU0   Tumor endothelial marker 1    867 . . . 1435    569/569 (100%)   0.0           precursor (Endosialin protein) -    189 . . . 757     569/569 (100%)             Homo sapiens  (Human), 757 aa.       Q96KB6   CDNA FLJ14384 fis, clone   1003 . . . 1435   432/433 (99%)   0.0           HEMBA1002150 -  Homo sapiens       1 . . . 433    432/433 (99%)           (Human), 433 aa.       Q91ZV1   Endosialin -  Mus musculus      867 . . . 1435   431/586 (73%)   0.0           (Mouse), 765 aa.    189 . . . 765    469/586 (79%)       Q91V98   Tumor endothelial marker 1    867 . . . 1435   430/586 (73%)   0.0           precursor (Endosialin) -  Mus      189 . . . 765    468/586 (79%)             musculus  (Mouse), 765 aa.       Q96CC8   Hypothetical 84.1 kDa protein -    595 . . . 866    271/272 (99%)   e−154             Homo sapiens  (Human), 783 aa.    489 . . . 760    272/272 (99%)                  
 
     [0444] PFam analysis indicates that the NOV21a protein contains the domains shown in the Table 21E.  
               TABLE 21E                          Domain Analysis of NOV21a                                     Identities/                   Similarities       Pfam   NOV21a Match   for the   Expect       Domain   Region   Matched Region   Value               arf   445 . . . 619    40/202 (20%)   0.0036                102/202 (50%)        ras   459 . . . 628    69/210 (33%)   1.6e−30               131/210 (62%)        VPS9   595 . . . 700    51/107 (48%)   2.7e−50               97/107 (91%)       RA   730 . . . 811    22/113 (19%)   9.8e−17               70/113 (62%)       EGF   913 . . . 949     13/47 (28%)   4.6e−06                31/47 (66%)       TIL   936 . . . 994     19/74 (26%)   0.17                  40/74 (54%)       EGF   994 . . . 1028    13/47 (28%)   0.00035                26/47 (55%)                  
 
     Example 22  
     [0445] The NOV22 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 22A.  
               TABLE 22A                       NOV22 Sequence Analysis                                                    SEQ ID NO: 55   1902 bp                             NOV22a,     CCCCAGTGCGGCCGGGGCGCGGGTTCGAGCTGCTGCTCGGCAAGCCTGGGTGTCTAGG             CG133508-01       DNA Sequence     GC   ATG AGCGGAGTGTGGGGGGCCGGCGGGCCTCGGTGCCAGGAGGCGCTCGCGGTCCT                   CGCCTCGCTGTGCCGGGCCCGGCCGCCCCCTCTCGGGCTGGACGTGGAGACTTGTCGG                   AGCTTCGAGCTGCAGCCCCCAGAGCGGAGTCCCAGCGCGGCAGGCGCAGGCACCTCTG                   TCAGCCTCCTCGCAGTTGTAGTTATTGTGTGTGGCGTGGCCCTGGTGGCAGTTTTTCT                   CTTTCTCTTTTGGAAGCTGTGCTGGATGCCCTGGAGGAACAAGGAGGCCTCCAGTCCC                   TCTTCTGCTAATCCCCCCTTGGAAGCCCTCCAGAGCCCCACCTTCAGAGGCAACATGG                   CGGACAAGCTGAAGGACCCCAGCACCCTGGGCTTCCTGGAGGCCGCCGTGAAGATCAG                   CCACACGTCCCCAGATATCCCACCTGAGGTGCAGATGTCGGTCAAGGAGCACATCATG                   CGTCACACCCGGCTGCAGCGGCAAACTACACAGCCAGCGTCATCCACCAGGCACACGT                   CCTTCAAGCGCCACCTGCCAAGGCAGATGCATGTCTCCAGTGTAGACTATGGCAATGA                   GCTTCCACCAGCAGCAGAGCAGCCCACCAGCATTGGCCGCATCAAGCCTGAGCTCTAC                   AAGCAGAAGTCGGTGGATGGGGAGGATGCCAAGTCTGAGGCCACCAAGAGCTGCGGGA                   AGATCAACTTCAGCCTACGCTACGATTACGAGACCGAGACCCTGATTGTGCGTATCCT                   GAAGGCTTTTGACCTCCCTGCCAAGGACTTTTGTGGAAGCTCTGACCCTTATGTCAAG                   ATCTACCTCCTGCCTGACCGCAAATGCAAGCTGCAGACCCGGGTGCACCGCAAGACCC                   TGAACCCCACCTTTGATGAGAACTTCCACTTCCCTGTGCCCTATGAGGAGCTGGCTGA                   CCGCAAGCTGCATCTCAGTGTCTTCGACTTTGACCGCTTCTCCCGCCATGACATGATT                   GGCGAGGTCATCCTGGACAACCTCTTTCAGGCCTCTGACCTGTCTCGGGAAACCTCCA                   TCTGGAAGGATATCCAATATGCCACAAGTGAAAGCGTGGACTTGGGAGAGATCATGTT                   CTCCCTTTGCTACCTGCCCACTGCAGGCAGGCTCACCCTCACAGTGATTAAGTGTCGG                   AACCTCAAGGCGATGGACATCACAGGCTATTCAGATCCCTATGTGAAAGTGTCCTTGC                   TCTGTGATGGGCGGAGGCTGAACAAGAAGAAAACAACCATAAACAAAAACACTCTCAA                   TCCTGTCTACAATGAGGCCATCATCTTTGACATTCCCCCGGAAAACATGGATCAAGTC                   AGCCTGCTCATCTCAGTCATGGACTATGATCGAGTGGGCCACAATGAGATCATAGGAG                   TCTGTCGTGTGGGGATCACTGCTGAAGGCCTGGGCAGGGACCACTGGAACGAGATGCT                   GGCATACCCCCGGAAGCCCATCGCACACTGGCACTCCTTGGTGGAGGTAAAGAAATCC                   TTCAAAGAGGGAAACCCTCGGTTG TGA   TTTCATTCACGTCCATGCCGCAAGCAGAGAG                       ACTGCCACCTGGAGTTAGGATGGCAGGCCCGAGCTGCTAGCTTCGACAGTGAGAGCTC                       GTGCCCATCTCCGAAACCACCTCCAACACCATGAGATGTGCAGCCAAATAACACAAAT                       GGGACTCAGCAATGTTCTCTTTGCACTTGTTCAACCGTCTAAACAGTGTTGTGCAGTC                       GCAGTGGCGGCAGCAGCGGCAGCCGTCCGTCACTCCAGAGTCTTACCTGCTCCTGTGT                       AGGTCAAAGCTGAGACACTTGTCATGTGGTCAGATCTGTCTTAGTC                                           ORF Start: ATG at 61   ORF Stop: TGA at 1591                                         SEQ ID NO:56   510 aa   MW at 57324.3 kD                             NOV22a   MSGVWGAGGPRCQEALAVLASLCRARPPPLGLDVETCRSFELQPPERSPSAAGAGTSV           CG133508-01       Protein Sequence   SLLAVVVIVCGVALVAVFLFLFWKLCWMPWRNKEASSPSSANPPLEALQSPSFRGNMA                   DKLKDPSTLGFLEAAVKISHTSPDIPAEVQMSVKEHIMRHTRLQRQTTEPASSTRHTS                   FKRHLPRQMHVSSVDYGNELPPAAEQPTSIGRIKPELYKQKSVDGEDAKSEATKSCCK                   INFSLRYDYETETLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTL                   NPTFDENFHFPVPYEELADRKLHLSVFDFDRFSRHDMIGEVILDNLFEASDLSRETSI                   WKDIQYATSESVDLGEIMFSLCYLPTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLL                   CDGRRLKKKKTTIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNETIGV                   CRVGITAEGLGRDHWNEMLAYPRKPIAHWHSLVEVKKSFKEGNPRL                                         SEQ ID NO: 57   675 bp                             NOV22b,     GGA TCCCTGATTGTGCGTATCCTGAAGGCTTTTGACCTCCCTGCCAAGGACTTTTGTG           225171562 DNA       Sequence   GAAGCTCTGACCCTTATGTCAAGATCTACCTCCTGCCTGACCGCAAATGCAAGCTGCA                   GACCCGGGTGCACCGCAAGACCCTGAACCCCACCTTTGATGAGAACTTCCACTTCCCT                   GTGCCCTATGAGGAGCTGGCTGACCGCAAGCTGCATCTCAGTGTCTTCGACTTTGACC                   GCTTCTCCCGCCATGACATGATTGGCGAGGTCATCCTGGACAACCTCTTTGAGGCCTC                   TGACCTGTCTCGGGPAACCTCCATCTGGAAGGATATCCAATATGCCACAAGTGAAAGC                   GTGGACTTGGGAGAGATCATGTTCTCCCTTTGCTACCTGCCCACTGCAGGCAGGCTCA                   CCCTCACAGTGATTAAGTGTCGGAACCTCAAGGCGATGGACATCACAGGCTATTCAGA                   TCCCTATGTGAAAGTGTCCTTGCTCTGTGATGGGCGGAGGCTGAAGAAGAAGAAAACA                   ACCATAAAGAAAAACACTCTCAATCCTGTCTACAATGAGGCCATCATCTTTGACATTC                   CCCCGGAAAACATGGATCAAGTCAGCCTGCTCATCTCAGTCATGGACTATGATCGAGT                   GGGCCACAATGAGATCATAGGAGTCTGTCGTCTCGAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 58   225 aa   MW at 25902.6 kD                             NOV22b,   GSLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTLNPTFDENFHFP           225171562       Protein Sequence   VPYEELADRKLHLSVFDFDRFSRHDMTGEVILDNLFEASDLSRETSIWKDIQYATSES                   VDLGEIMFSLCYLRTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLLCDGRRLKKKKT                   TIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNEIIGVCRLE                  
 
     [0446] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 22B.  
               TABLE 22B                          Comparison of NOV22a against NOV22b.                                         Identities/           Protein   NOV22a Residues/   Similarities for           Sequence   Match Residues   the Matched Region                       NOV22b   245 . . . 467   210/223 (94%)                2 . . . 224   212/223 (94%)                      
 
     [0447] Further analysis of the NOV22a protein yielded the following properties shown in Table 22C.  
               TABLE 22C                       Protein Sequence Properties NOV22a                                        PSort   0.6760 probability located in plasma membrane; 0.1000       analysis:   probability located in endoplasmic reticulum (membrane);           0.1000 probability located in endoplasmic reticulum           (lumen); 0.1000 probability located in outside       SignalP   Cleavage site between residues 26 and 27       analysis:                  
 
     [0448] A search of the NOV22a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 22D.  
               TABLE 22D                          Geneseq Results for NOV22a                                         NOV22a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAU19715   Human novel extracellular matrix   82 . . . 510   428/429 (99%)   0.0           protein, Seq ID No 365 -  Homo     33 . . . 461   429/429 (99%)             sapiens , 461 aa. [WO200155368-           A1, 02 AUG. 2001]       AAU87165   Novel central nervous system   82 . . . 421   339/340 (99%)   0.0           protein #75 -  Homo sapiens , 412 aa.   33 . . . 372   340/340 (99%)           [WO200155318-A2, 02 AUG. 2001]       ABB05693   Human cell   12 . . . 510   261/580 (45%)   e−127           signaling/communication protein   10 . . . 583   340/580 (58%)           clone amy2_2o13 -  Homo sapiens ,           590 aa. [WO200198454-A2, 27           DEC. 2001]       AAE17499   Human secretion and trafficking   12 . . . 510   261/580 (45%)   e−127           protein-8 (SAT-8) -  Homo sapiens ,   10 . . . 583   340/580 (58%)           590 aa. [WO200202610-A2, 10           JAN. 2002]       AAU19714   Human novel extracellular matrix   230 . . . 500    179/272 (65%)   e−105           protein, Seq ID No 364 -  Homo     10 . . . 281   218/272 (79%)             sapiens , 295 aa. [WO200155368-           A1, 02 AUG. 2001]                  
 
     [0449] In a BLAST search of public sequence datbases, the NOV22a protein was found to have homology to the proteins shown in the BLASTP data in Table 22E.  
               TABLE 22E                          Public BLASTP Results tor NOV22a                                         NOV22a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q9R0N8   Synaptotagmin VI -  Mus      1 . . . 510   493/511 (96%)   0.0             musculus  (Mouse), 511 aa.    1 . . . 511   498/511 (96%)       Q62746   Synaptotagmin VI -  Rattus      1 . . . 510   490/511 (95%)   0.0             norvegicus  (Rat), 511 aa.    1 . . . 511   498/511 (96%)       Q9QUK7   Synaptotagmin VIDELTATM2 -   86 . . . 510   413/426 (96%)   0.0             Mus musculus  (Mouse), 426 aa.    1 . . . 426   416/426 (96%)       Q9R0N4   Synaptotagmin X (SytX) -  Mus     12 . . . 499   331/499 (66%)   0.0             musculus  (Mouse), 523 aa.   13 . . . 501   390/499 (77%)       Q925B8   Synaptotagmin 10 -  Rattus     12 . . . 499   330/499 (66%)   0.0             norvegicus  (Rat), 523 aa.   13 . . . 501   390/499 (78%)                  
 
     [0450] PFam analysis indicates that the NOV22a protein contains the domains shown in the Table 22F.  
               TABLE 22F                          Domain Analysis of NOV22a                                             Identities/                       Similarities for           Pfam   NOV22a Match   the Matched   Expect           Domain   Region   Region   Value                       C2   246 . . . 332   45/97 (46%)   5.2e−35                   77/97 (79%)           C2   378 . . . 466   44/97 (45%)   7.3e−37                   78/97 (80%)                      
 
     Example 23  
     [0451] The NOV23 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 23A.  
               TABLE 23A                       NOV23 Sequence Analysis                                                    SEQ ID NO: 59   1751 bp                             NOV23a,     CGGGAGCCTCTCCCTGAGGGGCACCGCGTTCTTCAGGAGCTGGGCCTCCAGTGCGGCG             CG133548-01       DNA Sequence     CGATGTCAGGCGCGGTGACAGCTCTGTGAGTCCGAGGCCGCGGCGTGTGGCTGGGCGG                       CTGCGGGGCCTGACCGGTCCGCTC   ATG GTGCCGCCACGACGCCATCGCGGGGCAGGAA                   GGCCAGGGGTGCTGAGTTCTTCACCTCCTTTTAGACTGAGATCTGCCAAGTTTTCCGG                   CATTGCTCTTGAGGATCTCAGAAGGGCTCTTAAGACAAGACTGCAAATGGTGTGTGTA                   TTTGTCATGAACCGAATGAATTCCCAGAACAGTGGTTTCACTCACCGCAGGCGAATGG                   CTCTTGGGATTGTTATTCTTCTGCTTGTTGATGTGATATGGGTTGCTTCCTCTGAACT                   TACTTCGTATGTTTTTACCCAGTACAACAAACCATTCTTCAGCACCTTTGCAAAAACA                   TCTATGTTTGTTTTGTACCTTTTGGGCTTTATTATTTGGAAGCCATGCAGACAACAGT                   GTACAAGAGGACTTCGCGGAAAGCATGCTGCTTTTTTTGCAGATGCTGAAGGTTACTT                   TCCTGCTTGCACAACAGATACAACTATGAATAGTTCTTTGAGTGAACCTCTGTATGTG                   CCTGTGAAATTCCATGATCTTCCAAGTGAAAAACCTGAGAGCACAAACATTGATACTG                   AAAAAAGTCCCAAAAAGTCTCGTGTGAGGTTCAGTAATATCATGGAGATTCGACAGCT                   TCCGTCAAGTCATGCATTGGAAGCAAAGTTGTCTCGCATGTCATATCCTGTGAAAGAA                   CAAGAATCCATACTGAAAACTGTGGGGAAACTTACTGCAACTCAAGTAGCGAAAATTA                   GCTTTTTTTTTTGCTTTGTGTGGTTTTTGGCAAATTTGTCATATCAAGAAGCACTTTC                   AGACACACAAGTTGCTATAGTTAATATTTTATCTTCAACTTCCGGTCTTTTTACCTTA                   ATCCTTGCTGCAGTATTTCCAAGTAACAGTGGAGATAGATTTACCCTTTCTAAACTAT                   TAGCTGTAATTTTAAGCATTGGAGGCGTTGTACTGGTAAACCTGGCAGGGTCTGAAAA                   ACCTGCTGGAACAGACACAGTAGGTTCCATTTGGTCTCTTGCTGGAGCCATGCTCTAT                   GCTGTCTATATTGTTATGATTAAGAGAAAAGTAGATAGAGAAGACAAGTTGGATATTC                   CAATGTTCTTTGGTTTTCTAGGTTTGTTTAATCTGCTGCTCTTATGGCCAGGTTTCTT                   TTTACTTCATTATACTGGATTTGAGQACTTCGAGTTTCCCAATAAAGTAGTATTAATC                   TGCATTATCATTAATGGCCTTATTGGAACAGTACTCTCAGAGTTCCTGTGGTTGTGGG                   GCTGCTTTCTTACCTCATCATTGATAGGCACACTTGCACTAAGCCTTACAATACCTCT                   GTCCATAATAGCTGACATGTGTATGCAAAAGGTACAGTTTTCTTGGTTATTTTTTGCA                   GGAGCTATCCCTGTATTTTTTTCATTTTTTATTGTAACTCTCCTATGCCATTATAATA                   ATTGGGATCCTGTGATGGTGGGAATCAGAAGAATATTTGCTTTTATATGCAGAAAACA                   TCGAATTCAGAGGCTTCCAGAAGACAGCGAACAGTGTGAGAGTCTCATTTCTATGCAC                   AGTGTTTCTCAGGAGGATGGAGCTAGTTAGCTGTCTGTTGTCTGTAGCCCAGGTTTGT                     ATGTGAGCTGG                                           ORF Start: ATG at 141   ORF Stop: TAG at 1710                                         SEQ ID NO: 60   523 aa   MW at 58872.3 kD                             NOV23a,   MVPPRRHRGAGRPGVLSSSPPFRLRSAKFSGIALEDLRRALKTRLQMVCVFVMNRMNS           CG133548-01       Protein Sequence   QNSGFTQRRRMALGIVILLLVDVIWVASSELTSYVFTQYNKPFFSTFAKTSMFVLYLL                   GFIIWKPWRQQCTRCLRGKHAAFFADAEGYFAACTTDTTMNSSLSEPLYVPVKFHDLP                   SEKPESTNIDTEKSPKKSRVRFSNIMEIRQLRSSHALEAKLSRMSYPVKEQESILKTV                   GKLTATQVAKISFFFCFVWFLANLSYQEALSDTQVAIVNILSSTSGLFTLILAAVFPS                   NSGDRFTLSKLLAVILSIGGVVLVNLAGSEKPAGRDTVGSIWSLAGAMLYAVYIVMIK                   RKVDREDKLDIPMFFGFVGLFNLLLLWPGFFLLHYTGFEDFEFPNKVVLMCIIINGLI                   GTVLSEFLWLWGCFLTSSLIGTLALSLTIPLSIIADMCMQKVQFSWLFFAGAIPVFPS                   FFIVTLLCHYNNWDPVMVGIRRIFAFICRKHRIQRVPEDSEQCESLISMHSVSQEDGA                                         SEQ ID NO:61   1607 bp                             NOV23b,     CGGGAGCCTCTCCCTGAGGCiAGCACCGCGTTCTTCAGGAGCTGGGCCTCCAGTGCGGCG             CG133548-02       DNA Sequence     CGATGTCAGGCGCGGTGACAGCTCTGTGAGTCCGAGGCCGCGGCGTGTGGCTGGGCGG                       CTGCGGGGCCTGACCGGTCCGCTC   ATG GTGCCGCCACGACGCCATCGCGGGGCAGGAA                   GGCCAGGGATGCTGAGTTCTTCACCTCCTTTTAGACTGAGATCTGCCAAGTTTTCCGG                   CATTGCTCTTGAGGATCTCAGAAGGGCTCTTAAGACAAGACTGCAAATGGTGTGTGTA                   TTTGTCATGACCGATGAATTCCCAGAACAGTGGTTTCACTCAGCGCAGGCGAAAATGG                   CTCTTGGGATTGTTATTCTTCTGCTTGTTGATGTGATATGGGTTGCTTCCTCTGAACT                   TACTTCGTTTGCAGATGCTGAAGGTTACTTTGCTGCTTGCACAACAGATACAACTATC                   AATAGTTCTTTGAGTGAACCTCTGTATGTGCCTGTGAAATTCCATGATCTTCCAAGTG                   AAAAACCTGAGAGCACAAACATTGATACTGAAAAAAGTCCCAAAAAGTCTCGTGTGAG                   GTTCAGTAATATCATGGAGATTCGACAGCTTCCGTCAACTCATGCATTGGAAGCAAAC                   TTGTCTCGCATGTCATATCCTGTGPAAGAACAAGAATCCATACTGAAAACTGTGGGGA                   AACTTACTGCAACTCAAGTAGCGAAAATTAGCTTTTTTTTTTGCTTTGTGTGGTTTTT                   GGCAAATTTGTCATATCAAGAAGCACTTTCAGACACACAAGTTGCTATAGTTAATATT                   TTATCTTCAACTTCCGGTCTTTTTACCTTAATCCTTGCTGCAGTATTTCCAAGTAACA                   GTGGAGATAGATTTACCCTTTCTAAACTATTAGCTGTAATTTTAAGCATTGGAGGCGT                   TGTACTGGTAAACCTGGCAGGGTCTGAAAAACCTGCTGGAAGAGACACAGTAGGTTCC                   ATTTGGTCTCTTGCTGGAGCCATGCTCTATGCTGTCTATATTGTTATGATTAAGAGAA                   AAGTAGATAGAGAAGACAAGTTGGATATTCCAATGTTCTTTGGTTTTGTAGGTTTGTT                   TAATCTGCTGCTCTTATGGCCAGGTTTCTTTTTACTTCATTATACTGGATTTGAGGAC                   TTCGAGTTTCCCAATAAAGTAGTATTAATGTGCATTATCATTAATGGCCTTATTGGAA                   CAGTACTCTCAGAGTTCCTGTGGTTGTCGGCCTGCTTTCTTACCTCATCATTGATAGG                   CACACTTGCACTAAGCCTTACAATACCTCTGTCCATAATAGCTGACATGTGTATGCAA                   AAGGTACAGTTTTCTTCGTTATTTTTTGCAGGAGCTATCCCTGTATTTTTTTCATTTT                   TTATTGTAACTCTCCTATGCCATTATAATAATTGGGATCCTGTGATGGTGGGAATCAG                   AAGAATATTTGCTTTTATATGCAGAAAACATCGAATTCAGAGGGTTCCAGAAGACAGC                   GAACAGTGTGAGAGTCTCATTTCTATGCACAGTGTTTCTCAGGAGGATGGAGCTAGT T                       AG   CTGTCTGTTGTCTGTAGCCCAGGTTTGTATGTGAGCTGG                                           ORF Start: ATG at 141   ORF Stop: TAG at 1566                                         SEQ ID NO: 62   475 aa   MW at 53094.6 kD                             NOV23b,   MVPPRRHRGAGRPGVLSSSPPFRLRSAKFSGIALEDLRRALKTRLQMVCVFVMNRMNS           CG133548-02       Protein Sequence   QNSGFTQRRRMALGIVILLLVDVIWVASSELTSFADAEGYFAACTTDTTMNSSLSEPL                   YVPVKFHDLPSEKPESTNIDTEKSPKKSRVRFSNIMEIRQLPSSHALEAKLSRMSYPV                   KEQESILKTVGKLTATQVAKISFFFCFVWFLANLSYQEALSDTQVAIVNILSSTSGLF                   TLILAAVPPSNSGDRFTLSKLLAVILSIGGVVLVNLAGSEKPAGRDTVGSIWSLAGAM                   LYAVYIVMIKRKVDREDKLDIPMFFGFVGLFNLLLLWPGFFLLHYTGFEDFEFPNKVV                   LMCIIINGLIGTVLSEFLWLWGCFLTSSLIGTLALSLTIPLSIIADMCMQKVQFSWLF                   FAGAIPVFFSFFIVTLLCHYNNWDPVMVGIRRIFAPICRKHRIQRVPEDSEQCESLIS                   MHSVSQEDGAS                  
 
     [0452] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 23B.  
               TABLE 23B                          Comparison of NOV23a against NOV23b.                                         Identities/                   Similarities for           Protein   NOV23a Residues/   the Matched           Sequence   Match Residues   Region                       NOV23b   15 . . . 523   431/509 (84%)               15 . . . 475   431/509 (84%)                      
 
     [0453] Further analysis of the NOV23a protein yielded the following properties shown in Table 23C.  
               TABLE 23C                       Protein Sequence Properties NOV23a                                        PSort   0.6000 probability located in plasma membrane; 0.4000       analysis:   probability located in Golgi body; 0.3000 probability           located in endoplasmic reticulum (membrane); 0.3000           probability located in microbody (peroxisome)       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0454] A search of the NOV23a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 23D.  
               TABLE 23D                          Geneseq Results for NOV23a                                         NOV23a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAU12294   Human PRO6097 polypeptide   1 . . . 523   522/523 (99%)   0.0           sequence -  Homo sapiens , 523 aa.   1 . . . 523   523/523 (99%)           [WO200140466-A2, 07 JUN. 2001]       AAE21623   Human gene 14 encoded secreted   1 . . . 523   520/523 (99%)   0.0           protein, SEQ ID NO: 95 -  Homo     1 . . . 523   521/523 (99%)             sapiens , 523 aa. [WO200222654-           A1, 21 MAR. 2002]       AAE21622   Human gene 14 encoded secreted   1 . . . 523   520/523 (99%)   0.0           protein, SEQ ID NO: 94 -  Homo     19 . . . 541    521/523 (99%)             sapiens , 541 aa. [WO200222654-           A1, 21 MAR. 2002]       AAE21611   Human gene 14 encoded secreted   56 . . . 523    465/468 (99%)   0.0           protein HOSDW58, SEQ ID NO: 83 -   1 . . . 468   466/468 (99%)             Homo sapiens , 468 aa.           [WO200222654-A1, 21 MAR. 2002]       AAB58385   Lung cancer associated polypeptide   187 . . . 523    336/337 (99%)   0.0           sequence SEQ ID 723 -  Homo     1 . . . 337   337/337 (99%)             sapiens , 337 aa. [WO200055180-           A2, 21 SEP. 2000]                  
 
     [0455] In a BLAST search of public sequence datbases, the NOV23a protein was found to have homology to the proteins shown in the BLASTP data in Table 23E.  
               TABLE 23E                          Public BLASTP Results for NOV23a                                         NOV23a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q8WV83   Similar to RIKEN cDNA   1 . . . 523   522/523 (99%)   0.0           1300003P13 gene -  Homo sapiens     1 . . . 523   523/523 (99%)           (Human), 523 aa.       Q8R314   RIKEN cDNA 1300003P13 gene -   1 . . . 523   492/524 (93%)   0.0             Mus musculus  (Mouse), 524 aa.   1 . . . 524   508/524 (96%)       Q9DBK9   1300003P13Rik protein -  Mus     1 . . . 523   491/524 (93%)   0.0             musculus  (Mouse), 524 aa.   1 . . . 524   508/524 (96%)       Q9H7D8   CDNA: FLJ21013 fis, clone   156 . . . 523    366/368 (99%)   0.0           CAE05223 -  Homo sapiens     1 . . . 368   367/368 (99%)           (Human), 368 aa.       Q9H6P8   CDNA: FLJ22004 fis, clone   10 . . . 247    234/238 (98%)   e−130           HEP06871 -  Homo sapiens     4 . . . 241   236/238 (98%)           (Human), 244 aa.                  
 
     [0456] PFam analysis indicates that the NOV23a protein contains the domains shown in the Table 23F.  
               TABLE 23F                          Domain Analysis of NOV23a                                             Identities/                       Similarities for           Pfam   NOV23a Match   the Matched   Expect           Domain   Region   Region   Value                       DUF6   338 . . . 470   19/136 (14%)   0.082                   92/136 (68%)                      
 
     Example 24  
     [0457] The NOV24 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 24A.  
               TABLE 24A                       NOV24 Sequence Analysis                                                    SEQ ID NO:63   5964 bp                             NOV24a,     GCTGACCACAAC   ATG GCTGCGGCGCCTGGGCTGCTCGTCTGGCTGCTCGTGCTCCGGC           CG133569-01       DNA Sequence   TGCCCTGGCGGGTGCCGGGCCAGCTGGACCCCAGCACTGGCCGGCGGTTCTCGGAGCA                   CAAACTCTGCGCGGACGACGAATGCAGCGTGTTAATGTACCGCGGTGAGGCTCTTGAA                   GATTTCACAGGCCCGGATTGTCGTTTTGTGAATTTTAAAAAAGGTGATCCTGTATATG                   TTTTGGATATTTTCCAAAAGATTTAATCCAGGTAGTTCATGAATATACCAAAGAAGAG                   CTACAAGTTCCAACAGATGAGACGGATTTTGTTTGTTTTGATGGAGGAAGAGATGATT                   TTCATAATTATAATGTAGAAGAACTTTTAGGGTTTTTGGAACTGTACAATTCTGCAGC                   TACAGATTCTGAGAAAGCTGTAGAAAAAACTTTACAGGATATGGAAAAAAACCCTGAA                   TTATCTAAGGAAAGGGAACCTGAACCTGAACCAGTAGAAGCCAACTCAGAGGAAAGTG                   ATAGTGTATTCTCAGAAAACACTGAGGATCTTCAGQAACAGTTTACAACTCAGAAGCA                   CCACTCCCATGCAAACAGCCAAGCAAATCATGCTCAGGGAGAGCAGGCTTCATTTGAA                   TCTTTTGAAGAAATGCTGCAAGATAACTAAAGTGCCAGAAAGTGAAAACAACAAAAAA                   CCAGCAATAGTTCTCAGGTCTCAAATGAACAGGATAAGATTGATGCCTATAAAATTTT                   GAAAAAAGAAATGACTCTAGACTTGAAAACCAAATTTGGCTCAACAGCTGATGCACTT                   GTATCTGATGATGAGACAACCAGACTCGTTACTTCATTAGAAGATCATTTTGATGAGG                   AATTGGATACTGAGTATTATGCAGTTGGAAAGGAAGATGAGGAGAACCAAGAAGACTT                   TGATGAGTTGCCATTACTTACCTTTACAGATGGGGAAGATATAAAAACTCCAGCAAAG                   TCTGGCGTTGAGAAATATCCAACAGATAAAAGAGCAGAAATTCATGAAGAGGACAAGG                   TTCAGCTAACTGTGCCCCCTGGCATCAAAAATGATGATAAAAATATACTAACAACCTG                   GGGGGACACTATCTTCTCTATTGTCACAGGAGGTGAAGAAACAAGAGATACGATGGAT                   TTAGAGAGCTCTAGTTCAGAGGAAGAAAAAGAAGATGATGATGATGCATTAGTCCCAG                   ATAGCAAACAGGGGAAACCACAGTCAGCAACAGATTATAGTGACCCTGACAATGTAGA                   TGATGGTCTTTTTATTGTAGACATTCCTAACAAAATAATGACAAGAAGTAAACGCAAA                   GAACATCACATTAAAGGAAAAGGGAGGGGAGTTCAGGAATCCAAGAGGGGCCTGGTAC                   AAGATAAGACAGAATTAGAGGATGAAAATCAAGAAGGCATGACTGTGCACAGTTCTGT                   TCACAGCAATAACCTCAACTCTATGCCAGCTGCTGAAAAGGGTAAACACACATTAAAA                   TCAGCTTATGATGATACAGAAAATGACCTAAAAGGAGCAGCTATTCATATCTCAAAAG                   GAATGCTCCACGAAGAAAAGCCTGGAGAGCAGATTTTGGAAGGTGGCTCAGAGAGTGA                   ATCTGCACAGAAAGCTGCAGGGAATCAAATGAATGACAGAAAGATTCAACAGGAATCC                   CTGGGTAGTGCACCACTCATGGGAGATGACCACCCTAACGCATCCAGAGACAGTGTGG                   AGGGAGACGCTTTGGTAAATGGGGCCAAACTGCACACGCTTTCAGTGGAGCATCAACG                   TGAGGAATTGAAAGAGGAATTAGTTCTTAAAACTCAAAACCAACCTAGATTCTCCTCT                   CCAGATGAGATTGATTTGCCCAGAGAACTGGAAGACGAGGTTCCCATTCTGGGAAGAA                   ATCTTCCCTGGCAACAAGAAAGAGATGTGGCTGCCACAGCCAGTAAGCAAATGAGTGA                   GAAGATAAGGCTCTCTGAGCGAGAAGCCAAAGAGGACTCCTTGGATGAAGAGTTTTTT                   CATCACAAGGCAATGCAGGGCACAGAGGTAGGACAGACAGACCAAACTGACAGCACAG                   GAGGACCAGCTTTCCTTTCTAAGTAGAIXGAGGATGATTATCCCTCTGAAGAACTACT                   AGAGGATGAAAACGCTATAAATGCAAAACGGTCTAAAGAAAAAAACCCTGGGAATCAG                   GGCAGGCAGTTTGATGTTAATCTCCAAGTCCCTGACAGAGCAGTTTTAGGGACCATTC                   ATCCAGATCCAGAAATTGAAGAAAGCAAGCAAGkAACTAGTATGATTTTGGATAGCGA                   AAAAACAAGTGAGACTGCTGCCAAAGGGGTCAACACAGGAGGCAGGGAACCAAATACA                   ATGGTGGAAAAAGAACGCCCTCTGGCAGATAAGAAAGCACAGAGACCATTTGAACGAA                   GTGACTTTTCTGACAGCATAAAAATTCAGACTCCAGAATTAGGTGAAGTGTTTCAGAA                   TAAAGATTCTGATTATCTGAAGAACGACAACCCTGAGGAACATCTGAAGACCTCAGGG                   CTTGCAGGGGAGCCTGAGGGAGAACTCTCAAAAGAGGACCATGAGAACACAGAGAAGT                   ACATGGGCACAGAAAGCCAGGGGTCTGCTGCTGCAGAACCTGAAGATGACTCGTTCCA                   CTGGACTCCACATACAAGTGTAGAGCCAGGGCATAGTGACAAGAGGGAGGACTTACTT                   ATCATAAGCAGCTTCTTTAAAGAACAACAGTCTTTGCAGCGGTTCCAGAAGTACTTTA                   ATGTCCATGAGCTGGAAGCCTTGCTACAAGAAATGTCATCAAAACTGAAGTCAGCGCA                   GCAGGAGAGCCTGCCCTATAATATGGAAAAAGTCCTAGATAAGGTCTTCCGTGCTTCT                   GAGTCACAAATTCTGAGCATAGCAGAAAAAATGCTTGATACTCGTGTGGCTGAAAATA                   GAGATCTGGGAATGAACGAAAATAACATATTTGAAGAGGCTGCAGTGCTTGATGACAT                   TCAAGACCTCATCTATTTTGTCAGGTACAAGCACTCCACAGCAGAGGAGACAGCCACA                   CTCGTCATCGCACCACCTCTAGAGGAAGGCTTGGGTGGAGCAATGGAAGAGATGCAAC                   CACTGCATGAAGATAATTTCTCACGAGAGAAGACAGCAGAACTTAATGTGCAGGTTCC                   TGAAGAACCCACCCACTTGGACCAACGTGTGATTGGGGACACTCATGCCTCAGAAGTG                   TCACAGAAGCCAAATACTGAGAAAGACCTGGACCCAGGGCCAGTTACAACAGAAGACA                   CTCCTATGGATGCTATTGATGCAAACAAGCAACCAGAGACAGCCGCCGAAGAGCCGGC                   AAGTGTCACACCTTTGGAAAACGCAATCCTTCTAATATATTCATTCATGTTTTATTTA                   ACTAAGTCGCTAGTTGCTACATTGCCTGATGATGTTCAGCCTGGGCCTGATTTTTATG                   GACTGCCATGGAAACCTGTATTTATCACTGCCTTCTTGGGAATTGCTTCGTTTGCCAT                   TTTCTTATGGAGAACTGTCCTTGTTGTGAAGGATAGAGTATATCAAGTCACGGAACAG                   CAAATTTCTGAGAAGTTGAAGACTATCATGAAAGAAAATACAGAACTTGTACAAAAAT                   TGTCAATTATGAACAGAAGATCAAGGAATCAJAAAGAACATGTTCAGGAAACCAGGAA                   ACAAAATATGATTCTCTCTGATGAAGCAATTAAATATAAGGATAAAATCAAGACACTT                   GAAAAAAATCAGGAAATTCTGGATGACACAGCTAAAAATCTTCGTGTTATGCTAGAAT                   CTGAGAGAGAACAGAATGTCAAGAATCAGGACTTGATATCAGAAAACAAGAAATCTAT                   AGAGAAGTTAAAGGATGTTATTTCAATGAATGCCTCAGAGTTTTCAGAGGTTCAGATT                   GCACTTAATGAAGCTAAGCTTAGTGPAGAGAAGGTGAAGTCTGAATGCCATCGGGTTC                   AAGAAGAAAATGCTAGGCTTAAGAAGAAAAAAGAGCAGTTGCAGCAGGAAATCGAAGA                   CTGGAGTAAATTACATGCTGAGCTCAGTGAGCAAATCAAATCATTTGAGAAGTCTCAG                   AAAGATTTGGAAGTAGCTCTTACTCACAAGGATGATAATATTAATGCTTTGACTAACT                   GAATTACACAGTTGAATCTGTTAGAGTGTGAATCTGAATCTGAGGGTCAAAATAAAGG                   TGGAAATGATTCAGATGAATTAGCAAATGGAGAACTGGGAGGTGACCGGAATGAGAAG                   ATGAAAAATCAAATTAAGCAGATGATGGATGTCTCTCGGACACAGACTGCAATATCGG                   TAGTTGAAGAGGATCTAAAGCTTTTACAGCTTAAGCTAAGAGCCTCCGTGTCCACTAA                   ATGTAACCTGGAAGACCAGGTAAAGAAATTGGAAGATGACCGCPACTCACTACAAGCT                   GCCAAAGCTGGACTGGAAGATGAATGCAAAACCTTGAGGCAGAAAGTGGAGATTCTGA                   ATGAGCTCTATCAGCAGAAGGAGATGGCTTTGCAAAAGAAGCTGAGTCAAGAAGAGTA                   TGAACGGCAAGAAAGAGAGCACAGGCTGTCAGCTGCAGATGAAAAGGCAGTTTCGGCT                   GCACAGGAAGTAAAAACTTACAAGCGGAGAATTGAAGAAATGGAGGATCAATTACAGA                   AGACAGAGCGGTCATTTAAAAACCAGATCGCTACCCATGAGAAGAAAGCTCATGAAAA                   CTGGCTCAAAGCTCGTGCTGCAGAAAGAGCTATAGCTGAAGAGAAAAGGGAAGCTGCC                   AATTTGAGACACAAATTATTAGAATTAACACAAAACATGGCAATGCTGCAAGAAGAAC                   CTGTGATTGTAAAACCAATGCCAGGAAAACCAAATACACAAAACCCTCCACCCACAGC                   TCCTCTGAGCCAGAATGGCTCTTTTCGCCCATCCCCTGTGAGTGGTGGAGAATGCTCC                   CCTCCATTGACAOTGOAOCCACCCGTGAGACCTCTCTCTGCTACTCTCAATCGPAGAG                   ATATGCCTAGAAGTGAATTTGGATCAGTCGACCOGCCTCTACCTCATCCTCGATGGTC                   AGCTGAGGCATCTGGGAAACCCTCTCCTTCTGATCCAGGATCTGGTACAGCTACCATG                   ATGAACAGCAGCTCAAGAGGCTCTTCCCCTACCAGGGTACTCGATGAAGGCAAGGTTA                   ATATGGCTCCAAAAOGOCCCCCTCCTTTCCCAGGAGTCCCTCTCATGAGCACCCCCAT                   GGGAGGCCCTGTACCACCACCCATTCOATATGGACCACCACCTCAGCTCTGCGGACCT                   TTTGGGCCTCGGCCACTTCCTCCACCCTTTGGCCCTGGTATGCGTCCACCACTAGGCT                   TAAGAGAATTTGCACCAGGCGTTCCACCAGGAAGACGGGACCTGCCTCTCCACCCTCG                   GGGATTTTTACCTGGACACGCACCATTTAGACCTTTAGGTTCACTTGGCCCAAGAGAG                   TACTTTATTCCTGGTACCCGATTACCACCCCCAACCCATGGTCCCCAGGAATACCCAC                   CACCACCTOCTGTAAGAGACTTACTGCCGTCAGGCTCTAGAGATGAGCCTCCACCTGC                   CTCTCAGAGCACTAGCCAGGACTGTTCACAOGCTTTAAAACAGAGCCCA TAA   AACTAT                       GACCTCTGAGGTTTCATTGGAAAGAAAGTGTACTGTGCATTATCCATTACAGTAAAGG                       ATTTCATTGGCTTCAAAATCCAAAAGTTTATTTTAAAAGGTTTGTTGTTAGAACTAAG                       CTGCCTTGGCAGTGTGCATTTTTGAGCCAAACAATTCAAAAATGTCATTTCTTCCCTA                       AATAAAAATCACCTTTTAAGCTAAAAAGAAAAAAAAAAAAAAAAAAAA                                           ORF Start: ATG at 13   ORF Stop: TAA at 5734                                         SEQ ID NO: 64   1907 aa   MW at 213668.2 kD                             NOV24a,   MAAAPGLLVWLLVLRLRWRVPGQLDPSTGRRFSEHKLCADDECSVLMYRGEALEDFTG           CG133569-01       Protein Sequence   PDCRFVNFKKGDPVYVYYKLARGWPEVWAGSVGRTFGYFPKDLIQVVHEYTKEELQVP                   TDETDFVCFDGGRDDFHNYNMEELLGFLELYNSAATDSEKAVEKTLQDMEKNPELSKE                   REPEPEPVEANSEESDSVFSENTEDLQEQFTTQKHHSHANSQANHAQGEQASFESFEE                   MLQDKLKVPESENNKTSNSSQVSNEQDKIDAYKLLKKEMTLDLKTKFGSTADALVSDD                   ETTRLVTSLEDDFDEELDTEYYAVGKEDEENQEDFDELPLLTFTDGEDMKTPAKSGVE                   KYPTDKEQNSNEEDKVQLTVPPGIKNDDKNILTTWGDTIFSIVTGGEETRDTMDLESS                   SSEEEKEDDDDALVPDSKQGKPQSATDYSDPDNVDDGLFIVDIPKTNNDKEVNAEHHI                   KGKGRGVQESKRGLVQDKTELEDENQEGMTVHSSVHSNNLNSMPAAEKGKDTLKSAYD                   DTENDLKGAAIHISKGMLHEEKPGEQILECGSESESAQKAAGNQMNDRKIQQESLGSA                   PLMGDDHPNASRDSVEGDALVNGAKLHTLSVEHQREELKEELVLKTQNQPRFSSPDEI                   DLRRELEDEVPILGRNLPWQQERDVAATASKQMSEKIRLSEGEAKEDSLDEEFFHHKA                   MQGTEVGQTDQTDSTGGPAFLSKVEEDDYPSEELLEDENAINAKRSKEKNPGNQGRQF                   DVNLQVPDRAVLGTIHPDPEIEESKQETSMILDSEKTSETAAKGVNTGGREPNTMVEK                   ERPLADKKAQRPFERSDFSDSTKIQTPELGEVFQNKDSDYLKNDNPEEHLKTSGLAGE                   PEGELSKEDHENTEKYMGTESQGSAAAEPEDDSFHWTPHTSVEPGHSDKREDLLIISS                   FFKEQQSLQRFQKYFNVHELEALLQEMSSKLKSAQQESLPYNMEKVLDKVFRASESQI                   LSIAEKMLDTRVAENRDLGMNENNIFEEAAVLDDIQDLIYFVRYKHSTAEETATLVMA                   PPLEEGLCGAMEEMQPLHEDNFSREKTAELNVQVPEEPTHLDQRVIGDTHASEVSQKP                   NTEKDLDPGPVTTEDTPMDAIDANKQPETAAEEPASVTPLENAILLIYSFMFYLTKSL                   VATLPDDVQPGPDFYGLPWKPVFTTAFLGIASFAIFLWRTVLVVKDRVYQVTEQQISE                   KLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQ                   EILDDTAKNLRVMLESEREQNVKNQDLTSENKKSIEKLKDVISMNASEFSEVQIALNE                   AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE                   VALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ                   IKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAG                   LEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEV                   KTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRH                   KLLELTQKMAMLQEEPVIVKPMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLT                   VEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKPSPSDPGSGTATMMNSS                   SRGSSPTRVLDEGKVNMAPKGPPPFPGVPLMSTPMGGPVPPRIRYGPPPQLCGPFGPR                   PLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIP                   GTRLPPPTHGPQEYPPPPAVRDLLPSGSRDEPPPASQSTSQDCSQALKQSP                                         SEQ ID NO: 65   4985 bp                             NOV24b,     GCTGACCACAAC   ATG GCTGCGGCGCCTGGGCTCCTCGTCTGGCTGCTCGTGCTCCGGC           CG133569-02       DNA Sequence   TGCCCTGGCGGGTGCCGGGCCAGCTGGACCCCACCACTGGCCGGCGGTTCTCGGAGCA                   CAAACTCTGCGCGGACGACGAATGCAGCGTGTTAATGTACCCCCGTGAGGCTCTTGAA                   GATTTCACAGGCCCGGATTGTCGTTTTGTGAATTTTAAAAAAGGTGATCCTGTATATG                   TTTACTATAAACTGGCAAGAGGATGGCCTGAAGTTTGGGCTGGAAGTGTAGGACGCAC                   TTTTGGATATTTTCCAAAAGATTTAATCCAGGTAGTTCATGAATATACCAAAGAAGAG                   CTACAAGTTCCAACAGATGAGACGGATTTTGTTTGTTTTGATGGAGGAAGAGATGATT                   TTCATAATTATAATGTAGAAGAACTTTTAGGGTTTTTGGAACTGTACAATTCTGCAGC                   TACAGATTCTGAGAAAGCTGTAGAAAAAACTTTACAGGATATGGAAAAAAACCCTGAA                   TTATCTAAGGAAAGGGAACCTGAACCTGAACCAGTAGAAGCCAACTCAGAGGAAAGTG                   ATAGTGTATTCTCAGAAAACACTGAGGATCTTCACGAACAGTTTACAACTCAGAAGCA                   CCACTCCCATGCAAACAGCCAAGCAAATCATGCTCAGGGAGAGCAGGCTTCATTTGAA                   TCTTTTGAAGAAATGCTGCAAGATAAAACTAAAAAGTGCCAGAAAGTGAACAACAAAA                   CCAGCAATAGTTCTCAGGTCTCAAATGAACAGGATAAGATTGATGCCTATAAACTTTT                   GAAAAAAGAAATGACTCTAGACTTGAAAACCAAATTTGGCTCAACAGCTGATGCACTT                   GTATCTGATGATGAGACAACCAGACTCGTTACTTCATTAGAAGATGATTTTGATGAGG                   AATTGGATACTGAGTATTATGCAGTTGGAGGAAGATGAGGAGAAACCAAGAAAGACTT                   TGATGAGTTGCCATTACTTACCTTTACAGATGGGGAAGATATGAAAACTCCAGCAAAG                   TCTGGCGTTGAGAAATATCCAACAGATAAGAGCAGAAATTCAAATGAAGAGGACAAGG                   TTCAGCTAACTGTGCCCCCTGGCATCAAAAATGATGATAAAAATATACTAACAACCTG                   GGGGGACACTATCTTCTCTATTGTCACAGGAGGTGAAGAAACAAGAGATACGATGGAT                   TTAGAGAGCTCTAGTTCAGAGGAAGAAAAAGAAGATGATGATGATGCATTAGTCCCAG                   ATAGCAAACAGGGGAAACCACAGTCAGCAACAGATTATAGTGACCCTGACAATGTAGA                   TGATGGTCTTTTTATTGTAGACATTCCTAAAACAAATAATGACAAAGAAGTAAACGCA                   GAACATCACATTAAAGGAAAAGAAACGGGAGTTCACGAATCCAAGAGGGGCCTGGTAC                   AAGATAAGACAGAATTAGAGGATGAAAATCAAGAAGGCATGACTGTGCACAGTTCTGT                   TCACAGCAATAACCTCAACTCTATGCCAGCTGCTGAAAAGGGTAAAGACACATTAAAA                   TCAGCTTATGATGATACAGAAAATGACCTAAAAGGAGCAGCTATTCATATCTCAAAAG                   GAATGCTCCACGAAGAAAAGCCTGGAGAGCAGATTTTGGAAGGTGGCTCAGAGAGTGA                   ATCTGCACAGAAAGCTGCAGGGAATCAAATGAATGACAGAAAGATTCAACAGGAATCC                   CTCGGTAGTGCACCACTCATGGGACATGACCACCCTAACGCATCCAGAGACAGTGTGG                   AGGGAGACGCTTTGGTAAATCGCGCCAAACTGCACACGCTTTCAGTGGAGCATCAACG                   TGAGGAATTGPAAGAGGAATTAGTTCTTAAAACTCAAAACCAACCTAGATTCTCCTCT                   CCAGATGAGATTGATTTGCCCAGAGAACTGGAAGACGAGGTTCCCATTCTGGGAAGAA                   ATCTTCCCTGGCAACAAGAAAGAGATGTGGCTGCCACAGCCAGTAAGCAAATGAGTGA                   GAAGATAAGGCTCTCTGAGGGAGAAGCCAAAGAGGACTCCTTGGATGAAGAGTTTTTT                   CATCACAAGGCAATGCAGGGCACAGAGGTAGGACAGACACACCAAACTGACAGCACAG                   GAGGACCAGCTTTCCTTTCTAAAGTAGAAGAGGATGATTATCCCTCTGAAGAACTACT                   AGAGGATGAAAACGCTATAAATGCAAAACGGTCTAAGAAAAAAAACCCTGGGAATCAG                   GGCAGGCAGTTTGATGTTAATCTGCAAGTCCCTGACAGAGCAGTTTTAGGGACCATTC                   ATCCAGATCCAGAAATTGAAGAAAGCAAGCAAGAAACTAGTATGATTTTGGATAGCGA                   AAAAACAAGTGAGACTGCTGCCAAAGGGGTCAACACAGGAGGCAGGGAACCAAATACA                   ATGGTGGAAAAAGAACGCCCTCTGGCAGATAAGAAAGCACAGAGACCATTTGAACGAA                   GTGACTTTTCTGACAGCATAAAAATTCAGACTCCAGAATTAGGTGAAGTGTTTCAGAA                   TAAAGATTCTGATTATCTGAAGAACGACAACCCTGAGGAACATCTGAAGACCTCAGGG                   CTTGCAGGGGAGCCTGAGGGAGAACTCTCAAAAGAGGACCATGAGAACACAGAGAAGT                   ACATCGGCACAGAAAGCCAGGGGTCTGCTGCTGCAGAACCTGAAGATGACTCGTTCCA                   CTGGACTCCACATACAAGTGTAGAGCCAGGGCATAGTGACAAGAGGGAGGACTTACTT                   ATCATAAGCAGCTTCTTTAAAGAACAACAGTCTTTGCAGCGGTTCCAGAAGTACTTTA                   ATGTCCATGAGCTGGAAGCCTTGCTACAAGAAATGTCATCAAAACTGAAGTCAGCGCA                   GCAGGAGAGCCTGCCCTATAATATGGAAAAAGTCCTAGATAAGGTCTTCCGTGCTTCT                   GAGTCACAAATTCTGAGCATAGCAGAAAAAATGCTTGATACTCGTGTGGCTGAAAATA                   GAGATCTGGGAATGAACGAAAATAACATATTTGAAGAGGCTGCAGTGCTTGATGACAT                   TCAAGACCTCATCTATTTTGTCAGGTACAAGCACTCCACAGCAGAGGAGACAGCCACA                   CTGGTGATGGCACCACCTCTAGAGGAAGGCTTGGGTGGAGCAATGGAAGAGATGCAAC                   CACTGCATGAAGATAATTTCTCACGAGAGAAGACAGCAGAACTTAATGTGCAGGTTCC                   TGAAGAACCCACCCACTTCGACCAACGTGTGATTGGGGACACTCATGCCTCAGAAGTG                   TCACAGAAGCCAAATACTGAGAAAGACCTGGACCCAGGGCCAGTTACAACAGAACACA                   CTCCTATGGATGCTATTGATGCAAACAAGCAACCAGAGACAGCCGCCGAAGAGCCGGC                   AAGTGTCACACCTTTGGAAAACGCAATCCTTCTAATATATTCATTCATGTTTTATTTA                   ACTAAGTCGCTAGTTGCTACATTGCCTGATGATGTTCACCCTGGGCCTGATTTTTATG                   GACTGCCATCGAAACCTGTATTTATCACTGCCTTCTTGGGAATTGCTTCGTTTGCCAT                   TTTCTTATGGAGAACTGTCCTTGTTGTGAAGGATAGAGTATATCAAGTCACGGAACAG                   CAAATTTCTGAGAAGTTGAAGACTATCATGAAAGAAAATACAGAACTTGTACAAAAAT                   TGTCAAATTATGAACAGAAGATCAAGGAATCAAAGAAACATGTTCAGGAAACCAGGAA                   ACAAAATATGATTCTCTCTGATGAAGCAATTAAATATAAGGATAAAATCAAGACACTT                   GAAAAAAATCAGGAAATTCTGGATGACACAGCTAAAAATCTTCGTGTTATGCTAGAAT                   CTGAGAGAGAACAGAATGTCAAGAATCAGGACTTGATATCAGAAAACAAGAAATCTAT                   AGAGAAGTTAAAGGATGTTATTTCAATGAATGCCTCAGAGTTTTCAGAGGTTCAGATT                   GCACTTAATGAAGCTAAGCTTAGTGAAGAGAAGGTGAAGTCTGAATGCCATCGGGTTC                   AAGAAGAAAATGCTAGGCTTAAGAAGAAAAAAGAGCAGTTGCAGCAGGAAATCGAAGA                   CTGGAGTAAATTACATGCTGAGCTCAGTGAGCAAATCAAATCATTTGAGAAGTCTCAG                   AAAGATTTGGAAGTAGCTCTTACTCACAAGGATGATAATATTAATGCTTTGACTAACT                   GCATTACACAGTTGAATCTGTTAGAGTGTGAATCTGAATCTGAGGGTCAAAATAAAGG                   TGGAAATGATTCAGATGAATTAGCAAATGGAGAAGTGGGAGGTGACCGGAATGAGAAG                   ATGAAAAATCAAATTAAGCAGATGATGGATGTCTCTCGGACACAGACTGCAATATCGG                   TAGTTGAAGAGGATCTAAAGCTTTTACAGCTTAAGCTAAGAGCCTCCGTGTCCACTCC                   TCCACCCTTTGGCCCTGGTATGCGTCCACCACTAGGCTTAAGAGAATTTGCACCAGGC                   GTTCCACCAGGAAGACGGGACCTGCCTCTCCACCCTCGGGGATTTTTACCTGGACACG                   CACCATTTAGACCTTTAGGTTCACTTGGCCCAAGAGAGTACTTTATTCCTGGTACCCG                   ATTACCACCCCCAACCCATGGTCCCCAGGAATACCCACCACCACCTGCTGTAAGAGAC                   TTACTGCCGTCAGGCTCTAGAGATGAGCCTCCACCTGCCTCTCAGAGCACTAGCCAGG                   ACTGTTCACAGGCTTTAAAACAGAGCCCA TAA   AACTATGACCTCTGAGGTTTCATTGG                       AAAGAAAGTGTACTGTGCATTATCCATTACAGTAAAGGATTTCATTGGCTTCAAAATC                       CAAAAGTTTATTTTAAAAGGTTTGTTGTTAGAACTAAGCTGCCTTGGCAGTGTGCATT                       TTTGAGCCAAACAATTCAAAAATGTCATTTCTTCCCTAAATAAAAATCACCTTTT                                           ORF Start: ATG at 13   ORF Stop: TAA at 4786                                         SEQ ID NO: 66   1591 aa   MW at 178733.8 kD                             NOV24b,   MAAAPGLLVWLLVLRLPWRVPGQLDPSTGRRFSEHKLCADDECSVLMYRGEALEDFTG           CG133569-02       Protein Sequence   PDCRFVNFKKGDRVYVYYKLARGWPEVWAGSVGRTFGYPPKDLIQVVHEYTKEELQVP                   TDETDFVCFDGGRDDFHNYNVEELLGFLELYNSAATDSEKAVEKTLQDMEKNPELSKE                   REPEPEPVEANSEESDSVFSENTEDLQEQFTTQKHHSHANSQANHAQGEQASFESFEE                   MLQDKLKVPESENNKTSNSSQVSNEQDKIDAYKLLKKEMTLDLKTKFGSTADALVSDD                   ETTRLVTSLEDDFDEELDTEYYAVGKEDEENQEDFDELPLLTFTDGEDMKTPAKSGVE                   KYPTDKEQNSNEEDKVQLTVPPGIKNDDKNILTTWGDTIFSIVTGGEETRDTMDLESS                   SSEEEKEDDDDALVPDSKQGKPQSATDYSDPDNVDDGLFIVDIPKTNNDKEVNAEHHI                   KGKGRGVQESKRGLVQDKTELEDENQEGMTVHSSVHSNNLNSMPAAEKGKDTLKSAYD                   DTENDLKGAAIHISKGMLHEEKPGEQILEGGSESESAQKAAGNQMNDRKIQQESLGSA                   PLMGDDHPNASRDSVEGDALVNGAKLHTLSVEHQREELKEELVLKTQNQPRFSSPDEI                   DLPRELEDEVPILGRNLPWQQERDVAATASKQMSEKIRLSEGEAKEDSLDEEFFHHKA                   MQGTEVGQTDQTDSTGGPAFLSKVEEDDYPSEELLEDENAINAKRSKEKNPGNQGRQP                   DVNLQVPDRAVLGTIHPDPEIEESKQETSMILDSEKTSETAAKGVNTGGREPNTMVEK                   ERPLADKKAQRPFERSDFSDSIKIQTPELGEVFQNKDSDYLKNDNPEEHLKTSGLAGE                   PEGELSKEDHENTEKYMGTESQGSAAAEPEDDSFHWTPHTSVEPGHSDKREDLLIISS                   FFKEQQSLQRFQKYFNVHELEALLQEMSSKLKSAQQESLPYNMEKVLDKVFRASESQI                   LSIAEKMLDTRVAENRDLGMNENNIFEEAAVLDDIQDLIYFVRYKHSTAEETATLVMK                   PPLEEGLGGAMEEMQPLHEDNFSREKTAELNVQVPEEPTHLDQRVIGDTHASEVSQKP                   NTEKDLDPGPVTTEDTPMDAIDANKQPETAAEEPASVTPLENAILLIYSFMPYLTKSL                   VATLPDDVQPGPDFYGLPWKPVFITAFLGIASFAIFLWRTVLVVKDRVYQVTEQQISE                   KLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQ                   EILDDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNE                   AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE                   VALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ                   IKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTPPPFGPGMRPPLGLREFAPGVPPG                   RRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRLPPPTHGPQEYPPPPAVRDLLPS                   GSRDEPPPASQSTSQDCSQALKQSP                  
 
     [0458] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 24B.  
               TABLE 24B                          Comparison of NOV24a against NOV24b.                                         Identities/                   Similarities for           Protein   NOV24a Residues/   the Matched           Sequence   Match Residues   Region                       NOV24b   23 . . . 1484   1386/1462 (94%)               23 . . . 1484   1386/1462 (94%)                      
 
     [0459] Further analysis of the NOV24a protein yielded the following properties shown in Table 24C.  
               TABLE 24C                       Protein Sequence Properties NOV24a                                        PSort   0.4600 probability located in plasma membrane; 0.1080       analysis:   probability located in nucleus; 0.1000 probability located           in endoplasmic reticulum (membrane); 0.1000 probability           located in endoplasmic reticulum (lumen)       SignalP   Cleavage site between residues 23 and 24       analysis:                  
 
     [0460] A search of the NOV24a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 24D.  
               TABLE 24D                          Geneseq Results for NOV24a                                         NOV24a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAM25602   Human protein sequence SEQ ID   715 . . . 1907    1191/1193 (99%)    0.0           NO: 1117 -  Homo sapiens , 1193   1 . . . 1193   1193/1193 (99%)            aa. [WO200153455-A2, 26 JUL.           2001]       AAU32407   Novel human secreted protein   715 . . . 1907    1186/1194 (99%)    0.0           #2898 -  Homo sapiens , 1194 aa.   1 . . . 1194   1186/1194 (99%)            [WO200179449-A2, 25 OCT.           2001]       AAU29319   Human PRO polypeptide   1 . . . 492    489/492 (99%)   0.0           sequence #296 -  Homo sapiens ,   1 . . . 491    491/492 (99%)           499 aa. [WO200168848-A2, 20           SEP. 2001]       AAG73911   Human colon cancer antigen   1325 . . . 1798      474/474 (100%)   0.0           protein SEQ ID NO: 4675 -   1 . . . 474     474/474 (100%)             Homo sapiens , 487 aa.           [WO200122920-A2, 05 APR.           2001]       AAY70210   Human TANGO 130 protein -   1 . . . 410    409/410 (99%)   0.0             Homo sapiens , 410 aa.   1 . . . 410    410/410 (99%)           [WO200012762-A1, 09 MAR.           2000]                  
 
     [0461] In a BLAST search of public sequence datbases, the NOV24a protein was found to have homology to the proteins shown in the BLASTP data in Table 24E.  
               TABLE 24E                          Public BLASTP Results for NOV24a                                         NOV24a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q92580   KIAA0268 protein -  Homo sapiens      715 . . . 1907   1192/1193 (99%)    0.0           (Human), 1193 aa (fragment).     1 . . . 1193   1192/1193 (99%)        O15320   Meningioma-expressed antigen   1158 . . . 1871   233/790 (29%)   1e−71           6/11 (MEA6) (MEA11) -  Homo      20 . . . 783   381/790 (47%)             sapiens  (Human), 804 aa.       Q14083   C219-reactive peptide -  Homo     1306 . . . 1441    136/136 (100%)   9e−71             sapiens  (Human), 136 aa    1 . . . 136    136/136 (100%)           (fragment).       Q96SG9   BA500G10.2 (Novel protein   1158 . . . 1900   217/812 (26%)   1e−66           similar to meningioma expressed    34 . . . 822   371/812 (44%)           antigen 6 (MEA6) and 11           (MEA 11)) -  Homo sapiens             (Human), 825 aa (fragment).       O95046   WUGSC: H_DJ0988G15.3 protein   1160 . . . 1873   214/781 (27%)   2e−62           (DJ1005H11.2)    22 . . . 775   368/781 (46%)           (WUGSC: H_DJ0988G15.3           protein) -  Homo sapiens  (Human),           777 aa.                  
 
     [0462] PFam analysis indicates that the NOV24a protein contains the domains shown in the Table 24F.  
               TABLE 24F                          Domain Analysis of NOV24a                                             Identities/                       Similarities for           Pfam   NOV24a Match   the Matched   Expect           Domain   Region   Region   Value                       SH3   48 . . . 105   16/61 (26%)   0.026                   34/61 (56%)                      
 
     Example 25  
     [0463] The NOV25 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 25A.  
               TABLE 25A                       NOV25 Sequence Analysis                                                    SEQ ID NO: 67   1153 bp                             NOV25a,     ATG CTGCCGTGGCTTCTTGTCTTCTCTGCTCTGGGTCTCCAGGCCTGGGGTGATTCCT           CG133858-01       DNA Sequence   CCTGGAACAAAACACAAGCTAAACAGGTATCAGAGGGGCTCCAGTACCTATTTGAGAA                   CATCTCCCAGCTCACTCAAAAAGGCCTCCCCACAGATGTCTCCACCACGGTCTCCCGC                   AAGGCATGGGGGGCAGAAGCTGTTGGCTGCAGTATTCAGCTGACCACGCCAGTGAATC                   TCCTTGTTATACACCATGTCCCTGGACTGGAGTGTCACGACCAGACAGTCTGCAGCCA                   GAGACTGCGGGAACTGCAGGCCCATCATGTCCACAACAACAGTGGGTGTGATGTGGCC                   TACAACTTCCTGGTTGGGGATGATGGCAGGGTGTATGAAGGTGTTGGCTGGAATATCC                   AAGGAGTGCACACCCAAGGCTACAACAACATCTCCCTGGGCTTTGCCTTCTTCGGCAC                   TAAGAAAGGCCACAGTCCCAGCCCTGCTGCCCTGTCGGCCATGGAAAACCTAATCACC                   TATGCTGTCCAGAAGCGCCACCTGTCATCCAGTTATGTTCAGCCACTTCTTGTGAAAG                   GCGAGAACTGCCTGGCCCCTCGGCAGAAGACAAGCCTGAAGAAGGCTTGCCCCGGCGT                   TGTCCCACGGTCTGTGTGGGGAGCCAGGGAGACCCACTGTCCCAGGATGACTCTCCCA                   GCGAAGTATGGCATCATTATCCACACTGCCGGGAGGACCTGCAACATTTCTGATGAGT                   GCCGCCTGCTGGTCCGGGACATCCAGTCTTTCTACATAGACAGGCTCAAGTCATGCGA                   CATTGGTTATAACTTCCTGGTGGGCCAGGATGGCGCCATTTATGAAGGGGTGGGCTGC                   AATGTCCAAGGCTCCTCCACCCCTGGCTACGATGACATTGCCCTGGGCATTACCTTCA                   TGGGCACCTTCACAGGTATACCACCCAATGCTGCAGCACTAGAGGCAGCCCAAGACCT                   GATCCAGTGTGCCATGGTCAAAGGGTACCTGACTCCCAACTACCTGCTGGTGGGCCAC                   AGTGATGTGGCCCGAACCTTGTCTCCTGGGCAGGCTTTATACAACATCATCAGCACCT                   GGCCTCATTTCAAGCACTGTGGACAAGAAGCCACGGCAGCA TAA   GGGCGAT                                           ORF Start: ATG at 1   ORF Stop: TAA at 1144                                         SEQ ID NO: 68   381 aa   MW at 41393.7 kD                             NOV25a,   MLPWLLVFSALGLQAWGDSSWNKTQAKQVSEGLQYLFENISQLTEKGLPTDVSTTVSR           CG133858-01       Protein Sequence   KAWGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVA                   YNFLVGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLIT                   YAVQKGHLSSSYVQPLLVKGENCLAPRQKTSLKKACPGVVPRSVWGARETHCPRMTLP                   AKYGIIIHTAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVGW                   NVQGSSTPGYDDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGH                   SDVARTLSPGQALYNIISTWPHFKHCGQEATAA                  
 
     [0464] Further analysis of the NOV25a protein yielded the following properties shown in Table 25B.  
               TABLE 25B                       Protein Sequence Properties NOV25a                                        PSort   0.5500 probability located in lysosome (lumen); 0.3700       analysis:   probability located in outside; 0.1000 probability located           in endoplasmic reticulum (membrane); 0.1000 probability           located in endoplasmic reticulum (lumen)       SignalP   Cleavage site between residues 18 and 19       analysis:                  
 
     [0465] A search of the NOV25a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 25C.  
               TABLE 25C                          Geneseq Results for NOV25a                                         NOV25a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABB53272   Human polypeptide #12 -  Homo     1 . . . 373   368/373 (98%)   0.0             sapiens , 369 aa.   1 . . . 369   369/373 (98%)           [WO200181363-A1, 01 NOV.           2001]       AAE00693   Human full length granulocyte   1 . . . 373   368/373 (98%)   0.0           peptide homolog Zgpa1 protein #2 -   1 . . . 369   369/373 (98%)             Homo sapiens , 369 aa.           [WO200129224-A2, 26 APR. 2001]       AAE00692   Human full length granulocyte   1 . . . 373   370/375 (98%)   0.0           peptide homolog Zgpa1 protein #1 -   1 . . . 375   371/375 (98%)             Homo sapiens , 375 aa.           [WO200129224-A2, 26 APR. 2001]       AAY96963   Wound healing tissue peptidoglycan   1 . . . 373   349/373 (93%)   0.0           recognition protein-like protein -   1 . . . 368   352/373 (93%)             Homo sapiens , 368 aa.           [WO200039327-A1, 06 JUL. 2000]       ABB53271   Human polypeptide #11 -  Homo     153 . . . 373    217/221 (98%)   e−127             sapiens , 241 aa. [WO200181363-   21 . . . 241    218/221 (98%)           A1, 01 NOV. 2001]                  
 
     [0466] In a BLAST search of public sequence datbases, the NOV25a protein was found to have homology to the proteins shown in the BLASTP data in Table 25D.  
               TABLE 25D                          Public BLASTP Results for NOV25a                                         NOV25a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q96LB8   Peptidoglycan recognition   1 . . . 373    373/373 (100%)   0.0           protein-I-beta precursor -  Homo     1 . . . 373    373/373 (100%)             sapiens  (Human), 373 aa.       CAC38715   Sequence 7 from Patent   1 . . . 373   368/373 (98%)   0.0           WO0129224 -  Homo sapiens     1 . . . 369   369/373 (98%)           (Human), 369 aa.       CAC38714   Sequence 4 from Patent   1 . . . 373   370/375 (98%)   0.0           WO0129224 -  Homo sapiens     1 . . . 375   371/375 (98%)           (Human), 375 aa.       Q9HD75   Hypothetical 40.0 kDa protein -   1 . . . 373   349/373 (93%)   0.0             Homo sapiens  (Human), 368 aa.   1 . . . 368   352/373 (93%)       Q96LB9   Peptidoglycan recognition   2 . . . 373   231/372 (62%)   e−136           protein-I-alpha precursor -  Homo     4 . . . 341   268/372 (71%)             sapiens  (Human), 341 aa.                  
 
     [0467] PFam analysis indicates that the NOV25a protein contains the domains shown in the Table 25E.  
               TABLE 25E                          Domain Analysis of NOV25a                                             Identities/                       Similarities           Pfam   NOV25a Match   for the   Expect           Domain   Region   Matched Region   Value                             No Significant Matches Found                  
 
     Example 26  
     [0468] The NOV26 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 26A.  
               TABLE 26A                       NOV26 Sequence Analysis                                                    SEQ ID NO: 69   1182 bp                             NOV26a,      GTCCTGGGACCACATGGGGACGCTGCC ATGGCTTCTTGCCTTCTTCATTCTGGGTCTC           CG134100-01        DNA Sequence    CAGGCTTGGGGTTCTCCTGGAGTGAGACCCAAGCCAGAGCCTTGTCCCAGAGGCTTAT                   GGACCTGTTTGTCAGCATCTCACAGTTCATTCACAAGGGTCGCAATGATACTCCCACC                   ATCGTCTCCCGCAAGGAGTGGGGGGCAAGACCGCTCGCCTGCAGGGCCCTGCTGACCC                   TGCCTGTGGCCTACATCATCACAGACCAGCTCCCAGGGATGCAGTGCCAGCAGCAGAG                   CGTTTGCAGCCAGATGCTGCGGGGGTTGCAGTCCCATTCCGTCTACACCATAGGCTGG                   TGCGACGTGGCCTACAACTTCCTGGTTGGGGATGATGGCAGGGTGTATGAAGGTGTTG                   GCTGGAACATCCAAGGCTTGCACACCCAGGGCTACAACAACATTTCCCTGGGCATCGC                   CTTCTTTGGCAATAAGATAAGCAGCAGTCCCAGCCCTGCTGCCTTATCAGCTGCAGAG                   GGTCTGATCTCCTATGCCATCCAGAAGGGTCACCTGTCGCCCAGGTATATTCAGCCAC                   TTCTTCTGAAAGAAGAGACCTGCCTGGACCCTCAACATCCAGTGATGCCCAGGAAGGT                   TTGCCCCAACATCATCAAACGATCTGCTTGGGAAGCCAGAGAGACACACTGCCCTAAA                   ATGAACCTCCCAGCCAAATATGTCATCATCATCCACACCGCTGGCACAAGCTGCACTG                   TATCCACAGACTGCCAGACTGTCGTCCGAAACATACAGTCCTTTCACATGGACACACG                   GAACTTTTGTGACATTGGATATCACTTCCTGGTGGGCCAGGATGGTGGCGTGTATGAA                   GGGGTTGGATGGCACATCCAAGGCTCTCACACTTATGGATTCAACGATATTGCCCTAG                   GAATTGCCTTCATCGGCTACTTTGTAGAAAAGCCTCCAAATGCTGCAGCGCTGGAGGC                   GGCCCAGGACCTGATCCAGTGTGCCGTGGTTGAGGGGTACCTGACTCCAAACTACCTG                   CTGATGGGCCACAGTGACGTGGTCAACATCCTGTCCCCTGGGCAGGCTTTGTATAACA                   TCATCAGCACCTGGCCTCATTTCAAGCACTGA AGGAGGCCCCACTCCCTTTGAGACT G                     CCCTCCCTCCCCTGCTGGGTCT                                           ORF Start: ATG at 28   ORF Stop: TGA at 1132                                         SEQ ID NO: 70   368 aa   MW at 40515.0kD                             NOV26a,    MASCLLHSGSPGLGFSWSETQARGLSQRLMDLFVSISQFIHKGRNDTPTIVSRKEWGA           CG134100-01        Protein Sequence    RPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTIGWCDVAYNFLV                   GDDGRVYEGVGWNIQGLHTQGYNNISLGIAFFGNKISSSPSPAALSAAECLISYAIQK                   GHLSPRYIQPLLLKEETCLDPQHPVMPRKVCPNIIKRSAWEARETHCPKMNLPAKYVI                   IIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGS                   HTYGFNDIALGIAFIGYFVEKRPNAAALEAAQDLIQCAVVEGYLTPNYLLMGHSDVVN                   ILSPGQALYNIISTWPHFKH                                         SEQ ID NO: 71   1087 bp                             NOV26b,      GTCCTGGGACCAC ATGGGGACGCTGCCATGGCTTCTTOCCTTCTTCATTCTGGGTCTC           CG134100-02        DNA Sequence    CAGGCTTGGGATACTCCCACCATCGTCTCCCGCAAGGAGTGGGGGGCAAGACCGCTCG                   CCTGCAGGGCCCTGCTGACCCTGCCTGTGGCCTACATCATCACAGACCAGCTCCCAGG                   GATGCAGTGCCAGCAGCAGAGCOTTTGCAGCCAGATGCTGCCGGGGTTGCAGTCCCAT                   TCCGTCTACACCATAGGCTGGTGCGACGTGGCGTACAACTTCCTGGTTGGGGATGATG                   GCAGGGTGTATGAAGGTGTTGGCTGGAACATCCAAGGCTTGCACACCCAGGGCTACAA                   CAACATTTCCCTGGGCATCGCCTTCTTTGGCAATAAGATAAGCAGCAGTCCCAGCCCT                   GCTGCCTTATCAGCTGCAGAGGGTCTGATCTCCTATGCCATCCAGAAGGGTCACCTGT                   CGCCCAGGTATATTCAGCCACTTCTTCTGAAAGAAGAGACCTGCCTGGACCCTCAACA                   TCCAGTGATGCCCAGGAAGGTTTGCCCCAACATCATCAAACGATCTGCTTGGGAAGCC                   AGAGAGACACACTGCCCTAAAATGAACCTCCCAGCCAAATATGTCATCATCATCCACA                   CCGCTGGCACAAGCTGCACTGTATCCACAGACTGCCAGACTGTCGTCCGAAACATACA                   GTCCTTTCACATCGACACACGGAACTTTTGTGACATTGGATATCACTTCCTGGTGGGC                   CAGGATGGTGGCGTGTATGAAGGGGTTGGATGGCACATCCAACGCTCTCACACTTATG                   GATTCAACGATATTGCCCTAGGAATTGCCTTCATCGGCTACTTTGTAGAAAAGCCTCC                   AAATGCTGCAGCGCTGGAGGCGGCCCAGGACCTGATCCAGTGTGCCGTGGTTGAGGGG                   TACCTGACTCCAAACTACCTGCTGATGGGCCACAGTGACGTGGTCAACATCCTGTCCC                   CTGGGCACGCTTTGTATAACATCATCAGCACCTGGCCTCATTTCAAGCACTGA AGGAC                       GCCCCACTCCCTTTGAGACTGCCCTCCCTCCCCTGCTGGGTCT                                           ORF Start: ATG at 14   ORF Stop: TGA at 1037                                         SEQ ID NO: 72   341 aa   MW at 37640.9kD                             NOV26b,    MGTLPWLLAFFILGLQAWDTPTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQ           CG134100-02        Protein Sequence    QQSVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISL                   GIAFFGNKISSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLLLKEETCLDPQHPVMP                   RKVCPNIIKRSAWEARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHM                   DTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAA                   LEAAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPGQALYNIISTWPHFKH                  
 
     [0469] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 26B.  
               TABLE 26B                          Comparison of NOV26a against NOV26b.                                         Identities/           Protein   NOV26a Residues/   Similarities for           Sequence   Match Residues   the Matched Region                       NOV26b   46 . . . 368   299/323 (92%)               19 . . . 341   299/323 (92%)                      
 
     [0470] Further analysis of the NOV26a protein yielded the following properties shown in Table 26C.  
               TABLE 26C                       Protein Sequence Properties NOV26a                                                PSort   0.4500 probability located in cytoplasm;           analysis:   0.3239 probability located in microbody               (peroxisome); 0.2643 probability               located in lysosome (lumen); 0.1000               probability located in mitochondrial               matrix space           SignalP   No Known Signal Sequence Indicated           analysis:                      
 
     [0471] A search of the NOV26a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 26D.  
               TABLE 26D                          Geneseq Results for NOV26a                                         NOV26a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAE00692   Human full length granulocyte   16 . . . 368   231/356 (64%)   e−139           peptide homolog Zgpa1 protein #1 -   20 . . . 375   276/356 (76%)             Homo sapiens , 375 aa.           [WO200129224-A2, 26 APR.           2001]       ABB53272   Human polypeptide #12 -  Homo     16 . . . 368   230/353 (65%)   e−138             sapiens , 369 aa. [WO200181363-   20 . . . 369   274/353 (77%)           A1, 01 NOV. 2001]       AAE00693   Human full length granulocyte   16 . . . 368   230/353 (65%)   e−138           peptide homolog Zgpa1 protein #2 -   20 . . . 369   274/353 (77%)             Homo sapiens , 369 aa.           [WO200129224-A2, 26 APR.           2001]       AAY76124   Human secreted protein encoded by   46 . . . 269    224/224 (100%)   e−133           gene 1 -  Homo sapiens , 244 aa.   19 . . . 242    224/224 (100%)           [WO9958660-A1, 18 NOV. 1999]       AAY96962   Keratinocyte peptidoglycan   46 . . . 269    224/224 (100%)   e−133           recognition protein-like protein -   19 . . . 242    224/224 (100%)             Homo sapiens , 243 aa.           [WO200039327-A1, 06 JUL. 2000]                  
 
     [0472] In a BLAST search of public sequence datbases, the NOV26a protein was found to have homology to the proteins shown in the BLASTP data in Table 26E.  
               TABLE 26E                          Public BLASTP Results for NOV26a                                         NOV26a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q96LB9   Peptidoglycan recognition   46 . . . 368   322/323 (99%)   0.0           protein-I-alpha precursor -  Homo     19 . . . 341   322/323 (99%)             sapiens  (Human), 341 aa.       Q96LB8   Peptidoglycan recognition   16 . . . 368   232/354 (65%)   e-139           protein-I-beta precursor -  Homo     20 . . . 373   275/354 (77%)             sapiens  (Human), 373 aa.       CAC38714   Sequence 4 from Patent   16 . . . 368   231/356 (64%)   e-138           WO0129224 -  Homo sapiens     20 . . . 375   276/356 (76%)           (Human), 375 aa.       CAC38715   Sequence 7 from Patent   16 . . . 368   230/353 (65%)   e-138           WO0129224 -  Homo sapiens     20 . . . 369   274/353 (77%)           (Human), 369 aa.       Q9HD75   Hypothetical 40.0 kDa protein -   16 . . . 368   221/353 (62%)   e-126             Homo sapiens  (Human), 368 aa.   20 . . . 368   263/353 (73%)                  
 
     [0473] PFam analysis indicates that the NOV26a protein contains the domains shown in the Table 26F.  
               TABLE 26F                          Domain Analysis of NOV26a                                             Identities/                       Similarities for           Pfam   NOV26a Match   the Matched   Expect           Domain   Region   Region   Value                             No Significant Matches Found                  
 
     Example 27  
     [0474] The NOV27 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 27A.  
               TABLE 27A                       NOV27 Sequence Analysis                                                    SEQ ID NO:73   2195 bp                             NOV27a,     TTTGTTCCTAACAGATTTCTTGCGACAAGGAAACCCGCAGTCTTCCGCTTCCGGTTGC             CG134403-01       DNA Sequence     TCTGTTGCCATACTAACCCCACCCATAACAGCCGTGGTGGTT   ATG GCTGGCCTGAGCG                   GCGCGCAGATCCCCGACGGGGAGTTCACCGCGGTCGTGTACCGCCTCATCCGCAATGC                   ACGCTACGCCGAGGCGGTGCAGCTGCTGGGCGGAGAACTGCACCGGAGCCCTAGGAGC                   CGCGCCGGCCTGTCGCTGCTAGGCTACTGCTACTACCGCCTGCAGGAGTTCGCGCTGG                   CGGCCGAGTGCTATGAGCAGCTGGGCCAGCTGCACCCGGAACTGGAGCAGTACCGCCT                   GTACCAGGCCCAGGCCCTGTACAAGGCCTGCCTTTATGCGGAGGCCACCCGGGTCGCC                   TTCCTTCTCCTGGATAACCCCGCCTACCACAGCCGGGTCCTCCGCCTGCAAGCTGCTA                   TCAAGTACAGCGAGGGCGATCTGCCAGGGTCCAGGAGCCTGGTAGAGCAGCTGCCGAG                   TAGGGAAGGGGGAGAGGAPAGTGGGGCCGAGAATCAGACCGATGGCCAGATCAACCTG                   GGTTGTTTGCTCTACAAGGAGGGACAGTATGAAGCTGCATGCTCCAAGTTTTTTGCCG                   CCCTGCAGGCCTCCGGCTACCAGCCTGACCTTTCCTACAACCTGGCTTTGGCCTATTA                   CAGCAGCCGACACTATCCTTCAGCACTGAAGCATATCGCTGAGATTATTGAGCGTGGC                   ATCCGCCAGCACCCTGAGCTAGGTGTCGGCATGACCACTGAGGGCATTGATGTTCGCA                   GTGTTCGCAACACCTTAGTCCTCCATCAGACTGCTCTGGTGGAAGCCTTCAACCTTAA                   GGCAGCTATAGAATACCAACTGAGAAACTATGAGGCAGCTCAAGAAGCCCTCACTCAC                   ATGCCACCCAGGGCAGAGGAAGAGTTGGACCCTGTGACCCTACACAACCAGGCACTAA                   TGAACATGGATGCCAGGCCTACAGAAGGGTTTGAAAAGCTACACTTTTTGCTCCAACA                   GAATCCCTTTCCTCCAGAGACTTTTGGCAACCTGTTGCTGCTCTACTGTAAATATGAG                   TATTTTGACCTGCCAGCAGATGTCCTGGCACAAAATGCCCATTTGATTTATAAGTTCC                   TCACACCCTATCTCTATGACTTCTTGGACGCTGTGATCACTTGCCAGACAGCTCCTGA                   AGAGGCTTTCATTAACCTTGATGGGCTAGCAGGGATGCTGACTGACCTCCTCCGGAAA                   CTTACCATACAAGTACAGGAAGCAAGACACAATAGAGATGATGAAGCTATCAAAAAGG                   CAGTGAATGAATATGATGAAACCATGGAGAAATACATTCCTGTGTTGATGGCTCAGGC                   AAAAATCTACTGGAATCTTGAAAATTATCCAATGGTGGAAAAGATCTTCCGCAAATCT                   GTGGAATTCTGTAACGACCATGATGTGTGGAAGTTGAATGTGGCTCATGTTCTGTTCA                   TGCAGGAAAACAAATACAAGAAGCCATTGGTTTCTATGAACCCATAGTCAAGAAAACA                   TTATGATAACATCCTCAATGTCAGTGCTATTGTACTGGCTAATCTCTGTGTTTCCTAT                   ATTATGACAAGTCAAAATGAAGAXGCAGAGGAGTTGATGAGGAAGATTGAAAAGGAGG                   AAGAGCAGCTCTCTTATGATGACCCAGATAAGAAAATGTACCATCTCTGCATTGTGAA                   TTTGGTGATACGAACTCTTTATTGTGCCAAAGGAAATTATGACTTTGGTATTTCTCGA                   GTTATCAAAAGCTTGGAACCTTACAACAAAAAGCTGGGAACAGACACCTGGTATTATG                   CCAAAAGATGCTTCCTGTCCTTGTTAGAAAACATGTCAAAACACACAATCATGCTTCG                   TCATAGTGTTATTCAAGAATGTGTCCAGTTTCTAGAACACTGTGAACTTCATCGCAGA                   AACATACCTGCTGTTATTGAACAACCCCTGGAAGAAGAAAGAATGCATGTTGGAAAGA                   ATACAGTCACATATGAGTCTAGGCAGTTAAAAGCTTTCATTTATGAGATTATAGGATC                   GAATATATAGTAA TAG   CTGATAGTGGCATTTATCAAATGGCTTTCTTATGTAAATTTG                       CATCGCTTTATTTACCCTTTGGCATCTTTATATTTGTTACATGTTGAAC                                           ORF Start: ATG at 101 ORF   Stop: TAG at 2096                                         SEQ ID NO: 74   665 aa   MW at 76098.0 kD                             NOV27a,   MAGLSGAQIPDGEFTAVVYRLIRNARYAEAVQLLGGELQRSPRSRAGLSLLGYCYYRL           CG134403-01       Protein Sequence   QEFALAAECYEQLGQLHPELEQYRLYQAQALYKACLYAEATRVAFLLLDNPAYHSRVL                   RLQAAIKYSEGDLPGSRSLVEQLPSREGGEESGGENETDGQINLGCLLYKEGQYEAAC                   SKFFAALQASCYQPDLSYNLALAYYSSRQYASALKHIAEIIERGIRQHPELGVGMTTE                   GIDVRSVGNTLVLHQTALVEAFNLKAAIEYQLRNYEAAQEALTDMPPRAEEELDPVTL                   HNQALMNMDARPTEGFEKLQFLLQQNPFPPETFGNLLLLYCKYEYFDLAADVLAENAH                   LIYKFLTPYLYDFLDAVITCQTAPEEAFIKLDGLAGMLTEVLRKLTIQVQEARHNRDD                   EAIKKAVNEYDETMEKYIPVLMAQAKIYWNLENYPMVEKIPRKSVEFCNDHDVWKLNV                   AHVLPMQENKYKEATGFYEPIVKKHYDNILNVSAIVLANLCVSYIMTSQNEEAEELMR                   KIEKEEEQLSYDDPDKKMYHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYNKKLGT                   DTWYYAKRCFLSLLENMSKHTIMLRDSVIQECVQFLEHCELHGRNIPAVIEQPLEEER                   MHVGKNTVTYESRQLKALIYEIIGWNI                  
 
     [0475] Further analysis of the NOV27a protein yielded the following properties shown in Table 27B.  
               TABLE 27B                       Protein Sequence Properties NOV27a                                                PSort   0.8500 probability located in endoplasmic           analysis:   reticulum (membrane); 0.6640 probability               located in plasma membrane; 0.3000               probability located in microbody               (peroxisome); 0.1000 probability located               in mitochondrial inner membrane           SignalP   No Known Signal Sequence Indicated           analysis:                      
 
     [0476] A search of the NOV27a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 27C.  
               TABLE 27C                          Geneseq Results for NOV27a                                         NOV27a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAM39821   Human polypeptide SEQ ID NO    1 . . . 640   636/640 (99%)   0.0           2966 -  Homo sapiens , 843 aa.   60 . . . 699   637/640 (99%)           [WO200153312-A1, 26 JUL. 2001]       AAM41607   Human polypeptide SEQ ID NO   356 . . . 664    293/309 (94%)   e−173           6538 -  Homo sapiens , 310 aa.    1 . . . 309   302/309 (96%)           [WO200153312-A1, 26 JUL. 2001]       ABB61288     Drosophila melanogaster     22 . . . 660   301/648 (46%)   e−157           polypeptide SEQ ID NO 10656 -   18 . . . 646   424/648 (64%)             Drosophila melanogaster , 652 aa.           [WO200171042-A2, 27 SEP. 2001]       AAB94836   Human protein sequence SEQ ID   385 . . . 664    266/280 (95%)   e−156           NO: 16004 -  Homo sapiens , 281 aa.    1 . . . 280   273/280 (97%)           [EP1074617-A2, 07 FEB. 2001]       ABB48602     Listeria monocytogenes  protein   59 . . . 317    57/260 (21%)   2e−04            #1306 -  Listeria monocytogenes ,   14 . . . 237   102/260 (38%)           417 aa. [WO200177335-A2, 18           OCT. 2001]                  
 
     [0477] In a BLAST search of public sequence datbases, the NOV27a protein was found to have homology to the proteins shown in the BLASTP data in Table 27D.  
               TABLE 27D                          Public BLASTP Results for NOV27a                                         NOV27a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q96NE6   CDNA FLJ30990 fis, clone   1 . . . 665   635/665 (95%)   0.0           HLUNG1000037 -  Homo sapiens     1 . . . 638   635/665 (95%)           (Human), 638 aa.       Q9CY00   2510042P03Rik protein -  Mus     1 . . . 665   615/665 (92%)   0.0             musculus  (Mouse), 664 aa.   1 . . . 664   642/665 (96%)       Q99J38   Similar to RIKEN cDNA   1 . . . 665   598/665 (89%)   0.0           2510042P03 gene -  Mus musculus     1 . . . 664   632/665 (94%)           (Mouse), 664 aa.       Q9D2H0   4930506L13Rik protein -  Mus     1 . . . 617   558/617 (90%)   0.0             musculus  (Mouse), 616 aa.   1 . . . 616   586/617 (94%)       Q9VK41   CG5142 protein -  Drosophila     22 . . . 660    301/648 (46%)   e−157             melanogaster  (Fruit fly), 652 aa.   18 . . . 646    424/648 (64%)                  
 
     [0478] PFam analysis indicates that the NOV27a protein contains the domains shown in the Table 27E.  
               TABLE 27E                          Domain Analysis of NOV27a                                             Identities/                       Similarities for           Pfam   NOV27a Match   the Matched   Expect           Domain   Region   Region   Value                       TPR   45 . . . 78   10/34 (29%)   0.97                   22/34 (65%)                      
 
     Example 28  
     [0479] The NOV28 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 28A.  
               TABLE 28A                       NOV28 Sequence Analysis                                                    SEQ ID NO:75   1165 bp                             NOV28a,   CCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCATCCTAGTCCTG           CG135049-01       DNA Sequence   TGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCTCTGCTCTCCC                   GGGGCTCCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGCGGGATATTAA                   CAAAGACAGAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAAACCACGCCCAGGAA                   TACAGACGGGGTGGCCTGGGATCTCTGTTCTATCTTACACTGGATGTGCTAGAGACTG                   ACTGCCATGTGCTCAGAAAGAAGGCATGGCAAGACTGTGGAATGAGGATATTTTTTGA                   ATCAGTTTATGGTCAATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTC                   TATTTAGCTGCTTATAACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGA                   CGTGCCCGGACTGCCCAGGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGA                   GGCTGCCACCGAGTCTCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCT                   CTCTTCAAAGTCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTGTGGG                   AATACTTAATTAAAGAATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCA                   GTCCTCCGACTCTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGG                   GAAAAGTTTGTCTCTGTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAA                   GTGAAAACTCTGCTGTTAACCAGAAACCTACAAACCTTCCCAAGGTGGAAGAATCCCA                   GCAGAAAAACACCCCCCCAACAGACTCCCCCTCCAAAGCTGGGCCAAGAGGATCTGTC                   CAATATCTTCCTGACTTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCT                   TTCCTGTGCATCTGGACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTT                   CCTCTTCCTGGAGCCTATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAA                   GCACGCACTGCTGAGTGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGC                   CA TGA                                           ORF Start: ATG at 17   ORF Stop: TGA at 1163                                         SEQ ID NO: 76   382 aa   MW at 42077.4 kD                             NOV28a,   MGLLLPLALCILVLCCGAMSPRQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD           CG135049-01       Protein Sequence   GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLETDCHVLRKKAWQDCGMRIFFESVYGQ                   CKAIFYMNNPSRVLYLAAYNCTLRPVSKKKIYMTCPDCPGSIPTDSSNHQVLEAATES                   LAKYNNENTSKQYSLFKVTPASSQWVVGPSYLWEYLIKESPCTKSQASSCSLQSSDSV                   PVGLCKGSLTRTHWEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTP                   PTDSPSKAGPRGSVQYLPDLDDKNSQEKGPQEAFPVHLDLTTNPQGETLDISFLFLEP                   MEEKLVVLPFPKEKARTAECPGPAQNASPLVLPP                                         SEQ ID NO: 77   1303 bp                             NOV28b,     GTAACAAAACCGCTCAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAG             CG135049-02       DNA Sequence     CTCCACAAACTGACCCATCCTGGGCCTTGTTCTCCACAGA   ATG GGTCTGCTCCTTCCC                   CTGGCACTCTGCATCCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCAA                   TCAACCCCTCGGCTCTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGC                   AGGCTTTGCCCTGCGGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTC                   AACCGAGTGAACGACGCCCAGGAATACAGACCGGGTGGCCTGGGATCTCTGTTCTATC                   TTACACTGGATGTGCTAGACTGTGGAATGAGGATATTTTTTGAATCAGTTTATGGTCA                   ATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTCTATTTAGCTGCTTAT                   AACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGACGTGCCCTGACTGCC                   CAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACCGAGTC                   TCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCTCTCTTCAAAGTCACC                   AGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTGGAATACTTAATTAAAG                   AATCACCATCTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGACTCTGT                   GCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTGTCTCT                   GTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTCTGCTG                   TTAACCAGAAACCTACAAACCTTCCCAAGGTGGAAGAATCCCAGCAGAAAAACACCCC                   CCCAACACACTCCCCCTCCAAAGCTGGGCCAAGAGGATCTGTCCAATATCTTCCTGAC                   TTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCATCTGG                   ACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTGGAGCC                   TATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTGCTGAG                   TGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCA TGA   GAATCACACA                       GAGTCTTCTGTAGGGGTATGGTGCGCCGCATGACATGGGAGGCGATGCGGACGATGGA                       CAGAGACAGAGCGTGCACACGTAGAGT                                           ORF Start: ATG at 99   ORF Stop: TGA at 1206                                         SEQ ID NO: 78   369 aa   MW at 40458.6 kD                             NOV28b,   MGLLLPLALCILVLCCGAIVISPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD           CG135049-02       Protein Sequence   GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLDCGMRIFFESVYGQCKAIFYMNNPSRVAA                   LYLAAYNCTLRPVSKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYNNENTSKQYAA                   SLFKVTRASSQWVVGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTH                   WEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGS                   VQYLPDLDDKNSQEKGPQEAFPVHLDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKE                   KARTAECPGPAQNASPLVLPP                                         SEQ ID NO: 79   1970 bp                             NOV28c     GTAACAAAACCGCTCAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAG             CG135049-03       DNA Sequence     CTCCACAAACTGACCCATCCTGGGCCTTGTTCTCCACAGA   ATG GGTCTGCTCCTTCCC                   CTGGCACTCTGCATCCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCC                   TCAACCCCTCGGCTCTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGC                   AGGCTTTGCCCTGCGGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTC                   AACCGAGTGAACGACGCCCAGGAATACAGACGGGGTGGCCTGGGATCTCTGTTCTATC                   TTACACTGGATGTGCTAGACTGTGGAATGAGGATATTTTTTGAATCAGTTTATGGTCA                   ATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTCTATTTAGCTGCTTAT                   AACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGACGTGCCCTGACTGCC                   CAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACCGAGTC                   TCTTGCGAAATACAACAATGAGAACACATCCAAAGCAGTATTCTCTCTTCAAGTCACC                   AGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTGGAATACTTAATTAAAG                   AATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGACTCTGT                   GCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTGTCTCT                   GTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTCTGCTG                   TTAACCAGAAACCTACAAACCTTCCCAAGGTGGAAGAATCCCAGCAGAAAAATACCCC                   CCCAACAGACTCCCCCTCCAAACCTGGGCCAAGAGGATCTGTCCAATATCTTCCTGAC                   TTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCATCTGG                   ACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTGGAGCC                   TATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTGCTGAG                   TGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCATGAGAATCACACA                     GAGTCTTCTCTAGGGGTATGGTGCGCCGCATGACATGGGAGGCGATGGGGACGATGGA                       CAGAGACAGAGCGTGCACACGTAGAGTACCAGGGGAAGGAGCAGACCCATCCTGGGCC                       TTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCATCCTAGTCCTGTG                       CTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCTCTGCTCTCCCCG                       GGCTGCAATCACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGGCGGGATATTAAC                       AAAGACAGAAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAACGACGCCCAGGAAT                       ACAGACGGGGTGGCCTGGGATCTCTGTTCTATCTTACACTGGATGTGCTAGAGACTGA                       CTGCCATGTGCTCAGAAAGAAGGCATGGCAAGACTGTGGAATGAGGATATTTTTTGAA                       TCAGTTTATGGTCAATGCAAAGCAATATTTTATATGAACAACCCAAGTAGAGTTCTCT                       ATTTAGCTGCTTATAACTGTACTCTTCGCCCAGTTTCAAAAAAAAAGATTTACATGAC                       GTGCCCTGACTGCCCAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAG                       GCTGCCACCGAGTCTCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCTC                       TCTTCAAAGTCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTGTGG                                           ORF Start: ATG at 99   ORF Stop: TGA at 1206                                         SEQ ID NO:80   1369 aa   MW at 40458.6 kD                             NOV28c,   MCLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD           CG135049-03       Protein Sequence   GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLDCGMRIFFESVYGQCKAIFYMNNPSRV                   LYLAAYNCTLRPVSKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYHNENTSKQY                   SLFKVTRASSQWVVGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTH                   WEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGS                   VQYLPDLDDKNSQEKGPQEAFPVHLDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKE                   KARTAECPGPAQNASPLVLPP                                         SEQ ID NO:81   1427 bp                             NOV28d,   AAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAGCTCCACiAACTGAC           CG135049-04       DNA Sequence   CCATCCTGGGCCTTGTTCTCCACAGAATGGGTCTGCTCCTTCCCCTGGCACTCTGCAT                   CCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCT                   CTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGC                   GGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAACGA                   CGCCCAGGAATACAGACGGGCAATTTCAAAAAAAAAGATTTACATGACGTGCCCTGAC                   TGCCCAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACCG                   AGTCTCTTGCGAAATACAACAATGAGAACACATCCAAGCAGTATTCTCTCTTCAAAGT                   CACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTGGAATACTTAATT                   AAAGAATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGACT                   CTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTGT                   CTCTGTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTCT                   GCTGTTAACCAGAAACCTACAACCTTCCCAAGGTGGAAAGAATCCCAGCAGAAAAACA                   CCCCCCCAACAGACTCCCCCTCCkAAGCTGGGCCAAGACGATCTGTCCAATATCTTCC                   TGACTTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCAT                   CTGGACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTGG                   AGCCTATGGAGGAGAAGCTGGTCGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTGC                   TGAGTGCCCACGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCA TGA   GAATCA                       CACAGAGTCTTCTGTAGGGGTATGGTGCGCCGCATGACATCGGAGGCGATGGGGACGA                       TGGACAGAGACAGAGCGTGCACACGTAGAGTGGCTAGTGAAGGACCCCTTTTTGACTC                       TTCTTGGTCTCAGCATGTTGACTGGGATTGGAAATAATGAGACTGAGCCCTCGGCTTG                       GGCTGCACTCTACCCT2TACACTGCCTTGTACCCTGAGCTGCATCACCTCCTAAACTG                       AGCAGTCTCATACCATGGAGAGATGCCTCTCTTATGTCTTCAGCCACTCACTTATAAA                       GATACTTATCTTTTCAGCAGTATATATGTGCTGAAATCTCAGCATGAAAGCATTGCAT                       GAGTAAGATACTTTCCCTAAAAAAAAAAAAAAAAA                                           ORF Start: ATG at 85   ORF Stop: TGA at 1036                                         SEQ ID NO: 82   317 aa   MW at 34555.7 kD                             NOV28d,   MGLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD           CG135049-04       Protein Sequence   GYVLRLNRVNDAQEYRRAISKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYNNE                   NTSKQYSLFKVTRASSQWVVGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKG                   SLTRTHWEKFVSVTCDFFESQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSK                   AGPRGSVQYLPDLDDKNSQEKGPQEAFPVHLDLTThPQGETLDISFLFLEPMEEKLVV                   LPFPKEKARTAECPGPAQNASPLVLPP                                         SEQ ID NO: 83   1544 bp                             NOV28e,     AAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAGCTCCACAAACTGAC             CG135049-05       DNA Sequence     CCATCCTGGGCCTTGTTCTCCACAGA   ATG GGTCTGCTCCTTCCCCTGGCACTCTGCAT                   CCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTCGCCCTCAACCCCTCGGCT                   CTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGC                   GGGATATTAACAAAGACAGAAAGGATGGCTATCTGCTGAGACTCAACCGAGTGAACGA                   CGCCCAGGAATACAGACGGGGTGGCCTGGGATCTCTGTTCTATCTTACACTGGATGTG                   CTAGAGACTGACTGCCATGTGCTCAGAAAGAAGGCATGGCAAGACTGTGGAATGAGGA                   TATTTTTTGAATCAGCATCAACAGTTTCAAAAAAAAAGATTTACATGACGTGCCCTGA                   CTGCCCAAGCTCCATACCCACTGACTCTTCCAATCACCAAGTGCTGGAGGCTGCCACC                   GAGTCTCTTGCGAAATACAACATGAGAACACATCCAAGCAGTATTCTCTCTTCAAAAG                   TCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCCCTTCTTACTTTGTCGAATACTTAAT                   TAAAGAATCACCATGTACTAAATCCCAGGCCAGCAGCTGTTCACTTCAGTCCTCCGAC                   TCTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTGACTCGAACACACTGGGAAAAGTTTG                   TCTCTGTGACTTGTGACTTCTTTGAATCACAGGCTCCAGCCACTGGAAGTGAAAACTC                   TGCTGTTAACCAGAAACCTACAAACCTTCCCkAGGTGGAAGAATCCCAGCAGAAAAAC                   ACCCCCCCAACAGACTCCCCCTCCAAAGCTGGGCCAAGAGGATCTGTCCAATATCTTC                   CTGACTTGGATGATAAAAATTCCCAGGAAAAGGGCCCTCAGGAGGCCTTTCCTGTGCA                   TCTGGACCTAACCACGAATCCCCAGGGAGAAACCCTGGATATTTCCTTCCTCTTCCTG                   GAGCCTATGGAGGAGAAGCTGGTGGTCCTGCCTTTCCCCAAAGAAAAAGCACGCACTG                   CTGAGTGCCCAGGGCCAGCCCAGAATGCCAGCCCTCTTGTCCTTCCGCCA TGA   GAATC                       ACACAGAGTCTTCTGTAGGGGTATGGTGCGCCGCATGACATGGGAGGCGATGGGGACG                       ATGGACAGAGACAGAGCGTGCACACGTAGAGTGGCTAGTGAAGGACGCCTTTTTGACT                       CTTCTTGGTCTCAGCATGTTGACTGGGATTGGAAATAATGAGACTGAGCCCTCGGCTT                       GGGCTGCACTCTACCCTGTACACTGCCTTGTACCCTGAGCTGCATCACCTCCTAAACT                       GAGCAGTCTCATACCATGGAGAGATGCCTCTCTTATGTCTTCAGCCACTCACTTATAA                       AGATACTTATCTTTTCAGCAGTATATATGTGCTGAAATCTCAGCATGAAAGCATTGCA                       TGAGTAAAGATACTTTCCCTAAAAAAAAAAAAAAAA                                           ORF Start: ATG at 85   ORF Stop: TGA at 1153                                         SEQ ID NO: 84   356 aa   MW at 38961.8 kD                             NOV28e,   MGLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD           CG135049-05       Protein Sequence   GYVLRLNRVNDAQEYRRGGLGSLFYLTLDVLETDCHVLRKKAWQDCGMRIFPESASTV                   SKKKIYMTCPDCPSSIPTDSSNHQVLEAATESLAKYNNENTSKQYSLFKVTRASSQWV                   VGPSYFVEYLIKESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTHWEKFVSVTCDFFE                   SQAPATGSENSAVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGSVQYLPDLDDKNSQ                   EKGPQEAFPVHLDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKEKARTAECPGPAQN                   ASPLVLPP                                         SEQ ID NO: 85   1511 bp                             NOV28f,     AAAGTCTGCCTTAAAGAGCCTTACAAGCCAGCCAGTCCCTGCAGCTCCACAAACTGAC             CG135049-06       DNA Sequence     CCATCCTGGGCCTTGTTCTCCACAGA   ATG GGTCTGCTCCTTCCCCTGGCACTCTGCAT                   CCTAGTCCTGTGCTGCGGAGCAATGTCTCCACCCCAGCTGGCCCTCAACCCCTCGGCT                   CTGCTCTCCCGGGGCTGCAATGACTCAGATGTGCTGGCAGTTGCAGGCTTTGCCCTGC                   GGGATATTAACAAAGACAGAAAGGATGGCTATGTGCTGAGACTCAACCGAGTGAACGA                   CGCCCAGGAATACAGACGGGTTTATGGTCAATGCAAAGCAATATTTTATATGAACAAC                   CCAAGTAGAGTTCTCTATTTAGCTGCTTATAACTGTACTCTTCGCCCAGTTTCAAAAA                   AAAAGATTTACATGACGTGCCCTGACTGCCCAAGCTCCATACCCACTGACTCTTCCAA                   TCACCAAGTGCTGGAGGCTGCCACCGAGTCTCTTGCGAAATACAACAATGAGAACACA                   TCCAAGCAGTATTCTCTCTTCAAAGTCACCAGGGCTTCTAGCCAGTGGGTGGTCGGCC                   CTTCTTACTTTGTGGAATACTTAATTAAAGAATCACCATGTACTAAATCCCAGGCCAG                   CAGCTGTTCACTTCAGTCCTCCGACTCTGTGCCTGTTGGTCTTTGCAAAGGTTCTCTG                   ACTCGAACACACTGGGAAAAGTTTGTCTCTCTGACTTGTGACTTCTTTGAATCACAGG                   CTCCAGCCACTGGAAGTGAAAACTCTGCTGTTAACCAGAAACCTACAAACCTTCCCAA                   GGTGGAAGAATCCCAGCAGAAAAACACCCCCCCAACAGACTCCCCCTCCAAAGCTGGG                   CCAAGAGGATCTGTCCAATATCTTCCTGACTTGGATGATAAAAATTCCCAGGAAAAGG                   GCCCTCAGGAGGCCTTTCCTGTGCATCTGGACCTAACCACGAATCCCCACGGAGAAAC                   CCTGGATATTTCCTTCCTCTTCCTGGAGCCTATGGAGGAGAAGCTGGTGGTCCTGCCT                   TTCCCCAAAGAAAAAGCACGCACTGCTGAGTGCCCAGGGCCAGCCCAGAATGCCAGCC                   CTCTTGTCCTTCCGCCA TGA   GAATCACACAGAGTCTTCTGTAGGGCTATGGTCCCCCG                       CATGACATGGGAGGCGATGGGGACGATGGACAGAGACAGAGCGTGCACACGTAGAGTG                       GCTAGTGAAGGACGCCTTTTTGACTCTTCTTGGTCTCAGCATGTTGACTGGCATTGGA                       AATAATGAGACTCAGCCCTCGGCTTGGGCTGCACTCTACCCTGTACACTGCCTTCTAC                       CCTGAGCTGCATCACCTCCTAAACTGAGCAGTCTCATACCATCGACAGATGCCTCTCT                       TATGTCTTCAGCCACTCACTTATAAAGATACTTATCTTTTCAGCAGTATATATGTGCT                       GAAATCTCAGCATGAAAGCATTGCATGAGTAAAGATACTTTCCCTAAAAAAAAAAAAA                       AAA                                           ORF Start: ATG at 85   ORF Stop: TGA at 1120                                         SEQ ID NO: 86   345 aa   MW at 37822.5 kD                             NOV28f,   MGLLLPLALCILVLCCGAMSPPQLALNPSALLSRGCNDSDVLAVAGFALRDINKDRKD           CG135049-06       Protein Sequence   GYVLRLNRVNDAQEYRRVYCQCKAIFYMNNPSRVLYLAAYNCTLRPVSKKKIYMTCPD                   CPSSIPTDSSNHQVLEAATESLAKYNNENTSKQYSLFKVTRASSQWVVGPSYFVEYLI                   KESPCTKSQASSCSLQSSDSVPVGLCKGSLTRTHWEKFVSVTCDFFESQAPATGSENS                   AVNQKPTNLPKVEESQQKNTPPTDSPSKAGPRGSVQYLPDLDDKNSQEKGPQEAFPVH                   LDLTTNPQGETLDISFLFLEPMEEKLVVLPFPKEKARTAECPGPAQNASPLVLPP                  
 
     [0480] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 28B.  
               TABLE 28B                          Comparison of NOV28a against NOV28b through NOV28f.                                         Identities/                   Similarities for           Protein   NOV28a Residues/   the Matched           Sequence   Match Residues   Region                       NOV28b   17 . . . 382   337/366 (92%)               17 . . . 369   337/366 (92%)           NOV28c   17 . . . 382   337/366 (92%)               17 . . . 369   337/366 (92%)           NOV28d   140 . . . 382    225/243 (92%)               75 . . . 317   226/243 (92%)           NOV28e   17 . . . 382   321/366 (87%)               17 . . . 356   321/366 (87%)           NOV28f   17 . . . 382   313/366 (85%)               17 . . . 345   313/366 (85%)                      
 
     [0481] Further analysis of the NOV28a protein yielded the following properties shown in Table 28C.  
               TABLE 28C                       Protein Sequence Properties NOV28a                                                PSort   0.8200 probability located in outside; 0.1900           analysis:   probability located in lysosome (lumen); 0.1000               probability located in endoplasmic reticulum               (membrane); 0.1000 probability located               in endoplasmic reticulum (lumen)           SignalP   Cleavage site between residues 19 and 20           analysis:                      
 
     [0482] A search of the NOV28a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 28D.  
               TABLE 28D                          Geneseq Results for NOV28a                                         NOV28a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAB75368   Human secreted protein #27 -   1 . . . 382   379/382 (99%)   0.0             Homo sapiens , 382 aa.   1 . . . 382   379/382 (99%)           [WO200100806-A2, 04 JAN. 2001]       AAB25782   Human secreted protein SEQ ID   1 . . . 382   379/382 (99%)   0.0           #94 -  Homo sapiens , 382 aa.   1 . . . 382   379/382 (99%)           [WO200037491-A2, 29 JUN. 2000]       AAW88491   Human liver clone HP01263-   1 . . . 382   379/382 (99%)   0.0           encoded transmembrane protein -   1 . . . 382   379/382 (99%)             Homo sapiens , 382 aa.           [WO9855508-A2, 10 DEC. 1998]       AAB51346   Human HS-glycoprotein-like   1 . . . 382   378/382 (98%)   0.0           protein sequence SEQ ID NO: 5 -   1 . . . 382   379/382 (98%)             Homo sapiens , 382 aa.           [JP2000300275-A, 31 OCT. 2000]       AAB51347   Bovine HS-glycoprotein-like   10 . . . 381    245/377 (64%)   e−141           protein sequence SEQ ID NO: 6 -   1 . . . 377   289/377 (75%)             Bos taurus , 378 aa. [JP2000300275-           A, 31 OCT. 2000]                  
 
     [0483] In a BLAST search of public sequence datbases, the NOV28a protein was found to have homology to the proteins shown in the BLASTP data in Table 28E.  
               TABLE 28E                          Public BLASTP Results for NOV28a                                         NOV28a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               CAC24999   Sequence 43 from Patent    1 . . . 382   379/382 (99%)   0.0           WO0100806 precursor -  Homo      1 . . . 382   379/382 (99%)             sapiens  (Human), 382 aa.       Q9UGM5   Fetuin-B precursor (IRL685)    1 . . . 382   377/382 (98%)   0.0           (16G2) -  Homo sapiens  (Human),    1 . . . 382   378/382 (98%)           382 aa.       Q9QXC1   Fetuin-B precursor (IRL685) -    1 . . . 382   246/397 (61%)   e−135             Mus musculus  (Mouse), 388 aa.    1 . . . 388   297/397 (73%)       Q9QX79   Fetuin-B precursor (IRL685) -    1 . . . 377   238/388 (61%)   e−129             Rattus norvegicus  (Rat), 378 aa.    1 . . . 378   295/388 (75%)       Q9D763   2310011017Rik protein -  Mus     61 . . . 382   208/334 (62%)   e−115             musculus  (Mouse), 325 aa.    1 . . . 325   254/334 (75%)                  
 
     [0484] PFam analysis indicates that the NOV28a protein contains the domains shown in the Table 28F.  
               TABLE 28F                          Domain Analysis of NOV28a                                             Identities/                       Similarities for           Pfam   NOV28a Match   the Matched   Expect           Domain   Region   Region   Value                       cystatin    37 . . . 104   23/68 (34%)   5.4e−13                   52/68 (76%)           cystatin   155 . . . 254   32/112 (29%)      6e−10                   70/112 (62%)                       
 
     Example 29  
     [0485] The NOV29 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 29A.  
               TABLE 29A                       NOV29 Sequence Analysis                                                    SEQ ID NO: 87   2973 bp                             NOV29a,   CGCCCCGGGCTGGCGATGCTGCGCCGCCCCGCTCCCGCGCTGGCCCCGGCCGCCCGGC           CG54912-02       DNA Sequence   TGCTGCTGGCCGGGCTGCTGTGCGGCGGCGGGGTCTGGGCCGCGCGAGTTAACAAGCA                   CAAGCCCTGGCTGGAGCCCACCTACCACGGCATAGTCACAGAGAACGACAACACCGTA                   CTCCTCGACCCCCCACTGATCGCGCTGGATAAAGATGCGCCTCTGCGATTTGCAGAGA                   GTTTTGAGGTGACAGTCACCAAAGAAGGTGAGATTTGTGGATTTAATTCACGCGCAAA                   GAATGTCCCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGC                   TCCAAAGAGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCT                   ATGATTGTGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGT                   TCATATTCAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTAC                   AAAGCCACGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGG                   ATGCCGACTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGA                   CGTGCCCTTTACTGTTGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTAC                   GGGAAAGAACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAG                   CCACAGAAGATGTTTTGGTGAAGATCAGCATTAAGCCCACCTGCACCCCTGGGTGGCA                   AGGATGGAACAACAGGATTGAGTATGAGCCGGGCACCGGCGCGTTGGCCGTCTTTCCA                   AATATCCACCTGCAGACATGTGACGAGCCAGTCGCCTCAGTACAGGCCACAGTGGAGC                   TAGAAACCAGCCACATAGGGAAAGGCTGCGACCGAGACACCTACTCAGAGAAGTCCCT                   CCACCGGCTCTGTGGTGCGGCCGCGGGCACTGCCGAGCTGCTGCCATCCCCGAGTGGA                   TCCCTCAACTGGACCATGGOCCTGCCCACCGACAATGGCCACCACAGCGACCAGGTGT                   TTGAGTTCAACGGCACCCAGGCAGTGAGGATCCCGGATGGCCTCGTGTCGGTCAGCCC                   CAAAGAGCCGTTCACCATCTCGGTGTGGATGAGACATGGGCCATTCGGCAGGAAGAAG                   GAGAGAATTCTTTGCAGTTCTGATAAAACAGATATGAATCGGCACCACTACTCCCTCT                   ATGTCCACGGGTGCCGGCTGATCTTCCTCTTCCGTCAGGATCCTTCTGAGGAGAAGAA                   ATACAGACCTGCAGAGTTCCACTGGAAGTTGAATCAGGTCTGTGATGAGGAATGGCAC                   CACTACGTCCTCAATGTAGAATTCCCGAGTCTGACTCTCTATGTGGATGGCACGTCCC                   ACGAGCCCTTCTCTGTGACTGAGGATTACCCGCTCCATCCATCCAAGATAGAAACTCA                   GCTCGTGGTGGGGGCTTGCTGGCAAGAGTTTTCAGGAGTTGAAAATGACAATGAAACT                   GAGCCTGTGACTGTGGCCTCTGCAGGTGGCGACCTGCACATGACCCAGTTTTTCCGAG                   GCAATCTGGCTGGCTTAACTCTCCGTTCCGGGAAACTCGCGGATAACAAGGTGATCGA                   CTGTCTGTATACCTGCAAGGAGGGGCTGGACCTGCAGGTCCTCGAAGACAGTGGCAGA                   GGCGTGCAGATCCAAGCACACCCCAGCCAGTTGGTATTGACCTTGGAGGGAGAAGACC                   TCGGGGAATTGGATAAGGCCATGCAGCACATCTCGTACCTGAACTCCCGGCAGTTCCC                   CACGCCCGGAATTCGCAGACTCAAATCACCAGCACAATCAAGTGTTTTAAACGAGGCC                   ACCTGCATTTCGGTCCCCCCGGTAGATGGCTACGTGATGGTTTTACAGCCCGAGGAGC                   CCAAGATCAGCCTGAGTGGCGTCCACCATTTTGCCCGAGCAGCTTCTGAATTTGAAAG                   CTCAGAAGCCGTGTTCCTTTTCCCTGAGCTTCGCATCATCAGCACCATCACGAGAGAA                   GTGGAGCCTGAAGGGGACGGGGCTGAGGACCCCACAGTTCAAGAATCACTGGTGTCCG                   AGGAGATCGTGCACGACCTGGATACCTGTGAGGTCACGGTGGAGGGAGAGGAGCTGAA                   CCACGAGCAGGAGAGCCTGGAGGTGGACATGGCCCGCCTGCAGCAGAAGGGCATTGAA                   GTGAGCAGCTCTGAACTGGGCATGACCTTCACAGGCGTGGACACCATGGCCAGCTACG                   AGGAGGTTTTGCACCTGCTGCGCTATCGGAACTGGCATGCCAGGTCCTTCCTTGACCG                   GAAGTTTAAGCTCATCTGCTCAGAGCTGAATGGCCGCTACATCAGCAACGAATTTAAG                   GTGGAGGTGAATGTAATCCACACGGCCAACCCCATGGAACACGCCAACCACATGGCTG                   CCCAGCCACAGTTCGTGCACCCGGAACACCGCTCCTTTGTTGACCTGTCAGGCCACAA                   CCTGGCCAACCCCCACCCGTTCGCAGTCGTCCCCAGCACTGCGACAGTTGTGATCGTG                   GTGTGCGTCAGCTTCCTGGTGTTCATGATTATCCTGGGGGTATTTCGGATCCGGGCCG                   CACATCGGCGGACCATGCGGGATCAGGACACCGGGAAGGAGAACGAGATGGACTGGGA                   CGACTCTGCCCTGACCATCACCGTCAACCCCATGGAGACCTATGAGGACCAGCACAGC                   AGTGAGGAGGAGGACGAAGAGGAAGAGGAAGAGGAAGCGAGGACGGCGIAAGAAGAGG                   ATGACATCACCAGCGCCGAGTCGGAGAGCAGCGAGGAGGAGGAGGGGGAGCAGGGCGA                   CCCCCAGAACGCAACCCGGCAGCAGCAGCTGGAGTGGGATGACTCCACCCTCAGCTAC                     TGA   CCCGTGCCCCCG                                           ORF Start: ATG at 16   ORF Stop: TGA at 2959                                         SEQ ID NO:88   981 aa   MW at 109791.7 kD                             NOV29a,   MLRRPAPALAPAARLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPP           CG54912-02       Protein Sequence   LIALDKDAPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGVIRSKEKL                   DCELQKDYSFTTQAYDCGKGPDGTNVKKSHKATVHIQVNDVNEYAPVFKEKSYKATVI                   EGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVPFTVDAAGYIKNTEKLNYGKEHQ                   YKLTVTAYDCGKKRATEDVLVKISIKPTCTPGWQGWNNRIEYEPGTGALAVFPNIHLE                   TCDEPVASVQATVELETSHIGKGCDRDTYSEKSLHRLCGAAAGTAELLPSPSGSLNWT                   MGLPTDNGHDSDQVFEFNGTQAVRIPDGVVSVSPKEPFTISVWMRHGPFGRKKETILC                   SSDKTDMNRHHYSLYVHGCRLIFLFRQDPSEEKKYRPAEFHWKLNQVCDEEWHHYVLN                   VEFPSVTLYVDGTSHEPFSVTEDYPLHPSKIETQLVVGACWQEFSGVENDNETEPVTV                   ASAGGDLHMTQFFRGNLAGLTLRSGKLADKKVIDCLYTCKEGLDLQVLEDSGRGVQIQ                   AHPSQLVLTLECEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISV                   PPVDGYVMVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEG                   DGAEDPTVQESLVSEEIVHDLDTCEVTVEGEELNHEQESLEVDMARLQQKGIEVSSSE                   LGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNEFKVEVNV                   IHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSF                   LVFMIILGVFRIRAAHRRTMRDQDTGKENEMDWDDSALTITVNPMETYEDQHSSEEEE                   EEEEAAEESEDGEEEDDITSAESESSEEEEGEQGDPQNATRQQQLEWDDSTLSY                                         SEQ ID NO: 89   672 bp                             NOV29b,     AGA TCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG           207601301 DNA       Sequence   TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA                   TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC                   CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG                   AGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCTATGATTG                   TGGGAAGGGACCTGATGGCACCAACGTGATAAAGTCTCATAAAGCAACTGTTCATATT                   CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTACAAAGCCA                   CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA                   CTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC                   TTTACTGTCGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTACGGGAAAG                   AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA                   AGATGTTTTGGTGAAGATCAGCATTAAGCTCGAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO 90   224 aa   MW at 25130.3 kD                             NOV29b,   RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV           207601301       Protein Sequence   PFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVIKSHKATVHI                   QVNDVNEYAPVFKEKSYKATVIEGKQYDSTLRVEAVDADCSPQFSQICSYEIITPDVP                   FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE                                         SEQ ID NO: 91   672 bp                             NOV29c,   AGATCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG           207601309 DNA       Sequence   TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA                   TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC                   CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG                   AGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCTATGATTG                   TGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGTTCATATT                   CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTACAAAGCCA                   CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA                   CTGCTCCCCTCAGTTTAGCCACATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC                   TTTACTGTTGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTACGGGAAAG                   AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA                   AGATGTTTTGGTGAAGATCAGCATTAAGCTCGAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 92   224 aa   MW at 25145.3 kD                             NOV29c,   RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV           207601309       Protein Sequence   PFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVKKSHKATVHI                   QVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQTCSYEIITPDVP                   FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE                                         SEQ ID NO: 93   702 bp                             NOV29d     AGA TCTGCGCCAGTTAACAAGCACAAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG           207601313 DNA       Sequence   TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA                   TGCGCCTCTGCGATTTGCAGAGAGTTTTGAGGTGACAGTCACCAAAGAAGGTGAGATT                   TGTGGATTTAAAATTCACGGGCAGAATGTCCCCTTTGATCCAGTGGTAGTGGATAAAT                   CCACTGGTGAGGGAGTCATTCGCTCCAAAGAGAAACTGGACTGTGAGCTGCAGAAAGA                   CTATTCATTCACCATCCAGGCCTGTGGTTGTGGGAAGGGACCTGATGGCACCAACGTG                   AAAAAGTCTCATAAAGCAACTGTTCATATTCAGGTGAACGACGTGAATGAGTACGCGC                   CCGTGTTCAAGGAGAAGTCCTACAAAGCCACGGTCATCGAGGGGAACCAGTACGACAG                   CATTTTGAGGGTGGAGGCCGTGGATGCCGACTGCTCCCCTCAGTTCAGCCAGATTTGC                   AGCTACGAAATCATCACTCCAGACGTGCCCTTTACTGTTGACAAAGATGGTTATATAA                   AAAACACAGAGAAATTAAACTACGGGAAAGAACATCAATATAAGCTGACCGTCACTGC                   CTATGACTGTGGGAAAAAAAGAGCCACAGAAGATGTTTTGGTGAAGATCAGCATTAAG                   CTCGAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 94   234 aa   MW at 26177.4 kD                             NOV29d,   RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAESFEVTVTKEGEI           207601313       Sequence   CGFKIHGQNVPFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQACGCGKGPDGTNV                   KKSHKATVHIQVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQIC                   SYEIITPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIK                   LE                                         SEQ ID NO: 95   672 bp                             NOV29e,     AGA TCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGAGCCCACCTACCACGGCATAG           207601331 DNA       Sequence   TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA                   TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC                   CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG                   AGAAACTGGACTGTGAGCTGCAGAAAGACTATTCATTCACCATCCAGGCCTATGATTG                   TGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGTTCATATT                   CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAGGTCCTACAAAGCCA                   CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA                   CTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC                   TTTACTGTTGACAAAGATGGTTATATAAAAAACACACAGAAATTAAACTACGGGAAAG                   AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA                   AGATGTTTTGGTGAAGATCAGCATTAAGCTCCAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO:96   224 aa   MW at 25173.3 kD                             NOV29e,   RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV           207601331       Protein Sequence   PFDAVVVDKSTGEGVTRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVKKSHKATVHI                   QVNDVNEYAPVFKERSYKATVIEGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVP                   FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE                                         SEQ ID NO: 97   672 bp                             NOV29f,   AGATCTGCGCGAGTTAACAAGCACAAGCCCTGGCTGGACCCCACCTACCACGGCATAG           207639332 DNA       Sequence   TCACAGAGAACGACAACACCGTGCTCCTCGACCCCCCACTGATCGCGCTGGATAAAGA                   TGCGCCTCTGCGATTTGCAGGTGAGATTTGTGGATTTAAAATTCACGGGCAGAATGTC                   CCCTTTGATGCAGTGGTAGTGGATAAATCCACTGGTGAGGGAGTCATTCGCTCCAAAG                   AGAAACTGGACTGTGAGCTGCACAAAGGCTATTCATTCACCATCCAGGCCTATGATTG                   TGGGAAGGGACCTGATGGCACCAACGTGAAAAAGTCTCATAAAGCAACTGTTCATATT                   CAGGTGAACGACGTGAATGAGTACGCGCCCGTGTTCAAGGAGAAGTCCTACAAAGCCA                   CGGTCATCGAGGGGAAGCAGTACGACAGCATTTTGAGGGTGGAGGCCGTGGATGCCGA                   CTGCTCCCCTCAGTTCAGCCAGATTTGCAGCTACGAAATCATCACTCCAGACGTGCCC                   TTTACTGTTGACAAAGATGGTTATATAAAAAACACAGAGAAATTAAACTACGGGAAAG                   AACATCAATATAAGCTGACCGTCACTGCCTATGACTGTGGGAAGAAAAGAGCCACAGA                   AGATGTTTTGGTGAAGATCAGCATTAAGCTCGAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 98   224 aa   MW at 25087.2 kD                             NOV29f,   RSARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAGEICGFKIHGQNV           207639332       Protein Sequence   PFDAVVVDKSTGEGVIRSKEKLDCELQKGYSFTIQAYDCGKGPDGTNVKKSHKATVHI                   QVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVP                   FTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKLE                  
 
     [0486] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 29B.  
               TABLE 29B                          Comparison of NOV29a against NOV29b through NOV29f.                                         Identities/                   Similarities for           Protein   NOV29a Residues/   the Matched           Sequence   Match Residues   Region                       NOV29b   28 . . . 258   219/231 (94%)                2 . . . 222   220/231 (94%)           NOV29c   28 . . . 258   220/231 (95%)                2 . . . 222   221/231 (95%)           NOV29d   28 . . . 258   228/231 (98%)                2 . . . 232   229/231 (98%)           NOV29e   28 . . . 258   219/231 (94%)                2 . . . 222   221/231 (94%)           NOV29f   28 . . . 258   219/231 (94%)                2 . . . 222   220/231 (94%)                      
 
     [0487] Further analysis of the NOV29a protein yielded the following properties shown in Table 29C.  
               TABLE 29C                       Protein Sequence Properties NOV29a                                        PSort   0.4600 probability located in plasma membrane; 0.1030       analysis:   probability located in microbody (peroxisome); 0.1000           probability located in endoplasmic reticulum           (membrane); 0.1000 probability located in endoplasmic           reticulum (lumen)       SignalP   Cleavage site between residues 29 and 30       analysis:                  
 
     [0488] A search of the NOV29a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 29D.  
               TABLE 29D                          Geneseq Results for NOV29a                                         NOV29a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAB93107   Human protein sequence SEQ ID   646 . . . 981    335/336 (99%)   0.0           NO: 11970 -  Homo sapiens , 336 aa.    1 . . . 336   336/336 (99%)           [EP1074617-A2, 07 FEB. 2001]       AAU19843   Human novel extracellular matrix   50 . . . 331   270/282 (95%)   e−158           protein, Seq ID No 493 -  Homo      5 . . . 276   270/282 (95%)             sapiens , 276 aa. [WO200155368-           A1, 02 AUG. 2001]       AAW95631     Homo sapiens  secreted protein gene   15 . . . 408   246/405 (60%)   e−146           clone hj968_2 -  Homo sapiens , 428    8 . . . 400   301/405 (73%)           aa. [WO9856805-A1, 17 DEC.           1998]       AAU91129   Human secreted protein sequence   514 . . . 949    198/444 (44%)   e−114           #49 -  Homo sapiens , 467 aa.   17 . . . 456   309/444 (69%)           [WO200218412-A1, 07 MAR.           2002]       AAB58434   Lung cancer associated polypeptide   514 . . . 944    195/444 (43%)   e−113           sequence SEQ ID 772 -  Homo     17 . . . 456   305/444 (67%)             sapiens , 467 aa. [WO200055180-           A2, 21 SEP. 2000]                  
 
     [0489] In a BLAST search of public sequence datbases, the NOV29a protein was found to have homology to the proteins shown in the BLASTP data in Table 29E.  
               TABLE 29E                          Public BLASTP Results for NOV29a                                         NOV29a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               O94985   KIAA0911 protein -  Homo     1 . . . 981    981/981 (100%)   0.0             sapiens  (Human), 981 aa.   1 . . . 981    981/981 (100%)       Q9EPL2   Calsyntenin-1 protein precursor -   1 . . . 981   907/981 (92%)   0.0             Mus musculus  (Mouse), 979 aa.   1 . . . 979   948/981 (96%)       Q9DDD3   Calsyntenin-1 protein -  Gallus     31 . . . 981    818/952 (85%)   0.0             gallus  (Chicken), 948 aa   1 . . . 948   891/952 (92%)           (fragment).       AAH29027   Hypothetical 83.0 kDa protein -   235 . . . 981    683/747 (91%)   0.0             Mus musculus  (Mouse), 745 aa   1 . . . 745   718/747 (95%)           (fragment).       Q9H4D0   Calsyntenin-2 -  Homo sapiens     28 . . . 981    528/968 (54%)   0.0           (Human), 955 aa.   34 . . . 955    707/968 (72%)                  
 
     [0490] PFam analysis indicates that the NOV29a protein contains the domains shown in the Table 29F.  
               TABLE 29F                          Domain Analysis of NOV29a                                             Identities/                       Similarities for           Pfam   NOV29a Match   the Matched   Expect           Domain   Region   Region   Value                                                 cadherin    42 . . . 155   30/127 (24%)   0.071                   72/127 (57%)           cadherin   169 . . . 258   28/108 (26%)   0.0034                   61/108 (56%)                      
 
     Example 30  
     [0491] The NOV30 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 30A.  
               TABLE 30A                       NOV30 Sequence Analysis                                                    SEQ ID NO: 99   24 bp                             NOV30a,    TTTGAGCAAAACAGAAGACAGCCC           CG56315-03 DNA Sequence                                                  ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 100   8 aa   MW at 1074.2kD                             NOV30a,    FEQNRRQP           CG56315-03 Protein Sequence                                                  SEQ ID NO: 101   24 bp                             NOV30b,    TTTGAGTGCAACAGGAGACAGCCC           CG56315-04 DNA Sequence                                                  ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 102   8 aa   MW at 1049.2kD                             NOV30b,    FECNRRQP           CG56315-04 Protein Sequence                                                  SEQ ID NO: 103   24 bp                             NOV30c,    TTTGAGCAAAACAGTAGACAGCCC           CG56315-05 DNA Sequence                                                  ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 104   8 aa   MW at 1005.1kD                             NOV30c,    FEQNSRQP           CG56315-05 Protein Sequence                                                  SEQ ID NO: 105   24 bp                             NOV30d,    TTTGAGTGCAACAGTAGACAGCCC           CG56315-06 DNA Sequence                                                  ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 106   8 aa   MW at 980.1kD                             NOV30d,    FECNSRQP           CG56315-06 Protein Sequence                                                  SEQ ID NO: 107   24 bp                             NOV30e,    TTTGAGCAAAACAGTAGACAGGCC           CG56315-07 DNA Sequence                                                  ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 108   8 aa   MW at 979.0kD                             NOV30e,    FEQNSRQA           CG56315-07 Protein Sequence                                                  SEQ ID NO: 109   24 bp                             NOV30f,    TTTGAGTGCAACAGTAGACAGGCC           CG56315-08 DNA Sequence                                                  ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 110   8 aa   MW at 954.0kD                             NOV30f,    FECNSRQA           CG56315-08 Protein Sequence                  
 
     [0492] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 30B.  
               TABLE 30B                          Comparison of NOV30a against NOV3Ob through NOV30f.                                         Identities/                   Similarities for           Protein   NOV30a Residues/   the Matched           Sequence   Match Residues   Region                                         NOV30b   No Significant Alignment Found.                                 NOV30c   1 . . . 8   7/8 (87%)               1 . . . 8   7/8 (87%)                             NOV30d   No Significant Alignment Found.           NOV30e   No Significant Alignment Found.           NOV30f   No Significant Alignment Found.                      
 
     [0493] Further analysis of the NOV30a protein yielded the following properties shown in Table 30C.  
               TABLE 30C                       Protein Sequence Properties NOV30a                                                PSort analysis:               SignalP analysis:   No Known Signal Sequence Indicated                      
 
     [0494] A search of the NOV30a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 30D.  
               TABLE 30D                          Geneseq Results for NOV30a                                         NOV30a   Identities/               Protein/   Residues/   Similarities for       Geneseq   Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value                         No Significant Matches Found                  
 
     [0495] In a BLAST search of public sequence datbases, the NOV30a protein was found to have homology to the proteins shown in the BLASTP data in Table 30E.  
               TABLE 30E                          Public BLASTP Results for NOV30a                                         NOV30a   Identities/           Protein       Residues/   Similarities for       Accession   Protein/   Match   the Matched   Expect       Number   Organism/Length   Residues   Portion   Value                         No Significant Matches Found                  
 
     [0496] PFam analysis indicates that the NOV30a protein contains the domains shown in the Table 30F.  
               TABLE 30F                          Domain Analysis of NOV30a                                             Identities/                       Similarities for               NOV30a   the Matched   Expect           Pfam Domain   Match Region   Region   Value                             No Significant Matches Found                  
 
     Example 31  
     [0497] The NOV31 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 31A.  
               TABLE 31A                       NOV31 Sequence Analysis                                                    SEQ ID NO: 115   2628 bp                             NOV31a,      ACCGTGCCTCTGCGGCCTGCGTGCCCGGAGTCCCCGCCTGTGTCGTCTCTGTCGCCGT             CG56326-01       DNA Sequence     CCCCGTCTCCTGCCAGGCGCGGAGCCCTGCGAGCCGCGGGTGGGCCCCAOGCGCGCAG                       ACATGGGCTGCTCCGCCAAAGCGCGCTGGGCTGCCGGGGCGCTGGGCGTCGNGGGGCT                       ACTGTGCGCTGTGCTCGGCGCTGTCATGATCGTGATGGTGCNG TCGCTCATCAAGCAG                   CAGGTCCTTAAGAACGTCCGCATCGACCCCAGTAGCCTGTCCTTCAACATGTGGAAGG                   AGATCCCTATCCCCTTCTATCTCTCCGTCTACTTCTTTGACGTCATGAACCCCAGCGA                   GATCCTGAAGGGCGAGAAGCCGCAGGTGCGGGAGCCCGGGCCCTACGTCTACAGGGAG                   TTCAGGCACAAAAGCAACATCACCTTCAACAACAACGACACCGTGTCCTTCCTCGAGT                   ACCGCACCTTCCAGTTCCAGCCCTCCAAGTCCCACGGCTCGGAGAGCGACTACATCGT                   CATGCCCAACATCCTGGTCTTGGGTGCGGCGGTGATGATGGAGAATAAGCCCATGACC                   CTGAAGCTCATCATGACCTTGGCATTCACCACCCTCGGCGAACGTGCCTTCATGAACC                   GCACTGTGGGTGAGATCATGTGGGGCTACAAGGACCCCCTTGTGAATCTCATCAACAA                   GTACTTTCCAGGCATGTTCCCCTTCAAGGACAAGTTCGGATTATTTGCTGAGCTCAAC                   AACTCCGACTCTGGGCTCTTCACGGTGTTCACGGGGGTCCAGAACATCAGCAGGATCC                   ACCTCGTGGACAAGTGGAACGGGCTGAGCAAGGTTGACTTCTGGCATTCCGATCAGTG                   CAACATGATCAATGGAACTTCTGGGCAAATGTGGCCGCCCTTCATGACTCCTGAGTCC                   TCGCTGGAGTTCTACAGCCCGGAGGCCTGCCGATCCATGAAGCTAATGTACAAGGAGT                   CAGGGGTGTTTGAAGGCATCCCCACCTATCGCTTCGTGGCTCCCAAAACCCTGTTTGN                   CAACGGGTCCATCTACCCACCCAACGAAGGCTTCTGCCCGTGCCTGGAGTCTGGAATT                   CAGAACGTCAGCACCTGCAGGTTCAGTGCCCCCTTGTTTCTCTCCCATCCTCACTTCC                   TCAACGCCGACCCGGTTCTGGCAGAAGNGGTGACTNNCCTGCACNCTAACCAGGAGGC                   ACACTCCTTGTTCCTGGACATCCACCCGGTCACGGGAATCCCCATGAACTGCTCTGTG                   AAACTGCAGCTGAGCCTCTACATGAAATCTGTCGCAGGCATTGGACAAACTGGGAAGA                   TTGAGCCTGTGGTCCTGCCGCTGCTCTGGTTTGCACAGAGCGGGGCCATGGAGGGGGA                   GACTCTTCACACATTCTACACTCAGCTGGTGTTGATGCCCAAGGTGATGCACTATGCC                   CAGTACGTCCTCCTGGCGCTGGGCTGCGTCCTGCTGCTGGTCCCTGTCATCTGCCAAA                   TCCGGAGCCAAGAGAAATGCTATTTATTTTGGAGTAGTAGTAAAAAGGGCTCAAAGGA                   TAAGGAGGCCATTCAGGCCTATTCTGAATCCCTGATGACATCAGCTCCCAAGGGCTCT                   GTGCTGCAGGAAGCAAAACTGTAGGCTCCTGAGGACACCGTGAGCCAGCCAGGCCTGG                   CCGCTGGGCCTGACCGGCCCCCCAGCCCCTACACNCCGCTTCTCCCGGACTCTCCCAG                   CAGACAG CCCCCCAGCCCCACAGCCTGAGCCTCCCAGCTGCCATGTCCCTGTTGCACA                       CCTGCACACACGCCCTGGCACACATACACACATGCGTGCAGGCTTGTGCAGACACTCA                       GGGATGGAGCTGCTGCTGAAGGGACTTGTAGGGAGAGGCTCGTCAACAACCACTGTTC                       TGGAACGTTCTCTCCACGTGGCCCACAGGCCTGACCACAGGGGCTGTGGGTCCTGCGT                       CCCCTTCCTCGGGTGAGCCTGGCCTGTCCCGTTCAGCCGTTGGGCCCAGGCTTCCTCC                       CCTCCAACGTGAAACACTGCAGTCCCGGTGTGGTGGCTCCCCATGCAGGACGGGCCAG                       GCTGGGAGTGCCGCCTTCCTGTGCCAAATTCAGTGGGGACTCAGTGCCCAGGCCGTGG                       CCACGAGCTTTGGCCTTGGTCTACCTGCCAGGCCAGGCAAAGCGCCTTTACACAGGCC                       TCGGAAAACAATGGAGTGAGCACAAGATGCCCTGTGCAGCTGCCCGAGGGTCTCCGCC                       CACCCCGGCCGGACTTTGATCCCCCCGAAGTCTTCACAGGCACTCCATCGGGTTGTCT                       GGCGCCCTTTTCCTCCAGCCTAAACTGACATCATCCTATGGACTGAGCCGGCCACTTT                       GGCCGAAGTGGCCGCAGGCTGTGCCCCCGAGCTGCCCCCACCCCCTCACAGGGTCCCT                       CAGATTATAGGTGCCCAGGCTGAGGTGAAGAGGCCTGGGGGCCCTGCCTTCCGGCCGC                       TCCTGGACCCTGGGGCAAACCTGTGACCCTTTTCTACTGGAATAGAAATGAGTTTTAT                       CATCTTTGAAAAATAATTCACTCTTGAAGTAATAAACGTTTAAAAAAATGGGAAAAAA                       AAAAAAAAAAAAAAAAAA                                           ORF Start: at 218   ORF Stop: at 1745                                         SEQ ID NO: 116   509 aa   MW at 56449.3kD                             NOV31a,    MGCSAKARWAAGALGVXGLLCAVLGAVMIVMVXSLIKQQVLKNVRIDPSSLSFNMWKE           CG56326-01        Protein Sequence   IPIPFYLSVYFFDVMNPSEILKGEKPQVREPGPYVYREFRHKSNITFNNNDTVSFLEY                   RTFQFQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNR                   TVGEIMWGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIH                   LVDKWNGLSKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKES                   GVFEGIPTYRFVAPKTLFXNGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFL                   NADPVLAEXVTXLHXNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKI                   EPVVLPLLWFAESGAMEGETLHTFYTQLVLMPKVMHYAQYVLLALGCVLLLVPVICQI                   RSQEKCYLFWSSSKKGSKDKEAIQAYSESLMTSAPKGSVLQEAKL                                         SEQ ID NO: 117   1248bp                             NOV31b,    AGATCTCTCATCAAGCAGCAGGTCCTTAAGAACGTGCCCATCGACCCCAGTAGCCTGT           175070268 DNA       Sequence   CCTTCAACATGTGGAAGGAGATCCCTATCCCCTTCTATCTCTCCGTCTACTTCTTTGA                   CGTCATGAACCCCAGCGAGATCCTGAAGGGCGAGAAGCCGCAGGTGCGGGAGCGCGGG                   CCCTACGTGTACAGGGAGTTCAGGCACAAAAGCAACATCACCTTCAACAACAACGACA                   CCGTGTCCTTCCTCGAGTACCGCACCTTCCAGTTCCAGCCCTCCAAGTCCCACGGCTC                   GGAGAGCGACTACATCGTCATGCCCAACATCCTGGTCTTGGGTGCGGCGGTGATGATG                   GAGAATAAGCCCATGACCCTGAAGCTCATCATGACCTTGGCATTCACCACCCTCGGCG                   AACGTGCCTTCATGAACCGCACTGTGGGTGAGATCATGTGGGGCTACAAGGACCCCCT                   TGTGAATCTCATCAACAAGTACTTTCCAGGCATGTTCCCCTTCAAGGACAAGTTCGGA                   TTATTTGCTGAGCTCAACAACTCCGACTCTGGGCTCTTCACGGTGTTCACGGGGGTCC                   AGAACATCAGCAGGATCCACCTCGTGGACAAGTGGAACGGGCTGAGCAAGGTTGACTT                   CTGGCATTCCGATCAGTGCAACATGATCAATGGAAGTTCTGGGCAAATGTGGCCGCCC                   TTCATGACTCCTGAGTCCTCGCTGGAGTTCTACAGCCCGGAGGCCTGCCGATCCATGA                   AGCTAATGTACAAGGAGTCAGGGGTGTTTGAAGGCATCCCCACCTATCGCTTCGTGGC                   TCCCAAAACCCTGTTTGCCAACGGGTCCATCTACCCACCCAACGAAGGCTTCTGCCCG                   TGCCTGGAGTCTGGAATTCAGAACGTCAGCACCTGCAGGTTCAGTGCCCCCTTGTTTC                   TCTCCCATCCTCACTTCCTCAACGCCGACCCGGTTCTGGCAGAAGCGGTGACTGGCCT                   GCACCCTAACCAGGAGGCACACTCCTTGTTCCTGGACATCCACCCGGTCACGGGAATC                   CCCATGAACTGCTCTGTGAAACTGCAGCTGAGCCTCTACATGAAATCTGTCGCAGGCA                   TTGGACAAACTGGGAAGATTGAGCCTGTGGTCCTGCCGCTGCTCTGGTTTGCAGAGAG                   CGGGGCCATGGAGGGCGAGACTCTTCACACATTCTACACTCAGCTGGTGTTGATGCCC                   AAGGTGATGCACTATGCCCAGTACGTCGAC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 118   416 aa   MW at 47303.3kD                             NOV31b,    RSLIKQQVLKNVRIDPSSLSFNMWKEIPIPFYLSVYFFDVMNPSEILKGEKPQVRERG           175070268       Protein Sequence   PYVYREFRHKSNITFNNNDTVSFLEYRTFQFQPSKSHGSESDYIVMPNILVLGAAVMM                   ENKPMTLKLIMTLAFTTLCERAFMNRTVGEIMWGYKDPLVNLINKYFPGMFPFKDKFG                   LFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGLSKVDFWHSDQCNMINCTSGQMWPP                   FMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYRFVAPKTLFANGSIYPPNEGFCP                   CLESGIQNXTSTCRFSAPLFLSHPHFLNADPVLAEAVTGLHPNQEAHSLFLDIHPVTGI                   PMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESGAJAEGETLHTFYTQLVLMP                   KVMHYAQYVD                  
 
     [0498] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 31B.  
               TABLE 31B                          Comparison of NOV31a against NOV31b.                                         Identities/                   Similarities for           Protein   NOV31a Residues/   the Matched           Sequence   Match Residues   Region                       NOV31b   34 . . . 447   409/414 (98%)                2 . . . 415   409/414 (98%)                      
 
     [0499] Further analysis of the NOV31a protein yielded the following properties shown in Table 31C.  
               TABLE 31C                       Protein Sequence Properties NOV31a                                        PSort   0.5644 probability located in microbody (peroxisome);       analysis:   0.4600 probability located in plasma membrane;           0.1000 probability located in endoplasmic reticulum           (membrane); 0.1000 probability located in endoplasmic           reticulum (lumen)       SignalP   Cleavage site between residues 35 and 36       analysis:                  
 
     [0500] A search of the NOV31a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 31D.  
               TABLE 31D                          Geneseq Results for NOV31a                                         NOV31a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAW97900   Human SR-BI class B scavenger -   1 . . . 509   503/509 (98%)   0.0             Homo sapiens , 509 aa.   1 . . . 509   503/509 (98%)           [WO9902736-A2, 21 JAN. 1999]       AAW97899   Human SR-BI class B scavenger -   1 . . . 509   502/509 (98%)   0.0             Homo sapiens , 509 aa.   1 . . . 509   502/509 (98%)           [WO9902735-A2, 21 JAN. 1999]       ABB12012   Human SR-BI class B scavenger   1 . . . 509   501/509 (98%)   0.0           homologue, SEQ ID NO: 2382 -   24 . . . 532    501/509 (98%)             Homo sapiens , 532 aa.           [WO200157188-A2, 09 AUG.           2001]       AAY49573   Human CLA-1 protein sequence -   1 . . . 509   501/509 (98%)   0.0             Homo sapiens , 509 aa.   1 . . . 509   501/509 (98%)           [WO9950454-A2, 07 OCT. 1999]       ABG22317   Novel human diagnostic protein   1 . . . 509   485/514 (94%)   0.0           #22308 -  Homo sapiens , 537 aa.   24 . . . 537    490/514 (94%)           [WO200175067-A2, 11 OCT. 2001]                  
 
     [0501] In a BLAST search of public sequence datbases, the NOV31a protein was found to have homology to the proteins shown in the BLASTP data in Table 31E.  
               TABLE 31E                          Public BLASTP Results for NOV31a                                             Identities/           Protein           Similarities for       Accession       NOV31a Residues/   the Matched   Expect       Number   Protein/Organism/Length   Match Residues   Portion   Value               Q14016   CLA-1 -  Homo sapiens  (Human),   1 . . . 509   501/509 (98%)   0.0           509 aa.   1 . . . 509   501/509 (98%)       Q8WTV0   Similar to CD36 antigen (collagen   1 . . . 467   460/467 (98%)   0.0           type I receptor, thrombospondin   1 . . . 467   460/467 (98%)           receptor)-like 1 -  Homo sapiens             (Human), 552 aa.       Q8SQC1   High density lipoprotein receptor   1 . . . 509   437/509 (85%)   0.0           SR-BI -  Sus scrofa  (Pig), 509 aa.   1 . . . 509   474/509 (92%)       O18824   Scavenger receptor class B type 1 -   1 . . . 509   418/509 (82%)   0.0             Bos taurus  (Bovine), 509 aa.   1 . . . 509   462/509 (90%)       Q60417   HaSR-BI -  Cricetulus griseus     1 . . . 509   409/509 (80%)   0.0           (Chinese hamster), 509 aa.   1 . . . 509   455/509 (89%)                  
 
     [0502] PFam analysis indicates that the NOV31a protein contains the domains shown in the Table 31F.  
               TABLE 31F                          Domain Analysis of NOV31a                                     Identities/           Pfam   NOV31a   Similarities for       Domain   Match Region   the Matched Region   Expect Value               CD36   5 . . . 445   213/567 (38%)   3.6e−227               410/567 (72%)                  
 
     Example 32  
     [0503] The NOV32 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 32A.  
               TABLE 32A                       NOV32 Sequence Analysis                                                    SEQ ID NO: 119   1284 bp                             NOV32a,    ATGCATCTTATCGACTACCTGCTCCTCCTGCTGGTTCGACTACTGGCCCTTTCTCATG           CG56711-01        DNA Sequence    GCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGCAGAT                   TCTGGAGACAGGTGGGGGCTCCCCCAGCCTCPAGATAGCCCCTGCCAATGCTGACTTT                   GCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTTTTCT                   CCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCACACAG                   CCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTCCGAT                   GTCCATAGGGGCTTCCACCACCTCCTGCACACTCTGAACCTCCCCGGCCATGGGCTGG                   AAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAAAATT                   CCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTACGAC                   ACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGGAAGA                   TTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATTACAT                   TTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAAAGAC                   TTTTATGTTGATGAGAACACAACACTCCGGGTGCCCATGATGCTGCAGGACCAGGAGC                   ATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATTACAA                   AGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGATTGAA                   GAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACPACTTGTTGCGGAAGAGGAATT                   TTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATGTATT                   AGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGACTTA                   TCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCCACCT                   TGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCAAATT                   CTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGTGGTG                   ATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCCACGA                   AACCATAG                                         ORF Start: ATG at 1   ORF Stop: TAG at 1282                                         SEQ ID NO: 120   427 aa   MW at 48469.3kD                             NOV32a,    MHLIDYLLLLLVGLLALSHGQLHVEHDGESCSNSSHQQILETGGGSPSLKIAPANADF           CG56711-01        Protein Sequence    AFRFYYLIASETPGKNIFFSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESD                   VHRGFQHLLHTLNLPGHGLETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYD                   TVGTIQLINDHVKKETRGKIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKD                   FYVDENTTVRVPMMLQDQEHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIE                   EVLTPEMLMRWNNLLRKRNFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADL                   SGITKQQKLEASKSFHKATLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVV                   IFSTSTQSVLFLGKVVDPTKP                                         SEQ ID NO: 121   1233 bp                             NOV32b,    GGATCCCAGCTGCACGTTGAGCATGATCGTGAGAGTTGCAGTAACAGCTCCCACCAGC           166280659 DNA        Sequence    AGATTCTGGAGACAGGTGAGGCCTCCCCCAGCCTGAAGATAGCCCCTGCCAATGCTGA                   CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT                   TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC                   ACAGCCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTC                   CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG                   CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCPA                   AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA                   CCACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG                   AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT                   ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA                   AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG                   GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT                   ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT                   TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG                   AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG                   TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA                   CTTATCCGGCATCACCAAACAGCAAAAACTGGACGCATCCAAAAGTTTCCACAAGGCC                   ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA                   AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT                   GGTGATCTTTTCCACCAGCACCCAGACTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC                   ACGAAACCAGAATTC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 122   411 aa   MW at 46775.1kD                             NOV32b,    GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF           166280659        Protein Sequence    FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG                   LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG                   KTVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ                   EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR                   NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGTTKQQKLEASKSFHKA                   TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP                   TKPEF                                         SEQ ID NO: 123   1233 bp                             NOV32c,    GGATCCCAGCTGCACGTTCAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC           166280667 DNA        166280667 DNA    AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA       Sequence            CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT                   TTCTCCCCGCTGACCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC                   ACAGCCGCAGCCAGATCCTTGAGGGCCTGGCCTTCAACCTCACCGAGCTGTCTGAGTC                   CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG                   CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA                   AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA                   CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG                   AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT                   ACATTTACTTCAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCGAGGG                   AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG                   GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCCGTGCTACGGATGGATT                   ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT                   TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG                   AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG                   TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA                   CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC                   ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA                   AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT                   GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC                   ACGAAACCAGAATTC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 124   411 aa   MW at 46775.1kD                             NOV32e,    GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF           166280667        Protein Sequence    FSPLSISAAYANLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG                   LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG                   KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ                   EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR                   NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA                   TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP                   TKPEF                                         SEQ ID NO: 125   1233 bp                             NOV32d,    GGATCCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC           166280670 DNA        Sequence    AGATTCTGGACACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA                   CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT                   TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC                   ACAGCCGCAGCCAGATCCTTGAGGGCCTGCGCTTCAACCTCACCGAGCTGTCTGAGTC                   CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG                   CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA                   AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA                   CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG                   AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT                   ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA                   AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG                   GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT                   ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT                   TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG                   AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG                   TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA                   CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC                   ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA                   AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT                   GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC                   ACGAAACCAGAATTC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 126   411 aa   MW at 46775.1kD                             NOV32d,    GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF           166280670        Protein Sequence    FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG                   LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG                   KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ                   EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR                   NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA                   TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP                   TKPEF                                         SEQ ID NO: 127   1233 bp                             NOV32e,    GGATCCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC           166280673 DNA        Sequence    AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA                   CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT                   TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC                   ACAGCCGCACCCAGATCCTTGAGCGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTC                   CGATGTCCATAGGCCCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG                   CTGGAAACACGCGTGCGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA                   AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA                   CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG                   AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGCACGTCTTGATGGTGCTGGTGAATT                   ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA                   AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATCATGCTGCAGGACCAG                   GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACCGATGGATT                   ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT                   TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG                   AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG                   TATTAGATCAGATTTTGCCCAGCCTGGGCTTCACGGATCTGTTCTCCAAGTGCGCTGA                   CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC                   ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA                   AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT                   GGTGATCTTTTCCACCAGCACCCAGACTCTCCTCTTTCTGGGCAAGGTCGTCGACCCC                   ACGAAACCAGAATTC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 128   411 aa   MW at 46775.1kD                             NOV32e,    GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF           166280673        Protein Sequence    FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRCFQHLLHTLNLPGHG                   LETRVOSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG                   KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ                   EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR                   NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA                   TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP                   TKPEF                                         SEQ ID NO: 129   1233 bp                             NOV32f,    GGATCCCAGCTGCACGTTGAGCATGATCGTCAGAGTTGCAGTAACAGCTCCCACCAGC           166280680 DNA       Sequence    AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA                   CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT                   TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC                   ACAGCCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTCAGTC                   CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG                   CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTCAAGTTCCTTGCAA                   AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA                   CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG                   AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGCTGAATT                   ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA                   AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCACGACCAG                   GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT                   ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT                   TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG                   AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG                   TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA                   CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC                   AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGOCCCTTCCTTGT                   GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC                   ACGAAACCAGAATTC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 130   411 aa   MW at 46775.1kD                             NOV32f,    GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF           166280680       Protein Sequence    FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG                   LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG                   KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ                   EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR                   NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA                   TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP                   TKPEF                                         SEQ ID NO: 131   1233 bp                             NOV32g,    GGATCCCAGCTGCACGTTGAGCATGATGGTGAGAGTTGCAGTAACAGCTCCCACCAGC           166280703 DNA        Sequence    AGATTCTGCAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA                   CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT                   TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC                   ACAGCCGCAGCCAGATCCTTGAGGGCCTCCGCTTCAACCTCACCGAGCTGTCTGAGTC                   CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG                   CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA                   AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA                   CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG                   AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT                   ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA                   AGACTTTTATGTTGATGAGAACACAACACTCCGGGTGCCCATGATGCTGCAGGACCAG                   GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATCGATT                   ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT                   TGAAGAGGTTCTGACTCCAGAGATGCTAATGAGGTGGAACAACTTGTTGCGGAAGAGG                   AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG                   TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCPAGTGGGCTGA                   CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC                   ACCTTGGACGTGGATGAGGCTGGCACCGACGCTGCAGCAGCCACCAGCTTCGCGATCA                   AATTCTTCTCTGCCCAGACCAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT                   GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC                   ACGAAACCAGAATTC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 132   411 aa   MW at 46775.1kD                             NOV32g,    GSQLHVEHDCESCSNSSHQQTLETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF           166280703       Protein Sequence    FSPLSISAAYAMLSLGACSHSRSQILEGLCFNLTELSESDVHRGFQHLLHTLNLPGHG                   LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG                   KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPNMLQDQ                   EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR                   NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA                   TLDVDEAGTEAAAATSFATKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP                   TKPEF                                         SEQ ID NO: 133   1233 bp                             NOV32h,    GGATCCCAGCTGCACGTTGAGCATGATGGTGAGACTTGCAGTAACAGCTCCCACCAGC           166280730 DNA           Sequence    AGATTCTGGAGACAGGTGAGGGCTCCCCCAGCCTCAAGATAGCCCCTGCCAATGCTGA                   CTTTGCCTTCCGCTTCTACTACCTGATCGCTTCGGAGACCCCGGGGAAGAACATCTTT                   TTCTCCCCGCTGAGCATCTCGGCGGCCTACGCCATGCTTTCCCTGGGGGCCTGCTCAC                   ACAGCCGCAGCCAGATCCTTGAGGGCCTGGGCTTCAACCTCACCGAGCTGTCTGAGTC                   CGATGTCCATAGGGGCTTCCAGCACCTCCTGCACACTCTCAACCTCCCCGGCCATGGG                   CTGGAAACACGCGTGGGCAGTGCTCTGTTCCTGAGCCACAACCTGAAGTTCCTTGCAA                   AATTCCTGAATGACACCATGGCCGTCTATGAGGCTAAACTCTTCCACACCAACTTCTA                   CGACACTGTGGGCACAATCCAGCTTATCAACGACCACGTCAAGAAGGAAACTCGAGGG                   AAGATTGTGGATTTGGTCAGTGAGCTCAAGAAGGACGTCTTGATGGTGCTGGTGAATT                   ACATTTACTTCAAAGCCCTGTGGGAGAAACCATTCATTTCCTCAAGGACCACTCCCAA                   AGACTTTTATGTTGATGAGAACACAACAGTCCGGGTGCCCATGATGCTGCAGGACCAG                   GAGCATCACTGGTATCTTCATGACAGATACTTGCCCTGCTCGGTGCTACGGATGGATT                   ACAAAGGAGACGCAACCGTGTTTTTCATTCTCCCTAACCAAGGCAAAATGAGGGAGAT                   TGAAGAGGTTCTGACTCCAGAGATGCTAATGACGTGGAACAACTTGTTGCGGAAGAGG                   AATTTTTACAAGAAGCTAGAGTTGCATCTTCCCAAGTTCTCCATTTCTGGCTCCTATG                   TATTAGATCAGATTTTGCCCAGGCTGGGCTTCACGGATCTGTTCTCCAAGTGGGCTGA                   CTTATCCGGCATCACCAAACAGCAAAAACTGGAGGCATCCAAAAGTTTCCACAAGGCC                   ACCTTGGACGTGGATGAGGCTGGCACCGAGGCTGCAGCAGCCACCAGCTTCGCGATCA                   AATTCTTCTCTGCCCAGACGAATCGCCACATCCTGCGATTCAACCGGCCCTTCCTTGT                   GGTGATCTTTTCCACCAGCACCCAGAGTGTCCTCTTTCTGGGCAAGGTCGTCGACCCC                   ACGAAACCAGAATTC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 134   411 aa   MW at 46775.1kD                             NOV32h,    GSQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIF           166280730        Protein Sequence    FSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHG                   LETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRG                   KIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQ                   EHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKR                   NFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKA                   TLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDP                   TKPEF                  
 
     [0504] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 32B.  
               TABLE 32B                          Comparison of NOV32a against NOV32b through NOV32h.                                         Identities/                   Similarities for           Protein   NOV32a Residues/   the Matched           Sequence   Match Residues   Region                       NOV32b   21 . . . 427   387/407 (95%)                3 . . . 409   387/407 (95%)           NOV32c   21 . . . 427   387/407 (95%)                3 . . . 409   387/407 (95%)           NOV32d   21 . . . 427   387/407 (95%)                3 . . . 409   387/407 (95%)           NOV32e   21 . . . 427   387/407 (95%)                3 . . . 409   387/407 (95%)           NOV32f   21 . . . 427   387/407 (95%)                3 . . . 409   387/407 (95%)           NOV32g   21 . . . 427   387/407 (95%)                3 . . . 409   387/407 (95%)           NOV32h   21 . . . 427   387/407 (95%)                3 . . . 409   387/407 (95%)                      
 
     [0505] Further analysis of the NOV32a protein yielded the following properties shown in Table 32C.  
               TABLE 32C                       Protein Sequence Properties NOV32a                                        PSort   0.7809 probability located in outside; 0.4253 probability       analysis:   located in lysosome (lumen); 0.2787 probability located           in microbody (peroxisome); 0.1000 probability located           in endoplasmic reticulum (membrane)       SignalP   Cleavage site between residues 21 and 22       analysis:                  
 
     [0506] A search of the NOV32a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 32D.  
               TABLE 32D                          Geneseq Results for NOV32a                                         NOV32a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAE15747   Human protease inhibitor (PI)   1 . . . 427   425/427 (99%)   0.0           4 (kallistatin) protein -  Homo     1 . . . 427   426/427 (99%)             sapiens , 427 aa.           [WO200179227-A2, 25 OCT.           2001]       AAM02223   Peptide #905 encoded by probe   1 . . . 216   215/216 (99%)   e−120           for measuring human breast   1 . . . 216   215/216 (99%)           gene expression -  Homo               sapiens , 216 aa.           [WO200157270-A2, 09 AUG.           2001]       AAM26911   Peptide #948 encoded by probe   1 . . . 216   215/216 (99%)   e−120           for measuring placental gene   1 . . . 216   215/216 (99%)           expression -  Homo sapiens ,           216 aa. [WO200157272-A2,           09 AUG. 2001]       AAM14496   Peptide #930 encoded by probe   1 . . . 216   215/216 (99%)   e−120           for measuring cervical gene   1 . . . 216   215/216 (99%)           expression -  Homo sapiens ,           216 aa. [WO200157278-A2,           09 AUG. 2001]       AAM66622   Human bone marrow expressed   1 . . . 216   215/216 (99%)   e−120           probe encoded protein SEQ ID   1 . . . 216   215/216 (99%)           NO: 26928 -  Homo sapiens ,           216 aa. [WO200157276-A2,           09 AUG. 2001]                  
 
     [0507] In a BLAST search of public sequence datbases, the NOV32a protein was found to have homology to the proteins shown in the BLASTP data in Table 32E.  
               TABLE 32E                          Public BLASTP Results for NOV32a                                         NOV32a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q96BZ5   Hypothetical 48.5 kDa protein -   1 . . . 427   426/427 (99%)   0.0             Homo sapiens  (Human), 427 aa.   1 . . . 427   426/427 (99%)       P29622   Kallistatin precursor (Kallikrein   1 . . . 427   425/427 (99%)   0.0           inhibitor) (Protease inhibitor 4) -   1 . . . 427   426/427 (99%)             Homo sapiens  (Human), 427 aa.       P97569   Kallistatin -  Rattus norvegicus     1 . . . 425   241/425 (56%)         e−132           (Rat), 423 aa.   1 . . . 422   312/425 (72%)       O46519   Alpha-1-antitrypsin -  Equus     4 . . . 426   202/427 (47%)        9e−97             caballus  (Horse), 421 aa.   5 . . . 420   273/427 (63%)       O54760   Alpha-1-antitrypsin-like protein   4 . . . 426   201/427 (47%)        4e−96           CM55-SI precursor -  Tamias     5 . . . 412   269/427 (62%)             sibiricus  (Siberian chipmunk)           (Asian chipmunk), 413 aa.                  
 
     [0508] PFam analysis indicates that the NOV32a protein contains the domains shown in the Table 32F.  
               TABLE 32F                          Domain Analysis of NOV32a                                             Identities/                       Similarities for           Pfam   NOV32a Match   the Matched   Expect           Domain   Region   Region   Value                       serpin   48 . . . 424   193/397 (49%)   1.6e−171                   317/397 (80%)                      
 
     Example 33  
     [0509] The NOV33 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 33A.  
               TABLE 33A                       NOV33 Sequence Analysis                                                SEQ ID NO: 135   24 bp                     NOV33a,     TTT GTCCAAAACAGGCTGCAGCCG       CG57658-02       DNA Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 136   8 aa   MW at 1001.2 kD                     NOV33a,   FVQNRLQP       CG57658-02       Protein Sequence                             SEQ ID NO: 137   24 bp                     NOV33b,     TTT GTCTGCAACAGGCTGCAGCCG       CG57658-03       DNA Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 138   8 aa   MW at 976.2 kD                     NOV33b,   FVCNRLQP       CG57658-03       Protein Sequence                             SEQ ID NO: 139   24 bp                     NOV33c,     TTT GTCCAAAACACGCTGCAGCCG       CG57658-04       DNA Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 140   8 aa   MW at 946.1 kD                     NOV33c,   FVQNTLQP       CG57658-04       Protein Sequence                             SEQ ID NO: 141   24 bp                     NOV33d,     TTT GTCTGCAACACGCTGCAGCCG       CG57658-05       DNA Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 142   8 aa   MW at 921.1 kD                     NOV33d,   FVCNTLQP       CG57658-05       Protein Sequence                             SEQ ID NO: 143   24 bp                     NOV33e,     TTT GTCCAAAACACGCTGCAGGCG       CG57658-06       DNA Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 144   8 aa   MW at 920.0 kD                     NOV33e,   FVQNTLQA       CG57658-06       Protein Sequence                             SEQ ID NO: 145   24 bp                     NOV33f,     TTT GTCTGCAACACGCTGCAGGCG       CG57658-07       DNA Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 146   8 aa   MW at 895.0 kD                     NOV33f,   FVCNTLQA       CG57658-07       Protein Sequence                  
 
     [0510] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 33B.  
               TABLE 33B                          Comparison of NOV33a against NOV33b through NOV33f.                                         Identities/               NOV33a Residues/   Similarities for           Protein Sequence   Match Residues   the Matched Region                                         NOV33b   No Significant Alignment Found.                                 NOV33c   1 . . . 8   7/8 (87%)               1 . . . 8   7/8 (87%)                             NOV33d   No Significant Alignment Found.           NOV33e   No Significant Alignment Found.           NOV33f   No Significant Alignment Found.                      
 
     [0511] Further analysis of the NOV33a protein yielded the following properties shown in Table 33C.  
               TABLE 33C                       Protein Sequence Properties NOV33a                                                PSort analysis:               SignalP analysis:   No Known Signal Sequence Indicated                      
 
     [0512] A search of the NOV33a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 33D.  
               TABLE 33D                          Geneseq Results for NOV33a                                         NOV33a   Identities/               Protein/Organism/   Residues/   Similarities       Geneseq   Length   Match   for the   Expect       Identifier   [Patent #, Date]   Residues   Matched Region   Value                         No Significant Matches Found                  
 
     [0513] In a BLAST search of public sequence datbases, the NOV33a protein was found to have homology to the proteins shown in the BLASTP data in Table 33E.  
               TABLE 33E                          Public BLASTP Results for NOV33a                                         NOV33a   Identities/           Protein       Residues/   Similarities       Accession   Protein/Organism/   Match   for the   Expect       Number   Length   Residues   Matched Portion   Value                         No Significant Matches Found                  
 
     [0514] PFam analysis indicates that the NOV33a protein contains the domains shown in the Table 33F.  
               TABLE 33F                          Domain Analysis of NOV33a                                             Identities/                       Similarities           Pfam   NOV33a Match   for the   Expect           Domain   Region   Matched Region   Value                             No Significant Matches Found                  
 
     Example 34  
     [0515] The NOV34 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 34A.  
               TABLE 34A                       NOV34 Sequence Analysis                                                SEQ ID NO: 149   72 bp                     NOV34a,     CAG GAGACACGGAACGCCAAGGGC       CG57664-02   CACGCGCAGATTTACCGAGTGAAC       DNA   CTGCGGACCCTGCTCCGCTATTAC       Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 150   24 aa   MW at 2964.4 kD                     NOV34a,   QETRNAKGHAQIYRVNLRTLLRYY       CG57664-02       Protein       Sequence                  
 
     [0516] Further analysis of the NOV34a protein yielded the following properties shown in Table 34B.  
               TABLE 34B                       Protein Sequence Properties NOV34a                                        PSort   0.8500 probability located in lysosome (lumen); 0.5392       analysis:   probability located in nucleus; 0.1000 probability           located in mitochondrial matrix space; 0.0000           probability located in endoplasmic reticulum (membrane)       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0517] A search of the NOV34a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 34C.  
               TABLE 34C                          Geneseq Results for NOV34a                                         NOV34a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length [Patent   Match   the Matched   Expect       Identifier   #, Date]   Residues   Region   Value               AAM23917   Rhesus monkey EST encoded    1 . . . 24    24/24 (100%)   3e−07           protein SEQ ID NO: 1442 -  Macaca     125 . . . 148    24/24 (100%)             mulatta , 153 aa. [WO200154477-           A2, 02 AUG. 2001]       AAB58652   Murine class I H-2 protein #5 -  Mus      1 . . . 24   16/24 (66%)   0.025             musculus , 311 aa. [US6153408-A,   62 . . . 85   20/24 (82%)           28 NOV. 2000]       AAY52891   Murine class I molecule H-2D-d    1 . . . 24   16/24 (66%)   0.025           peptide SEQ ID NO: 69 - Mus sp,   62 . . . 85   20/24 (82%)           311 aa. [US5976551-A, 02 NOV.           1999]       AAY68237   Murine class I molecule protein SEQ    1 . . . 24   16/24 (66%)   0.025           ID NO: 69 - Mus sp, 311 aa.   62 . . . 85   20/24 (82%)           [US6011146-A, 04 JAN. 2000]       AAB58650   Murine class I H-2 protein #3 -  Mus      3 . . . 24   16/22 (72%)   0.043             musculus , 350 aa. [US6153408-A,   64 . . . 85   19/22 (85%)           28 NOV. 2000]                  
 
     [0518] In a BLAST search of public sequence datbases, the NOV34a protein was found to have homology to the proteins shown in the BLASTP data in Table 34D.  
               TABLE 34D                          Public BLASTP Results for NOV34a                                         NOV34a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q30714   MHC class I antigen Mamu B*06 -   1 . . . 24   19/24 (79%)   0.004             Macaca mulatta  (Rhesus macaque),   18 . . . 41    20/24 (83%)           294 aa.       Q95H92   Similar to histocompatibility 2, Q   1 . . . 24   17/24 (70%)   0.010           region locus 7 -  Mus musculus     89 . . . 112   21/24 (86%)           (Mouse), 332 aa.       Q31152   MHC class I Q4 beta-2-   1 . . . 24   17/24 (70%)   0.010           microglobulin (Qb-1) -  Mus     83 . . . 106   21/24 (86%)             musculus  (Mouse), 326 aa           (fragment).       Q9QYQ3   A1h -  Rattus norvegicus  (Rat), 346   1 . . . 24   17/24 (70%)   0.013           aa (fragment).   62 . . . 85    20/24 (82%)       Q951L1   MHC class I antigen -  Felis     1 . . . 24   17/24 (70%)   0.017             silvestris catus  (Cat), 62 aa   34 . . . 57    20/24 (82%)           (fragment).                  
 
     [0519] PFam analysis indicates that the NOV34a protein contains the domains shown in the Table 34E.  
               TABLE 34E                          Domain Analysis of NOV34a                                     Identities/                   Similarities           NOV34a Match   for the       Pfam Domain   Region   Matched Region   Expect Value               MHC_I   1 . . . 24   16/24 (67%)   6.1e−07                24/24 (100%)                  
 
     Example 35  
     [0520] The NOV35 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 35A.  
               TABLE 35A                       NOV35 Sequence Analysis                                                SEQ ID NO: 153   72 bp                     NOV35a,     CGG AACACACAGATCTGCAAGGCC       CG57668-02   CAAGCACGGACTGAACGAGAGAAC       DNA   CTGCGGATCGCGCTCCGCTACTAC       Sequence                             ORF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 154   24 aa   MW at 2967.4 kD                     NOV35a,   RNTQICKAQARTERENLRIALRYY       CG57668-02       Protein       Sequence                  
 
     [0521] Further analysis of the NOV35a protein yielded the following properties shown in Table 35B.  
               TABLE 35B                       Protein Sequence Properties NOV35a                                        PSort   0.8191 probability located in mitochondrial       analysis:   intermembrane space; 0.5581 probability located in           mitochondrial matrix space; 0.5500 probability located           in nucleus; 0.3285 probability located in lysosome           (lumen)       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0522] A search of the NOV35a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 35C.  
               TABLE 35C                          Geneseq Results for NOV35a                                         NOV35a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length [Patent   Match   the Matched   Expect       Identifier   #, Date]   Residues   Region   Value               AAM05915   Peptide #4597 encoded by probe for   1 . . . 24   24/24 (100%)   5e−07           measuring breast gene expression -   51 . . . 74    24/24 (100%)             Homo sapiens , 79 aa.           [WO200157270-A2, 09 AUG. 2001]       AAM18309   Peptide #4743 encoded by probe for   1 . . . 24   24/24 (100%)   5e−07           measuring cervical gene expression -   51 . . . 74    24/24 (100%)             Homo sapiens , 79 aa.           [WO200157278-A2, 09 AUG. 2001]       AAM70472   Human bone marrow expressed   1 . . . 24   24/24 (100%)   5e−07           probe encoded protein SEQ ID NO:   51 . . . 74    24/24 (100%)           30778 - Homo sapiens , 79 aa.           [WO200157276-A2, 09 AUG. 2001]       AAW33794   Peptide B2702.60-84 tested for   1 . . . 23   19/23 (82%)    3e−04           immunomodulating activity -   3 . . . 25   22/23 (95%)            Synthetic, 25 aa. [WO9744351-A1,           27 NOV. 1997]       AAR83090   HLA-B2702 CTL modulating   1 . . . 23   19/23 (82%)    3e−04           peptide (B2702.60-84) - Synthetic,   3 . . . 25   22/23 (95%)            25 aa. [WO9526979-A1, 12 OCT.           1995]                  
 
     [0523] In a BLAST search of public sequence datbases, the NOV35a protein was found to have homology to the proteins shown in the BLASTP data in Table 35D.  
               TABLE 35D                          Public BLASTP Results for NOV35a                                         NOV35a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Values               CAB22750   HLA-H PROTEIN -  Homo sapiens     1 . . . 24    24/24 (100%)   1e−06           (Human), 90 aa (fragment).   62 . . . 85     24/24 (100%)       HLHU12   MHC class I histocompatibility   1 . . . 24   23/24 (95%)   3e−06           antigen HLA alpha chain precursor   83 . . . 106   24/24 (99%)           (clone pHLA 12.4) - human, 359           aa.       CAB66931   Gogo-H protein -  Gorilla gorilla     1 . . . 24   23/24 (95%)   3e−06           (gorilla), 359 aa (fragment).   83 . . . 106   24/24 (99%)       CAB22754   HLA-H PROTEIN -  Homo sapiens     1 . . . 24   23/24 (95%)   3e−06           (Human), 90 aa (fragment).   62 . . . 85    24/24 (99%)       CAB22753   HLA-H PROTEIN -  Homo sapiens     1 . . . 24   23/24 (95%)   3e−06           (Human), 90 aa (fragment).   62 . . . 85    24/24 (99%)                  
 
     [0524] PFam analysis indicates that the NOV35a protein contains the domains shown in the Table 35E.  
               TABLE 35E                          Domain Analysis of NOV35a                                     Identities/                   Similarities           NOV35a Match   for the       Pfam Domain   Region   Matched Region   Expect Value               MHC_I   1 . . . 24   13/24 (54%)   0.00021               23/24 (96%)                  
 
     Example 36  
     [0525] The NOV36 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 36A.  
               TABLE 36A                       NOV36 Sequence Analysis                                                SEQ ID NO: 157   72 bp                     NOV36a,     GAG GAGACACGGAACACCAAGGCCC       CG59256-02   ACGCACAGACTGACAGAATGAACCT       DNA   GCAGACCCTGCGCGGCTACTAC       Sequence                             QRF Start: at 1   ORF Stop: end of sequence                                 SEQ ID NO: 158   24 aa   MW at 2897.2 kD                     NOV36a,   EETRNTKAHAQTDRMNLQTLRGYY       CG59256-02       Protein       Sequence                  
 
     [0526] Further analysis of the NOV36a protein yielded the following properties shown in Table 36B.  
               TABLE 36B                       Protein Sequence Properties NOV36a                                        PSort   0.8169 probability located in lysosome (lumen); 0.6500       analysis:   probability located in cytoplasm; 0.1000 probability           located in mitochondrial matrix space; 0.0000           probability located in endoplasmic reticulum (membrane)       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0527] A search of the NOV36a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 36C.  
               TABLE 36C                          Geneseq Results for NOV36a                                         NOV36a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/   Match   the Matched   Expect       Identifier   Length [Patent #, Date]   Residues   Region   Value               AAU79455   HLA-G recombinant protein 2 -    1 . . . 24   24/24 (100%)   2e−07             Homo sapiens , 234 aa.    93 . . . 116   24/24 (100%)           [WO200222784-A2, 21 MAR.           2002]       AAU79454   HLA-G recombinant protein 1 -    1 . . . 24   24/24 (100%)   2e−07             Homo sapiens , 326 aa.    93 . . . 116   24/24 (100%)           [WO200222784-A2, 21 MAR.           2002]       AAU79450   HLA-G alpha1 domain protein -    1 . . . 24   24/24 (100%)   2e−07             Homo sapiens , 92 aa.   64 . . . 87   24/24 (100%)           [WO200222784-A2, 21 MAR.           2002]       AAM48340   Human leukocyte antigen,    1 . . . 24   24/24 (100%)   2e−07           HLA-G7 -  Homo sapiens , 116    86 . . . 109   24/24 (100%)           aa. [WO200196564-A2, 20           DEC. 2001]       AAM02055   Peptide #737 encoded by probe    1 . . . 24   24/24 (100%)   2e−07           for measuring human breast   61 . . . 84   24/24 (100%)           gene expression -  Homo               sapiens , 89 aa. [WO200157270-           A2, 09 AUG. 2001]                  
 
     [0528] In a BLAST search of public sequence datbases, the NOV36a protein was found to have homology to the proteins shown in the BLASTP data in Table 36D.  
               TABLE 36D                          Public BLASTP Results for NOV36a                                         NOV36a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               CAD20672   Sequence 7 from Patent    1 . . . 24   24/24 (100%)   3e−07           WO0196564 -  Homo sapiens      86 . . . 109   24/24 (100%)           (Human), 116 aa.       Q31611   B2 microglobulin -  Homo sapiens      1 . . . 24   24/24 (100%)   3e−07           (Human), 246 aa.    86 . . . 109   24/24 (100%)       Q8WLP2   MHC-G protein -  Homo sapiens      1 . . . 24   24/24 (100%)   3e−07           (Human), 165 aa (fragment).   52 . . . 75   24/24 (100%)       Q8WLS1   HLA-G histocompatibility    1 . . . 24   24/24 (100%)   3e−07           antigen, class I, G -  Homo sapiens      86 . . . 109   24/24 (100%)           (Human), 338 aa.       Q95391   HLA-G -  Homo sapiens (Human),    1 . . . 24   24/24 (100%)   3e−07           182 aa (fragment).   62 . . . 85   24/24 (100%)                  
 
     [0529] PFam analysis indicates that the NOV36a protein contains the domains shown in the Table 36E.  
               TABLE 36E                          Domain Analysis of NOV36a                                             Identities/                       Similarities for           Pfam   NOV36a   the Matched   Expect           Domain   Match Region   Region   Value                       MHC_I   1 . . . 24   13/24 (54%)   2.1e−05                   23/24 (96%)                      
 
     Example 37  
     [0530] The NOV37 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 37A.  
               TABLE 37A                       NOV37 Sequence Analysis                                                    SEQ ID NO: 161   555 bp                             NOV37a,    ATGCACAGCCACCGCGACTTCCAGCCGGTGCTCCACCTGGTTGCGCTCAACAGCCCCC           CG59437-01       DNA Sequence   TGTCAGGCGGCATGCGGGGCATCCGCGGGGCCGACTTCCAGTGCTTCCAGCAGGCGCG                   GGCCGTGGGGCTGGCGGGCACCTTCCGCGCCTTCCTGTCCTCGCGCCTGCACGACCTG                   TACAGCATCGTGCGCCGTGCCGACCGCGCAGCCGTGCCCATCGTCAACCTCAAGGACG                   AGCTGCTGTTTCCCAGCTGGGAGGCTCTGTTCTCAGGCTCTGAGGGTCCGCTGAAGCC                   CGGGGCACGCATCTTCTCCTTTAACGGCAAGGACGTCCTGACCCACCCCACCTGGCCC                   CAGAAGAGCGTGTGGCATGGCTCGGACCCCAACGGGCGCAGGCTGACCGAGAGCTACT                   GTGAGACGTGGCGGACGGAGGCTCCCTCGGCCACGGGCCAGGCCTACTCGCTGCTGGG                   GGGCAGGCTCCTGGGGCAGAGTGCCGCGAGCTGCCATCACGCCTACATCGTGCTATGC                   ATTGAGAACAGCTTCATGACTGCCTCCPAGTAG                                         ORF Start: ATG at 1   ORF Stop: TAG at 553                                         SEQ ID NO: 162   184 aa   MW at 20246.8kD                             NOV37a,    MHSHRDPQPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDL           CG59437-01       Protein Sequence    YSIVRRADRAAVPIVNLKDELLFPSWEALFSGSEGPLKPGARTFSFNGKDVLTHPTWP                   QKSVWHGSDPNGRRLTESYCETWRTEAPSATGQAYSLLGGRLLGQSAASCHHAYIVLC                   IENSFMTASK                                         SEQ ID NO: 163   482 bp                             NOV37b,      GG ATCCGGCATGCGGGGCATCCGCGGGGCCGACTTCCAGCGCTTCCACCAGGCGCGGA           170108827 DNA       Sequence    AGGTGCCCGCCAGCCCCACGGCCCGCGCCTGCAGGACCTGTACAGCATCGTGCGCCGT                   GCCGACCGCGCAGCCGTGCCCATCGTCAACCTCAAGGACGAGCTGCTGTTTCCCAGCT                   GGGAGGCCCTGTTCTCAGGCTCTGAGGGTCCGCTGAAGCCCGGGGCACGCATCTTCTC                   CTTTGACGGCAAGGACGTCCTGAGGCACCCCACCTGGCCCCAGAAGAGCGTGTGGCAT                   GGCTCGGACCCCAACGGGCCCAGGCTGACCGAGAGCTACTGTGAGACGTGGCGGACGG                   AGGCTCCCTCGGCCACGGGCCAGCCCTCCTCGCTGCTGGGGGGCAGGCTCCTGGGGCA                   GAGTGCCGCGAGCTGCCATCACGCCTACATCGTGCTCTGCATTGAGAACAGCTTCATG                   ACTGCCTCCAAGCTCGAG                                         ORF Start: at 3   ORF Stop: end of sequence                                         SEQ ID NO: 164   160 aa   MW at 17488.6kD                             NOV37b,    IRHAGHPRGRLPALPAGAEGARQPHGPRLQDLYSIVRRADRAAVPIVNLKDELLFPSW           170108827       Protein Sequence    EALFSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTE                   APSATGQASSLLGGRLLGQSAASCHHAYIVLCIENSFMTASKLE                                         SEQ ID NO: 165   480 bp               NOV37c,    GGATCCGGCATGCGGGGCATCCGCGGGGCCGACTTCCAGTGCTTCCAGCAGGCGCGGA           170108863 DNA           Sequence    AGGTGCCCGCCAGCCCCACGGCCCGCGCCTGCAGGACCTGTACAGCATCGTGCGCCGT                           GCCGACCGCGCAGCCGTGCCCATCGTCAACCTCAAGGACGAGCTGCTQTTTCCCAGCT                           GGGAGGCTCTGTTCTCAGGCTGAGGGTCCGCTGAAGCCCGGGGCACCCATCTTCTCCT                           TTGACCGCAAGGACGTCCTGAGGCACCCCACCTCGCCCCAGAAGAGCGTGTGGCATGG                           CTCGGACCCCAACGGGCGCAGGCTGACCGAGAGCTACTGTGAGACGTGGCGGACGGAG                           GCTCCCTCGGCCACGGGCCAGGCCTCCTCCCTGCTGGGGGGCAGGCTCCTGGCGCAGA                           GTCCCGCGAGCTGCCATCACGCCTACATCGTGCTCTGCATTGAGAACAGCTTCATGAC                           TGCCTCCAAGCTCGAG                       ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 166   160 aa   MW at 17082.1kD                             NOV37c,    GSGMRGIRGADFQCFQQARKVPASPTARACRTCTASCAVPTAQPCPSSTSRTSCCFPA           170108863       Protein Sequence    GRLCSQAEGPLKPGARIFSFDGKDVLRHRTWPQKSVWHGSDPNGRRLTESYCETWRTE                   APSATGQASSLLGGRLLGQSAASCHHAYIVLCIENSFNTASKLE                  
 
     [0531] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 37B.  
               TABLE 37B                          Comparison of NOV37a against NOV37b and NOV37c.                                 Identities/               Similarities for       Protein   NOV37a Residues/   the Matched       Sequence   Match Residues   Region               NOV37b   54 . . . 184   111/131 (84%)           28 . . . 158   112/131 (84%)       NOV37c   23 . . . 184    95/162 (58%)            3 . . . 158    99/162 (60%)                  
 
     [0532] Further analysis of the NOV37a protein yielded the following properties shown in Table 37C.  
               TABLE 37C                       Protein Sequence Properties NOV37a                                        PSort   0.7480 probability located in microbody (peroxisome);       analysis:   0.2213 probability located in lysosome (lumen); 0.1000           probability located in mitochondrial matrix space;           0.0000 probability located in endoplasmic reticulum           (membrane)       SignalP   No Known Signal Sequence Indicated       analysis:                  
 
     [0533] A search of the NOV37a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 37D.  
               TABLE 37D                          Geneseq Results for NOV37a                                         NOV37a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent#, Date]   Residues   Region   Value               AAU76689   Synthetic plasmid pEnd-HR#1 FPD   2 . . . 184   180/183 (98%)   e−103           fusion protein sequence - Chimeric -   93 . . . 275    181/183 (98%)           Mus sp, 275 aa. [WO200210372-           A1, 07 FEB. 2002]       AAU76688   Human collagen XVIII 1alpha NCI   2 . . . 184   180/183 (98%)   e−103           domain protein sequence -  Homo     128 . . . 310    181/183 (98%)             sapiens , 310 aa. [WO200210372-           A1, 07 FEB. 2002]       AAM49503   Human endostatin protein -  Homo     2 . . . 184   180/183 (98%)   e−103             sapiens , 183 aa. [CN1177005-A,   1 . . . 183   181/183 (98%)           25 MAR. 1998]       AAM48895   Human endostatin protein -  Homo     2 . . . 184   180/183 (98%)   e−103             sapiens , 183 aa. [WO200193897-   1 . . . 183   181/183 (98%)           A2, 13 DEC. 2001]       AAB49379   Human endostatin SEQ ID NO: 2 -   2 . . . 184   180/183 (98%)   e−103             Homo sapiens , 183 aa.   1 . . . 183   181/183 (98%)           [WO200067771-A1, 16 NOV.           2000]                  
 
     [0534] In a BLAST search of public sequence datbases, the NOV37a protein was found to have homology to the proteins shown in the BLASTP data in Table 37E.  
               TABLE 37E                          Public BLASTP Results for NOV37a                                         NOV37a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               A53019   collagen alpha 1(XVIII) chain -    2 . . . 184   180/183 (98%)   e−103           human, 684 aa (fragment).   502 . . . 684   181/183 (98%)       AAM52249   Multi-functional protein MFP -    2 . . . 184   180/183 (98%)   e−103             Homo sapiens  (Human), 261 aa.    79 . . . 261   181/183 (98%)       Q8WX15   Collagen XVIII -  Homo sapiens      2 . . . 184   180/183 (98%)   e−103           (Human), 187 aa (fragment).    5 . . . 187   181/183 (98%)       P39060   Collagen alpha 1(XVIII) chain    2 . . . 184   180/183 (98%)   e−103           precursor [Contains: Endostatin] -   1334 . . . 1516   181/183 (98%)             Homo sapiens (Human), 1516 aa.       B56101   collagen alpha 1(XVIII) chain    2 . . . 182   152/181 (83%)   4e−88            precursor, long splice form -   1591 . . . 1771   168/181 (91%)           mouse, 1774 aa.                  
 
     [0535] PFam analysis indicates that the NOV37a protein contains the domains shown in the Table 37F.  
               TABLE 37F                          Domain Analysis of NOV37a                                             Identities/                       Similarities for           Pfam   NOV37a   the Matched   Expect           Domain   Match Region   Region   Value                             No Significant Matches Found                  
 
     Example 38  
     [0536] The NOV38 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 38A.  
               TABLE 38A                       NOV38 Sequence Analysis                                                    SEQ ID NO: 167   678 bp                             NOV38a,      GCTGCTGCAGTTGCCATGGTACAAGGGATGGGTTGTGGATTAGAGTTGGCATACTTGG             CG59739-01       DNA Sequence      CAGCCCGCTGCTTGATGAATGCAGCCAACAGCTGGGGGTTGGCGTGAAGGATACTAAG                       CACCTGTCGCTGCTGCAGTTGCCATGGTGACAAGGGTTGCTGGCACAAGGATCTGCAA                       CAAGCTGGCAGCTAGAATTCAGCGGCCGCTGAATTCTAGCTTCAACTTCACTACTTCT                       GTAGTCTCATCTTGAGTAAAAGAGAACCCAGCCAACT ATGAAGTTCCTTGTCTTTGCC                   TTCATCTTGGCTCTCATGGTTTCCATGATTGGAGCTGATTCATCTGAAGAGAAATTTT                   TGCGTAGAATTGGAAGATTCGGTTATGGGTATGGCCCTTATCAGCCAGTTCCAGAACA                   ACCACTATACCCACAACCATACCAACCACAATACCAACAATATACCTTTTAA TATCAT                       CAGTAACTGCAGGACATGATTATTGAGGCTTGATTGGCAAATACGACTTCTACATCCA                       TATTCTCATCTTTCATACCATATCACACTACTACCACTTTTTGAAGAATCATCAAAGA                       GCAATGCAAATGAAAAACACTATAATTTACTGTATACTCTTTGTTTCAGGATACTTGC                       CTTTTCAATTGTCACTTGATCATATAATTGCATTTAAACT                                           ORF Start: ATG at 270   ORF Stop: TAA at 456                                         SEQ ID NO: 168   62 aa   MW at 7304.4kD                             NOV38a,    MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQ           CG59739-01        Protein Sequence    QYTF                                         SEQ ID NO: 169   141 bp                             NOV38 b,    GGATCCGATTCATCTGAAGAGAAATTTTTGCGTAGAATTGGAAGATTCGGTTATGGGT           169679148 DNA       Sequence    ATGGCCCTTATCAGCCAGTTCCAGAACAACCACTATACCCACAACCATACCAACCACA                   ATACCAACAATATACCTTTCTCGAG                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 170   47 aa   MW at 5606.1kD                             NOV38b   GSDSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTFLE           169679148        Protein Sequence                  
 
     [0537] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table 38B.  
               TABLE 38B                          Comparison of NOV38a against NOV38b.                             NOV38a   Identities/           Residues/   Similarities       Protein   Match   for the       Sequence   Residues   Matched Region               NOV38b   18 . . . 38   20/21 (95%)            1 . . . 21   21/21 (99%)                  
 
     [0538] Further analysis of the NOV38a protein yielded the following properties shown in Table 38C.  
               TABLE 38C                       Protein Sequence Properties NOV38a                                                PSort   0.8200 probability located in outside;           analysis:   0.3016 probability located in microbody               (peroxisome); 0.1000 probability located               in endoplasmic reticulum (membrane);               0.1000 probability located in endoplasmic               reticulum (lumen)           SignalP   Cleavage site between residues 20 and 21           analysis:                      
 
     [0539] A search of the NOV38a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 38D.  
               TABLE 38D                          Genesq Results for NOV38a                                         NOV38a   Identities/                   Residues/   Similarities       Genesp   Protein/Organism/Length [Patent   Match   for the   Expect       Identifier   #, Date]   Residues   Matched Region   Value               AAY94527   Human statherin protein -  Homo     1 . . . 62   62/62 (100%)   9e−32             sapiens , 62 aa. [WO200024779-A1   1 . . . 62   62/62 (100%)           04 MAY 2000]       AAB42456   Human ORFX ORF2220   3 . . . 62   54/67 (80%)    2e−24           polypeptide sequence SEQ ID   16 . . . 82    56/67 (82%)            NO: 4440 -  Homo sapiens , 82 aa.           [WO200058473-A2, 05 OCT. 2000]       AAG80022   Strathin homologue peptide   33 . . . 47    15/15 (100%)   0.002           fragment - Unidentified, 15 aa.   1 . . . 15   15/15 (100%)           [DE10017249-A1, 11 OCT. 2001]       AAW90168   BK-RiV plant stratherin peptide   33 . . . 47    15/15 (100%)   0.002           fragment homologue - Unknown, 15   1 . . . 15   15/15 (100%)           aa. [EP889053-A2, 07 JAN. 1999]       AAU90983   Transplant media associated   1 . . . 25   17/25 (68%)    0.033           antimicrobial peptide #19 -  Homo     1 . . . 25   20/25 (80%)              sapiens , 51 aa. [WO200209738-A1,           07 FEB. 2002]                  
 
     [0540] In a BLAST search of public sequence datbases, the NOV38a protein was found to have homology to the proteins shown in the BLASTP data in Table 38E.  
               TABLE 38E                          Public BLASTP Results for NOV38a                                             Identities/                   NOV38a   Similarities       Protein       Residues/   for the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               P02808   Statherin precursor -  Homo sapiens     1 . . . 62    62/62 (100%)   2e−31           (Human), 62 aa.   1 . . . 62    62/62 (100%)       P02809   Statherin precursor -  Macaca     1 . . . 60   38/61 (62%)   6e−14             fascicularis  (Crab eating macaque)   1 . . . 61   39/61 (63%)           (Cynomolgus monkey), 61 aa.       P14709   Statherin -  Macaca arctoides  (Stump-   20 . . . 60    30/42 (71%)   6e−10           tailed macaque), 42 aa.   1 . . . 42   31/42 (73%)       P15515   Histatin 1 precursor (Histidine-rich   1 . . . 25   17/25 (68%)   0.015           protein 1) (Post-PB protein) (PPB)   1 . . . 25   21/25 (84%)           [Contains: Histatin 2] -  Homo sapiens             (Human), 57 aa.       P15516   Histatin 3 precursor (Histidine-rich   1 . . . 25   17/25 (68%)   0.075           protein 3) (PB) (Basic histidine-rich   1 . . . 25   20/25 (80%)           protein) [Contains: Histatins 4 to 12] -             Homo sapiens  (Human), 51 aa.                  
 
     [0541] PFam analysis indicates that the NOV38a protein contains the domains shown in the Table 38F.  
               TABLE 38F                          Domain Analysis of NOV38a                                             Identities/                       Similarities               NOV38a   for the           Pfam   Match   Matched   Expect           Domain   Region   Region   Value                             No Significant Matches Found                  
 
     Example 39  
     [0542] The NOV39 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 39A.  
               TABLE 39A                       NOV39 Sequence Analysis                                                    SEQ ID NO: 171   72 bp                             NOV39a,    CTACAGACACTGGGCGCCAAGGCCCAGGCACAGACTGACCGAGTGAACCTGCGGACCC           CG94630-02        DNA Sequence    TGCTCCGCTACTAC                                         ORF Start: at 1   ORF Stop: end of sequence                                         SEQ ID NO: 172   24 aa   MW at 2793.2kD                             NOV39a.    LQTLGAKAQAQTDRVNLRTLLRYY           CG94630-02        Protein Sequence                  
 
     [0543] Further analysis of the NOV39a protein yielded the following properties shown in Table 39B.  
               TABLE 39B                       Protein Sequence Properties NOV39a                                                PSort   0.8500 probability located in lysosome           analysis:   (lumen); 0.7847 probability located in               mitochondrial intermembrane space;               0.4500 probability located in cytoplasm;               0.4488 probability located in               mitochondrial matrix space           SignalP   No Known Signal Sequence Indicated           analysis:                      
 
     [0544] A search of the NOV39a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 39C.  
               TABLE 39C                          Geneseq Results for NOV39a                                             Identities/                   NOV39a   Similarities               Residues/   for the       Geneseq   Protein/Organism/Length [Patent #,   Match   Matched   Expect       Identifier   Date]   Residues   Region   Value               AAP70155   Sequence encoded by genomic DNA   2 . . . 24   16/23 (69%)   0.17           encoding human histocompatibility   87 . . . 109   19/23 (82%)           antigen HLA-B 27 -  Homo sapiens ,           362 aa. [EP226069-A, 24 JUN. 1987]       AAM23917   Rhesus monkey EST encoded protein   2 . . . 24   16/23 (69%)   0.22           SEQ ID NO: 1442 -  Macaca mulatta ,   126 . . . 148    17/23 (73%)           153 aa. [WO200154477-A2, 02 AUG.           2001]       AAU79455   HLA-G recombinant protein 2 -  Homo     2 . . . 24   14/23 (60%)   0.85             sapiens , 234 aa. [WO200222784-A2,   94 . . . 116   17/23 (73%)           21 MAR. 2002]       AAU79454   HLA-G recombinant protein 1 -  Homo     2 . . . 24   14/23 (60%)   0.85             sapiens , 326 aa. [WO200222784-A2,   94 . . . 116   17/23 (73%)           21 MAR. 2002]       AAU79450   HLA-G alpha1 domain protein -   2 . . . 24   14/23 (60%)   0.85             Homo sapiens , 92 aa.   65 . . . 87    17/23 (73%)           [WO200222784-A2, 21 MAR. 2002]                  
 
     [0545] In a BLAST search of public sequence datbases, the NOV39a protein was found to have homology to the proteins shown in the BLASTP data in Table 39D.  
               TABLE 39D                          Public BLASTP Results for NOV39a                                             Identities/                   NOV39a   Similarities       Protein       Residues/   for the       Accession       Match   Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q30175   MHC class I HLA-J antigen -   1 . . . 24    24/24 (100%)   4e−06             Homo sapiens  (Human), 218 aa   85 . . . 108    24/24 (100%)           (fragment).       Q8WW48   Hypothetical 28.9 kDa protein -   1 . . . 24    24/24 (100%)   4e−06             Homo sapiens  (Human), 264 aa   89 . . . 112    24/24 (100%)           (fragment).       Q95533   Class I histocompatibility antigen -   3 . . . 24   18/22 (81%)   0.013             Pan troglodytes  (Chimpanzee), 137   29 . . . 50    18/22 (81%)           aa (fragment).       Q9MXK1   MHC class I antigen -  Pan     3 . . . 24   18/22 (81%)   0.013             troglodytes  (Chimpanzee), 362 aa.   88 . . . 109   18/22 (81%)       Q95430   MHC class I -  Pongo pygmaeus     2 . . . 24   18/23 (78%)   0.017           (Orangutan), 354 aa (fragment).   79 . . . 101   20/23 (86%)                  
 
     [0546] PFam analysis indicates that the NOV39a protein contains the domains shown in the Table 39E.  
               TABLE 39E                          Domain Analysis of NOV39a                                             Identities/                   NOV39a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                       MHC_I   2 . . . 24   15/23 (65%)   7.1e−05                   21/23 (91%)                      
 
     Example 40  
     [0547] The NOV40 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table 40A.  
               TABLE 40A                       NOV40 Sequence Analysis                                                    SEQ ID NO: 175   1513 bp                             NOV40a,      TCGCG ATGCTGCTGCGCCTGTTGCTGGCCTGGGCGGCCGCAGGGCCCACACTGGGCCA           CG95205-02       DNA Sequence    GGACCCCTGGGCTGCTGAGCCCCGTGCCGCCTGCGGCCCCAGCAGCTGCTACGCTCTC                   TTCCCACGGCGCCGCACCTTCCTGGAGGCCTGGCGCGCCTGCCGCGAGCTGGGGGGCG                   ACCTGGCCACTCCTCGGACCCCCGAGGAGGCCCAGCGTGTGGACAGCCTGGTGGGTGC                   GGGCCCAGCCAGCCGGCTGCTGTGGATCGGCCTGCAGCGGCAGGCCCGGCAATGCCAG                   CTGCAGCGCCCACTGCGCGGCTTCACGTGGACCACAGGGGACCAGGACACGGCTTTCA                   CCAACTGGGCCCAGCCAGCCTCTGGAGGCCCCTGCCCGGCCCAGCGCTCTGTGGCCCT                   GGAGGCAAGTGGCGAGCACCGCTGGCTGGAGGGCTCGTGCACCCTGGCTGTCGACGGC                   TACCTGTGCCAGTTTGGCTTCGAGGGCGCCTGCCCGGCGCTGCAAGATGAGGCGGGCC                   AGGCCGGCCCAGCCGTGTATACCACGCCCTTCCACCTGGTCTCCACAGAGTTTGAGTG                   GCTGCCCTTCGGCTCTGTGGCCGCTGTGCAGTGCCAGGCTGGCAGGGGAGCCTCTCTG                   CTCTGCGTGAAGCAGCCTGAGGGAGGTGTGGGCTGGTCACGGGCTGGGCCCCTGTGCC                   TGGGGACTGGCTGCAGCCCTGACAACGGCGGCTGCGAACACGAATGTGTGGAGGAGGT                   GGATGGTCACGTGTCCTGCCGCTGCACTGAGGGCTTCCGGCTGGCAGCAGACGGGCGC                   AGTTGCGAGCACCCCTGTGCCCAGGCTCCGTGCGAGCAGCAGTGTGAGCCCGGTGGGC                   CACAAGGCTACAGCTGCCACTGTCGCCTCGGTTTCCGGCCAGCGGAGGATGATCCGCA                   CCGCTGTGTGGACACAGATGAGTGCCAGATTGCCGGTGTGTGCCAGCAGATGTGTGTC                   AACTACGTTGCTGGCTTCGAGTGTTATTGTAGCGAGGGACATGAGCTGGAGGCTCATG                   GCATCAGCTGCAGCCCTGCAGGGGCCATGGGTGCCCAGGCTTCCCAGGACCTCGGAGA                   TGAGTTGCTGGATGACGCGGAGGATGAGGAAGATGAAGACGAGGCCTGGAAGGCCTTC                   AACGGTGGCTGGACGGAGATGCCTGGGATCCTGTGGATGGAGCCTACGCAGCCGCCTG                   ACTTTGCCCTGGCCTATAGACCGAGCTTCCCAGAGGACAGAGAGCCACAGATACCCTA                   CCCGGAGCCCACCTGGCCACCCCCGCTGCCCAGCTGGACAGATGGCTTCCTGCTCCCC                   AGGCCCAGCCAGGGTCCTCTCTCAACCACTAGACTTGGCTCTCAGGAACTCTGCTTCC                   TGGCCCAGCGCTCGTGA CCAAGGATACACCAAAGCCCTTAAGACCTCAGGGGGCGGGT                       GCTGGGGTCTTCTCCAATAAATGGGGTGTCACCCTTAAAAAAAAAAAAAAAAAAAAAA                       AAAAA                                           ORF Start: ATG at 6   ORF Stop: TGA at 1407                                         SEQ ID NO: 176   467 aa   MW at 50389.6kD                             NOV40a,    MLLRLLLAWAAAGPTLGQDPWAAEPRAACGPSSCYALFPRRRTFLEAWRACRELGGDL           CG95205-02       Protein Sequence   ATPRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQLQRPLRGFTWTTGDQDTAFTN                   WAQPASGGPCPAQRCVALEASGEHRWLEGSCTLAVDGYLCQEGFEGACPALQDEAGQA                   GPAVYTTPFHLVSTEFEWLPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLG                   TGCSPDNGGCEHECVEEVDGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQ                   GYSCHCRLGFRPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGI                   SCSPAGAMGAQASQDLGDELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDF                   ALAYRPSFPEDREPQIPYPEPTWPPPLPSWTDGFLLPRPSQGPLSTTRLGSQELCFLA                   QRS                  
 
     [0548] Further analysis of the NOV40a protein yielded the following properties shown in Table 40B.  
               TABLE 40B                       Protein Sequence Properties NOV40a                                                PSort   0.3700 probability located in outside;           analysis:   0.1440 probability located in microbody               (peroxisome); 0.1000 probability               located in endoplasmic reticulum               (membrane); 0.1000 probability located               in endoplasmic reticulum (lumen)           SignalP   Cleavage site between residues 18 and 19           analysis:                      
 
     [0549] A search of the NOV40a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table 40C.  
               TABLE 40C                          Geneseq Results for NOV40a                                         NOV40a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABB90732   Human Tumour Endothelial Marker   1 . . . 433    433/433 (100%)   0.0           polypeptide SEQ ID NO 196 -   1 . . . 433    433/433 (100%)             Homo sapiens , 757 aa.           [WO200210217-A2, 07 FEB. 2002]       ABB90721   Human Tumour Endothelial Marker   1 . . . 433    433/433 (100%)   0.0           polypeptide SEQ ID NO 177 -   1 . . . 433    433/433 (100%)             Homo sapiens , 757 aa.           [WO200210217-A2, 07 FEB. 2002]       ABB90780   Mouse Tumour Endothelial Marker   1 . . . 433   382/433 (88%)   0.0           polypeptide SEQ ID NO 291 -  Mus     1 . . . 433   397/433 (91%)             musculus , 765 aa. [WO200210217-           A2, 07 FEB. 2002]       ABB90727   Mouse Tumour Endothelial Marker   1 . . . 433   382/433 (88%)   0.0           polypeptide SEQ ID NO 190 -  Mus     1 . . . 433   397/433 (91%)             musculus , 765 aa. [WO200210217-           A2, 07 FEB. 2002]       AAE05343   Mouse tumour endothelial marker I   3 . . . 464   388/469 (82%)   0.0           precursor protein - Mus sp, 492 aa.   1 . . . 469   408/469 (86%)           [WO200148192-A1, 05 JUL. 2001]                  
 
     [0550] In a BLAST search of public sequence datbases, the NOV40a protein was found to have homology to the proteins shown in the BLASTP data in Table 40D.  
               TABLE 40D                          Public BLASTP Results for NOV40a                                         NOV40a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q9HCU0   Tumor endothelial marker I   1 . . . 433    433/433 (100%)   0.0           precursor (Endosialin protein) -   1 . . . 433    433/433 (100%)             Homo sapiens  (Human), 757 aa.       Q91V98   Tumor endothelial marker I   1 . . . 433   382/433 (88%)   0.0           precursor (Endosialin) -  Mus     1 . . . 433   397/433 (91%)             musculus  (Mouse), 765 aa.       Q91ZV1   Endosialin -  Mus musculus     1 . . . 433   382/433 (88%)   0.0           (Mouse), 765 aa.   1 . . . 433   397/433 (91%)       Q96KB6   CDNA FLJ14384 fis, clone   325 . . . 433     109/109 (100%)   2e−64           HEMBA1002150 -  Homo sapiens     1 . . . 109    109/109 (100%)           (Human), 433 aa.       THHUB   thrombomodulin precursor   2 . . . 352   147/375 (39%)   2e−54           [validated] - human, 575 aa.   1 . . . 365   184/375 (48%)                  
 
     [0551] PFam analysis indicates that the NOV40a protein contains the domains shown in the Table 40E.  
               TABLE 40E                          Domain Analysis of NOV40a                                             Identities/                   NOV40a   Similarities for           Pfam   Match   the Matched   Expect           Domain   Region   Region   Value                                                 Xlink   43 . . . 61    9/19 (47%)   0.034                   15/19 (79%)           lectin_c    40 . . . 158   29/134 (22%)    8.4e−06                   80/134 (60%)            sushi   176 . . . 230   15/66 (23%)   0.72                   39/66 (59%)           EGF   235 . . . 271   13/47 (28%)   4.6e−06                   31/47 (66%)           TIL   258 . . . 316   19/74 (26%)   0.17                   40/74 (54%)           EGF   316 . . . 350   13/47 (28%)   0.00035                   26/47 (55%)                      
 
     Example B  
     [0552] Sequencing Methodology and Identification of NOVX Clones  
     [0553] 1. GeneCalling™ Technology: This is a proprietary method of performing differential gene expression profiling between two or more samples developed at CuraGen and described by Shimkets, et al., “Gene expression analysis by transcript profiling coupled to a gene database query” Nature Biotechnology 17:198-803 (1999). cDNA was derived from various human samples representing multiple tissue types, normal and diseased states, physiological states, and developmental states from different donors. Samples were obtained as whole tissue, primary cells or tissue cultured primary cells or cell lines. Cells and cell lines may have been treated with biological or chemical agents that regulate gene expression, for example, growth factors, chemokines or steroids. The cDNA thus derived was then digested with up to as many as 120 pairs of restriction enzymes and pairs of linker-adaptors specific for each pair of restriction enzymes were ligated to the appropriate end. The restriction digestion generates a mixture of unique cDNA gene fragments. Limited PCR amplification is performed with primers homologous to the linker adapter sequence where one primer is biotinylated and the other is fluorescently labeled. The doubly labeled material is isolated and the fluorescently labeled single strand is resolved by capillary gel electrophoresis. A computer algorithm compares the electropherograms from an experimental and control group for each of the restriction digestions. This and additional sequence-derived information is used to predict the identity of each differentially expressed gene fragment using a variety of genetic databases. The identity of the gene fragment is confirmed by additional, gene-specific competitive PCR or by isolation and sequencing of the gene fragment.  
     [0554] 2. SeqCalling™ Technology: cDNA was derived from various human samples representing multiple tissue types, normal and diseased states, physiological states, and developmental states from different donors. Samples were obtained as whole tissue, primary cells or tissue cultured primary cells or cell lines. Cells and cell lines may have been treated with biological or chemical agents that regulate gene expression, for example, growth factors, chemokines or steroids. The cDNA thus derived was then sequenced using CuraGen&#39;s proprietary SeqCalling technology. Sequence traces were evaluated manually and edited for corrections if appropriate. cDNA sequences from all samples were assembled together, sometimes including public human sequences, using, bioinformatic programs to produce a consensus sequence for each assembly. Each assembly is included in CuraGen Corporation&#39;s database. Sequences were included as components for assembly when the extent of identity with another component was at least 95% over 50 bp. Each assembly represents a gene or portion thereof and includes information on variants, such as splice forms single nucleotide polymorphisms (SNPs), insertions, deletions and other sequence variations.  
     [0555] 3. PathCalling™ Technology: The NOVX nucleic acid sequences are derived by laboratory screening of cDNA library by the two-hybrid approach. cDNA fragments covering either the full length of the DNA sequence, or part of the sequence, or both, are sequenced. In silico prediction was based on sequences available in CuraGen Corporation&#39;s proprietary sequence databases or in the public human sequence databases, and provided either the full length DNA sequence, or some portion thereof.  
     [0556] The laboratory screening was performed using the methods summarized below:  
     [0557] cDNA libraries were derived from various human samples representing multiple tissue types, normal and diseased states, physiological states, and developmental states from different donors. Samples were obtained as whole tissue, primary cells or tissue cultured primary cells or cell lines. Cells and cell lines may have been treated with biological or chemical agents that regulate gene expression, for example, growth factors, chemokines or steroids. The cDNA thus derived was then directionally cloned into the appropriate two-hybrid vector (Gal4-activation domain (Gal4-AD) fusion). Such cDNA libraries as well as commercially available cDNA libraries from Clontech (Palo Alto, Calif.) were then transferred from  E. coli  into a CuraGen Corporation proprietary yeast strain (disclosed in U.S. Pat. Nos. 6,057,101 and 6,083,693, incorporated herein by reference in their entireties).  
     [0558] Gal4-binding domain (Gal4-BD) fusions of a CuraGen Corportion proprietary library of human sequences was used to screen multiple Gal4-AD fusion cDNA libraries resulting in the selection of yeast hybrid diploids in each of which the Gal4-AD fusion contains an individual cDNA. Each sample was amplified using the polymerase chain reaction (PCR) using non-specific primers at the cDNA insert boundaries. Such PCR product was sequenced; sequence traces were evaluated manually and edited for corrections if appropriate. cDNA sequences from all samples were assembled together, sometimes including public human sequences, using bioinformatic programs to produce a consensus sequence for each assembly. Each assembly is included in CuraGen Corporation&#39;s database. Sequences were included as components for assembly when the extent of identity with another component was at least 95% over 50 bp. Each assembly represents a gene or portion thereof and includes information on variants such as splice forms single nucleotide polymorphisms (SNPs), insertions, deletions and other sequence variations.  
     [0559] Physical clone: the cDNA fragment derived by the screening procedure, covering the entire open reading frame is, as a recombinant DNA, cloned into pACT2 plasmid (Clontech) used to make the cDNA library. The recombinant plasmid is inserted into the host and selected by the yeast hybrid diploid generated during the screening procedure by the mating of both CuraGen Corporation proprietary yeast strains N106′ and YULH (U.S. Pat. Nos. 6,057,101 and 6,083,693).  
     [0560] 4. RACE: Techniques based on the polymerase chain reaction such as rapid amplification of cDNA ends (RACE), were used to isolate or complete the predicted sequence of the cDNA of the invention. Usually multiple clones were sequenced from one or more human samples to derive the sequences for fragments. Various human tissue samples from different donors were used for the RACE reaction. The sequences derived from these procedures were included in the SeqCalling Assembly process described in preceding paragraphs.  
     [0561] 5. Exon Linking: The NOVX target sequences identified in the present invention were subjected to the exon linking process to confirm the sequence. PCR primers were designed by starting at the most upstream sequence available, for the forward primer, and at the most downstream sequence available for the reverse primer. In each case, the sequence was examined, walking inward from the respective termini toward the coding sequence, until a suitable sequence that is either unique or highly selective was encountered, or, in the case of the reverse primer, until the stop codon was reached. Such primers were designed based on in silico predictions for the full length cDNA, part (one or more exons) of the DNA or protein sequence of the target sequence, or by translated homology of the predicted exons to closely related human sequences from other species. These primers were then employed in PCR amplification based on the following pool of human cDNAs: adrenal gland, bone marrow, brain—amygdala, brain—cerebellum, brain—hippocampus, brain—substantia nigra, brain—thalamus, brain—whole, fetal brain, fetal kidney, fetal liver, fetal lung, heart, kidney, lymphoma—Raji, mammary gland, pancreas, pituitary gland, placenta, prostate, salivary gland, skeletal muscle, small intestine, spinal cord, spleen, stomach, testis, thyroid, traclea, uterus. Usually the resulting amplicons were gel purified, cloned and sequenced to high redundancy. The PCR product derived from exon linking was cloned into the pCR2.1 vector from Invitrogen. The resulting bacterial clone has an insert covering the entire open reading frame cloned into the pCR2.1 vector. The resulting sequences from all clones were assembled with themselves, with other fragments in CuraGen Corporation&#39;s database and with public ESTs. Fragments and ESTs were included as components for an assembly when the extent of their identity with another component of the assembly was at least 95% over 50 bp. In addition, sequence traces were evaluated manually and edited for corrections if appropriate. These procedures provide the sequence reported herein.  
     [0562] 6. Physical Clone: Exons were predicted by homology and the intron/exon boundaries were determined using standard genetic rules. Exons were further selected and refined by means of similarity determination using multiple BLAST (for example, tBlastN, BlastX, and BlastN) searches, and, in some instances, GeneScan and Grail. Expressed sequences from both public and proprietary databases were also added when available to further define and complete the gene sequence. The DNA sequence was then manually corrected for apparent inconsistencies thereby obtaining the sequences encoding the full-length protein.  
     [0563] The PCR product derived by exon linking, covering the entire open reading frame, was cloned into the pCR2.1 vector from Invitrogen to provide clones used for expression and screening purposes.  
     Example C  
     [0564] Quantitative Expression Analysis of Clones in Various Cells and Tissues  
     [0565] The quantitative expression of various clones was assessed using microtiter plates containing RNA samples from a variety of normal and pathology-derived cells, cell lines and tissues using real time quantitative PCR (RTQ PCR). RTQ PCR was performed on an Applied Biosystems ABI PRISM® 7700 or an ABI PRISM® 7900 HT Sequence Detection System. Various collections of samples are assembled on the plates, and referred to as Panel 1 (containing normal tissues and cancer cell lines), Panel 2 (containing samples derived from tissues from normal and cancer sources), Panel 3 (containing cancer cell lines), Panel 4 (containing cells and cell lines from normal tissues and cells related to inflammatory conditions), Panel 5D/5I (containing human tissues and cell lines with an emphasis on metabolic diseases), AI_comprehensive_panel (containing normal tissue and samples from autoinflammatory diseases), Panel CNSD.01 (containing samples from normal and diseased brains) and CNS_neurodegeneration_panel (containing samples from normal and Alzheimer&#39;s diseased brains).  
     [0566] RNA integrity from all samples is controlled for quality by visual assessment of agarose gel electropherograms using 28S and 18S ribosomal RNA staining intensity ratio as a guide (2:1 to 2.5:1 28s:18s) and the absence of low molecular weight RNAs that would be indicative of degradation products. Samples are controlled against genomic DNA contamination by RTQ PCR reactions run in the absence of reverse transcriptase using probe and primer sets designed to amplify across the span of a single exon.  
     [0567] First, the RNA samples were normalized to reference nucleic acids such as constitutively expressed genes (for example, β-actin and GAPDH). Normalized RNA (5 ul) was converted to cDNA and analyzed by RTQ-PCR using One Step RT-PCR Master Mix Reagents (Applied Biosystems; Catalog No. 4309169) and gene-specific primers according to the manufacturer&#39;s instructions.  
     [0568] In other cases, non-normalized RNA samples were converted to single strand cDNA (sscDNA) using Superscript II (Invitrogen Corporation; Catalog No. 18064-147) and random hexamers according to the manufacturer&#39;s instructions. Reactions containing up to 10 μg of total RNA were performed in a volume of 20 μl and incubated for 60 minutes at 42° C. This reaction can be scaled up to 50 μg of total RNA in a final volume of 100 μl. sscDNA samples are then normalized to reference nucleic acids as described previously, using 1×TaqMan® Universal Master mix (Applied Biosystems; catalog No. 4324020), following the manufacturer&#39;s instructions.  
     [0569] Probes and primers were designed for each assay according to Applied Biosystems Primer Express Software package (version I for Apple Computer&#39;s Macintosh Power PC) or a similar algorithm using the target sequence as input. Default settings were used for reaction conditions and the following parameters were set before selecting primers: primer concentration=250 nM, primer melting temperature (Tm) range=58°-60° C., primer optimal Tm=59° C., maximum primer difference=2° C., probe does not have 5′G, probe Tm must be 10° C. greater than primer Tm, amplicon size 75 bp to 100 bp. The probes and primers selected (see below) were synthesized by Synthegen (Houston, Tex., USA). Probes were double purified by HPLC to remove uncoupled dye and evaluated by mass spectroscopy to verify coupling of reporter and quencher dyes to the 5′ and 3′ ends of the probe, respectively. Their final concentrations were: forward and reverse primers, 900 nM each, and probe, 200 nM.  
     [0570] PCR conditions: When working with RNA samples, normalized RNA from each tissue and each cell line was spotted in each well of either a 96 well or a 384-well PCR plate (Applied Biosystems). PCR cocktails included either a single gene specific probe and primers set, or two multiplexed probe and primers sets (a set specific for the target clone and another gene-specific set multiplexed with the target probe). PCR reactions were set up using, TaqMan® One-Step RT-PCR Master Mix (Applied Biosystems, Catalog, No. 4313803) following manufacturer&#39;s instructions. Reverse transcription was performed at 48° C. for 30 minutes followed by amplification/PCR cycles as follows: 95° C. 10 min, then 40 cycles of 95° C. for 15 seconds, 60° C. for 1 minute. Results were recorded as CT values (cycle at which a given sample crosses a threshold level of fluorescence) using a log scale, with the difference in RNA concentration between a given sample and the sample with the lowest CT value being represented as 2 to the power of delta CT. The percent relative expression is then obtained by taking the reciprocal of this RNA difference and multiplying by 100.  
     [0571] When working with sscDNA samples, normalized sscDNA was used as described previously for RNA samples. PCR reactions containing one or two sets of probe and primers were set up as described previously, using 1×TaqMan® Universal Master mix (Applied Biosystems; catalog No. 4324020), following the manufacturer&#39;s instructions. PCR amplification was performed as follows: 95° C. 10 min, then 40 cycles of 95° C. for 15 seconds, 60° C. for 1 minute. Results were analyzed and processed as described previously.  
     [0572] Panels 1, 1.1, 1.2, and 1.3D  
     [0573] The plates for Panels 1, 1.1, 1.2 and 1.3D include 2 control wells (genomic DNA control and chemistry control) and 94 wells containing cDNA from various samples. The samples in these panels are broken into 2 classes: samples derived from cultured cell lines and samples derived from primary normal tissues. The cell lines are derived from cancers of the following types: lung cancer, breast cancer, melanoma, colon cancer, prostate cancer, CNS cancer, squamous cell carcinoma, ovarian cancer, liver cancer, renal cancer, gastric cancer and pancreatic cancer. Cell lines used in these panels are widely available through the American Type Culture Collection (ATCC), a repository for cultured cell lines, and were cultured using the conditions recommended by the ATCC. The normal tissues found on these panels are comprised of samples derived from all major organ systems from single adult individuals or fetuses. These samples are derived from the following organs: adult skeletal muscle, fetal skeletal muscle, adult heart, fetal heart, adult kidney, fetal kidney, adult liver, fetal liver, adult lung, fetal lung, various regions of the brain the spleen, bone marrow, lymph node, pancreas, salivary gland, pituitary gland, adrenal gland, spinal cord, thymus, stomach, small intestine, colon, bladder, trachea, breast, ovary, uterus, placenta, prostate, testis and adipose.  
     [0574] In the results for Panels 1, 1.1, 1.2 and 1.3D, the following abbreviations are used:  
     [0575] ca.=carcinoma,  
     [0576] *=established from metastasis,  
     [0577] met=metastasis,  
     [0578] s cell var=small cell variant,  
     [0579] non-s=non-sm=non-small,  
     [0580] squam=squamous,  
     [0581] pl. eff=pl effusion=pleural effusion,  
     [0582] glio=glioma,  
     [0583] astro=astrocytoma, and  
     [0584] neuro=neuroblastoma.  
     [0585] General_screening_panel_v1.4, v1.5 and v1.6  
     [0586] The plates for Panels 1.4, 1.5, and 1.6 include 2 control wells (genomic DNA control and chemistry control) and 94 wells containing cDNA from various samples. The samples in Panels 1.4, 1.5, and 1.6 are broken into 2 classes: samples derived from cultured cell lines and samples derived from primary normal tissues. The cell lines are derived from cancers of the following types: lung cancer, breast cancer, melanoma, colon cancer, prostate cancer, CNS cancer, squamous cell carcinoma, ovarian cancer, liver cancer, renal cancer, gastric cancer and pancreatic cancer. Cell lines used in Panels 1.4, 1.5, and 1.6 are widely available through the American Type Culture Collection (ATCC), a repository for cultured cell lines, and were cultured using the conditions recommended by the ATCC. The normal tissues found on Panels 1.4, 1.5, and 1.6 are comprised of pools of samples derived from all major organ systems from 2 to 5 different adult individuals or fetuses. These samples are derived from the following organs: adult skeletal muscle, fetal skeletal muscle, adult heart, fetal heart, adult kidney, fetal kidney, adult liver, fetal liver, adult lung, fetal lung, various regions of the brain, the spleen, bone marrow, lymph node, pancreas, salivary gland, pituitary gland, adrenal gland, spinal cord, thymus, stomach, small intestine, colon, bladder, trachea, breast, ovary, uterus, placenta, prostate, testis and adipose. Abbreviations arc as described for Panels 1, 1.1, 1.2, and 1.3D.  
     [0587] Panels 2D, 2.2, 2.3 and 2.4  
     [0588] The plates for Panels 2D, 2.2, 2.3 and 2.4 generally include 2 control wells and 94 test samples composed of RNA or cDNA isolated from human tissue procured by surgeons working in close cooperation with the National Cancer Institute&#39;s Cooperative Human Tissue Network (CHTN) or the National Disease Research Initiative (NDRI) or from Ardais or Clinomics). The tissues are derived from human malignancies and in cases where indicated many malignant tissues have “matched margins” obtained from noncancerous tissue just adjacent to the tumor. These are termed normal adjacent tissues and are denoted “NAT” in the results below. The tumor tissue and the “matched margins” are evaluated by two independent pathologists (the surgical pathologists and again by a pathologist at NDRI/CHTN/Ardais/Clinomics). Unmatched RNA samples from tissues without malignancy (normal tissues) were also obtained from Ardais or Clinomics. This analysis provides a gross histopathological assessment of tumor differentiation grade. Moreover, most samples include the original surgical pathology report that provides information regarding the clinical stage of the patient. These matched margins are taken from the tissue surrounding (i.e. immediately proximal) to the zone of surgery (designated “NAT”, for normal adjacent tissue, in Table RR). In addition, RNA and cDNA samples were obtained from various human tissues derived from autopsies performed on elderly people or sudden death victims (accidents, etc.). These tissues were ascertained to be free of disease and were purchased from various commercial sources such as Clontech (Palo Alto, Calif.), Research Genetics, and Invitrogen.  
     [0589] HASS Panel v 1.0  
     [0590] The HASS panel v 1.0 plates are comprised of 93 cDNA samples and two controls. Specifically, 81 of these samples are derived from cultured human cancer cell lines that had been subjected to serum starvation, acidosis and anoxia for different time periods as well as controls for these treatments, 3 samples of human primary cells, 9 samples of malignant brain cancer (4 medulloblastomas and 5 glioblastomas) and 2 controls. The human cancer cell lines are obtained from ATCC (American Type Culture Collection) and fall into the following tissue groups: breast cancer, prostate cancer, bladder carcinomas, pancreatic cancers and CNS cancer cell lines. These cancer cells are all cultured under standard recommended conditions. The treatments used (serum starvation, acidosis and anoxia) have been previously published in the scientific literature. The primary human cells were obtained from Clonetics (Walkersville, Md.) and were grown in the media and conditions recommended by Clonetics. The malignant brain cancer samples are obtained as part of a collaboration (Henry Ford Cancer Center) and are evaluated by a pathologist prior to CuraGen receiving the samples. RNA was prepared from these samples using the standard procedures. The genomic and chemistry control wells have been described previously.  
     [0591] ARDAIS Panel v 1.0  
     [0592] The plates for ARDAIS panel v 1.0 generally include 2 control wells and 22 test samples composed of RNA isolated from human tissue procured by surgeons working in close cooperation with Ardais Corporation. The tissues are derived from human lung malignancies (lung adenocarcinoma or lung squamous cell carcinoma) and in cases where indicated many malignant samples have “matched margins” obtained from noncancerous lung tissue just adjacent to the tumor. These matched margins are taken from the tissue surrounding (i.e. immediately proximal) to the zone of surgery (designated “NAT”, for normal adjacent tissue) in the results below. The tumor tissue and the “matched margins” arc evaluated by independent pathologists (the surgical pathologists and again by a pathologist at Ardais). Unmatched malignant and non-malignant RNA samples from lungs were also obtained from Ardais. Additional information from Ardais provides a gross histopathological assessment of tumor differentiation grade and stage. Moreover, most samples include the original surgical pathology report that provides information regarding the clinical state of the patient.  
     [0593] Panel 3D, 3.1 and 3.2  
     [0594] The plates of Panel 3D, 3.1, and 3.2 are comprised of 94 cDNA samples and two control samples. Specifically, 92 of these samples are derived from cultured human cancer cell lines, 2 samples of human primary cerebellar tissue and 2 controls. The human cell lines are generally obtained from ATCC (American Type Culture Collection), NCI or the German tumor cell bank and fall into the following tissue groups: Squamous cell carcinoma of the tongue, breast cancer, prostate cancer, melanoma, epidermoid carcinoma, sarcomas, bladder carcinomas, pancreatic cancers, kidney cancers, leukemias/lymphomas, ovarian/uterine/cervical, gastric, colon, lung and CNS cancer cell lines. In addition, there arc two independent samples of cerebellum. These cells are all cultured under standard recommended conditions and RNA extracted using the standard procedures. The cell lines in panel 3D, 3.1, 3.2, 1, 1.1., 1.2, 1.3D, 1.4, 1.5, and 1.6 are of the most common cell lines used in the scientific literature.  
     [0595] Panels 4D, 4R, and 4.1D  
     [0596] Panel 4 includes samples on a 96 well plate (2 control wells, 94 test samples) composed of RNA (Panel 4R) or cDNA (Panels 4D/4.1D) isolated from various human cell lines or tissues related to inflammatory conditions. Total RNA from control normal tissues such as colon and lung (Stratagene, La Jolla, Calif.) and thymus and kidney (Clontech) was employed. Total RNA from liver tissue from cirrhosis patients and kidney from lupus patients was obtained from BioChain (Biochain Institute, Inc., Hayward, Calif.). Intestinal tissue for RNA preparation from patients diagnosed as having, Crohn&#39;s disease and ulcerative colitis was obtained from the National Disease Research Interchange (NDRI) (Philadelphia, Pa.).  
     [0597] Astrocytes, lung fibroblasts, dermal fibroblasts, coronary artery smooth muscle cells, small airway epithelium, bronchial epithelium, microvascular dermal endothelial cells, microvascular lung endothelial cells, human pulmonary aortic endothelial cells, human umbilical vein endothelial cells were all purchased from Clonetics (Walkersville, Md.) and grown in the media supplied for these cell types by Clonetics. These primary cell types were activated with various cytokines or combinations of cytokines for 6 and/or 12-14 hours, as indicated. The following cytokines were used; IL-1 beta at approximately 1-5 ng/ml, TNF alpha at approximately 5-10 ng/ml, IFN gamma at approximately 20-50 ng/ml, IL-4 at approximately 5-10 ng/ml, IL-9 at approximately 5-10 ng/ml, IL-13 at approximately 5-10 ng/ml. Endothelial cells were sometimes starved for various times by culture in the basal media from Clonetics with 0.1% serum.  
     [0598] Mononuclear cells were prepared from blood of employees at CuraGen Corporation, using Ficoll. LAK cells were prepared from these cells by culture in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco/Life Technologies, Rockville, Md.), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and Interleukin 2 for 4-6 days. Cells were then either activated with 10-20 ng/ml PMA and 1-2 μg/ml ionomycin, IL-12 at 5-10 ng/ml, IFN gamma at 20-50 ng/ml and IL-18 at 5-10 ng/ml for 6 hours. In some cases, mononuclear cells were cultured for 4-5 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) with PHA (phytohemagglutinin) or PWM (pokeweed mitogen) at approximately 5 μg/ml. Samples were taken at 24, 48 and 72 hours for RNA preparation. MLR (mixed lymphocyte reaction) samples were obtained by taking blood from two donors, isolating the mononuclear cells using Ficoll and mixing the isolated mononuclear cells 1:1 at a final concentration of approximately 2×10 6  cells/mil in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol (5.5×10 −5 M) (Gibco), and 10 mM Hepes (Gibco). The MLR was cultured and samples taken at various time points ranging from 1-7 days for RNA preparation.  
     [0599] Monocytes were isolated from mononuclear cells using CD14 Miltenyi Beads, +ve VS selection columns and a Vario Magnet according to the manufacturer&#39;s instructions. Monocytes were differentiated into dendritic cells by culture in DMEM 5% fetal calf serum (FCS) (Hyclone, Logan, Utah), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco), 50 ng/ml GMCSF and 5 ng/ml IL-4 for 5-7 days. Macrophages were prepared by culture of monocytes for 5-7 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10  −5 M (Gibco), 10 mM Hepes (Gibco) and 10% AB Human Serum or MCSF at approximately 50 ng/ml. Monocytes, macrophages and dendritic cells were stimulated for 6 and 12-14 hours with lipopolysaccharide (LPS) at 100 ng/ml. Dendritic cells were also stimulated with anti-CD40 monoclonal antibody (Pharmingen) at 10 μg/ml for 6 and 12-14 hours.  
     [0600] CD4 lymphocytes, CD8 lymphocytes and NK cells were also isolated from mononuclear cells using CD4, CD8 and CD56 Miltenyi beads, positive VS selection columns and a Vario Magnet according to the manufacturer&#39;s instructions. CD45RA and CD45RO CD4 lymphocytes were isolated by depleting mononuclear cells of CD8, CD56, CD14 and CD19 cells using CD8, CD56, CD14 and CD19 Miltenyi beads and positive selection. CD45RO beads were then used to isolate the CD45RO CD4 lymphocytes with the remaining cells being CD45RA CD4 lymphocytes. CD45RA CD4, CD45RO CD4 and CD8 lymphocytes were placed in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and plated at 10 6 cells/ml onto Falcon 6 well tissue culture plates that had been coated overnight with 0.5 μg/ml anti-CD28 (Pharmingen) and 3 ug/ml anti-CD3 (OKT3, ATCC) in PBS. After 6 and 24 hours, the cells were harvested for RNA preparation. To prepare chronically activated CD8 lymphocytes, we activated the isolated CD8 lymphocytes for 4 days on anti-CD28 and anti-CD3 coated plates and then harvested the cells and expanded them in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and IL-2. The expanded CD8 cells were then activated again with plate bound anti-CD3 and anti-CD28 for 4 days and expanded as before. RNA was isolated 6 and 24 hours after the second activation and after 4 days of the second expansion culture. The isolated NK cells were cultured in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyrivate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and IL-2 for 4-6 days before RNA was prepared.  
     [0601] To obtain B cells, tonsils were procured from NDRI. The tonsil was cut up with sterile dissecting scissors and then passed through a sieve. Tonsil cells were then spun down and resupended at 10 6 cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco). To activate the cells, we used PWM at 5 μg/ml or anti-CD40 (Pharmingen) at approximately 10 μg/ml and IL-4 at 5-10 ng/ml. Cells were harvested for RNA preparation at 24, 48 and 72 hours.  
     [0602] To prepare the primary and secondary Th1/Th2 and Tr1 cells, six-well Falcon plates were coated overnight with 10 μg/ml anti-CD28 (Pharmingen) and 2 μg/ml OKT3 (ATCC), and then washed twice with PBS. Umbilical cord blood CD4 lymphocytes (Poietic Systems, German Town, Md.) were cultured at 10 5 -10 6  cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), 10 mM Hepes (Gibco) and IL-2 (4 ng/ml). IL-12 (5 ng/ml) and anti-IL4 (1 μg/ml) were used to direct to Th1, while IL-4 (5 ng/ml) and anti-IFN gamma (1 μg/ml) were used to direct to Th2 and IL-10 at 5 ng/ml was used to direct to Tr1. After 4-5 days, the activated Th1, Th2 and Tr1 lymphocytes were washed once in DMEM and expanded for 4-7 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), 10 mM Hepes (Gibco) and IL-2 (1 ng/ml). Following this, the activated Th1, Th2 and Tr1 lymphocytes were re-stimulated for 5 days with anti-CD28/OKT3 and cytokines as described above, but with the addition of anti-CD95L (1 μg/ml) to prevent apoptosis. After 4-5 days, the Th1, Th2 and Tr1 lymphocytes were washed and then expanded again with IL-2 for 4-7 days. Activated Th1 and Th2 lymphocytes were maintained in this way for a maximum of three cycles. RNA was prepared from primary and secondary Th1 , Th2 and Tr1 after 6 and 24 hours following the second and third activations with plate bound anti-CD3 and anti-CD28 mAbs and 4 days into the second and third expansion cultures in Interleukin 2.  
     [0603] The following leukocyte cells lines were obtained from the ATCC: Ramos, EOL-1, KU-812. EOL cells were further differentiated by culture in 0.1 mM dbcAMP at 5×10 5  cells/ml for 8 days, changing the media every 3 days and adjusting the cell concentration to 5×10 5  cells/ml. For the culture of these cells, we used DMEM or RPMI (as recommended by the ATCC), with the addition of 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), 10 mM Hepes (Gibco). RNA was either prepared from resting cells or cells activated with PMA at 10 ng/ml and ionomycin at 1 μg/ml for 6 and 14 hours. Keratinocyte line CCD106 and an airway epithelial tumor line NCI-H292 were also obtained from the ATCC. Both were cultured in DMEM 5% FCS (Hyclone) 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco). CCD1106 cells were activated for 6 and 14 hours with approximately 5 ng/ml TNF alpha and 1 ng/ml IL-1 beta, while NCI-H292 cells were activated for 6 and 14 hours with the following cytokines: 5 ng/ml IL-4, 5 ng/ml IL-9, 5 ng/ml IL-13 and 25 ng/ml IFN gamma.  
     [0604] For these cell lines and blood cells, RNA was prepared by lysing approximately 10 7  cells/ml using Trizol (Gibco BRL). Briefly, 1/10 volume of bromochloropropane (Molecular Research Corporation) was added to the RNA sample, vortexed and after 10 minutes at room temperature, the tubes were spun at 14,000 rpm in a Sorvall SS34 rotor. The aqueous phase was removed and placed in a 15 ml Falcon Tube. An equal volume of isopropanol was added and left at −20° C. overnight. The precipitated RNA was spun down at 9,000 rpm for 15 min in a Sorvall SS34 rotor and washed in 70% ethanol. The pellet was redissolved in 300 μl of RNAse-free water and 35 μl buffer (Promega) 5 μl DTT, 7 μl RNAsin and 8 μl DNAse were added. The tube was incubated at 37° C. for 30 minutes to remove contaminating genomic DNA, extracted once with phenol chloroform and re-precipitated with 1/10 volume of 3M sodium acetate and 2 volumes of 100% ethanol. The RNA was spun down and placed in RNAse free water. RNA was stored at −80° C.  
     [0605] AI_comprehensive panel_v1.0  
     [0606] The plates for AI_comprehensive panel_v1.0 include two control wells and 89 test samples comprised of cDNA isolated from surgical and postmortem human tissues obtained from the Backus Hospital and Clinomics (Frederick, Md.). Total RNA was extracted from tissue samples from the Backus Hospital in the Facility at CuraGen. Total RNA from other tissues was obtained from Clinomics.  
     [0607] Joint tissues including synovial fluid, synovium, bone and cartilage were obtained from patients undergoing total knee or hip replacement surgery at the Backus Hospital. Tissue samples were immediately snap frozen in liquid nitrogen to ensure that isolated RNA was of optimal quality and not degraded. Additional samples of osteoarthritis and rheumatoid arthritis joint tissues were obtained from Clinomics. Normal control tissues were supplied by Clinomics and were obtained during autopsy of trauma victims.  
     [0608] Surgical specimens of psoriatic tissues and adjacent matched tissues were provided as total RNA by Clinomics. Two male and two female patients were selected between the ages of 25 and 47. None of the patients were taking prescription drugs at the time samples were isolated.  
     [0609] Surgical specimens of diseased colon from patients with ulcerative colitis and Crohns disease and adjacent matched tissues were obtained from Clinomics. Bowel tissue from three female and three male Crohn&#39;s patients between the ages of 41-69 were used. Two patients were not on prescription medication while the others were taking dexamethasone, phenobarbital, or tylenol. Ulcerative colitis tissue was from three male and four female patients. Four of the patients were taking lebvid and two were on phenobarbital.  
     [0610] Total RNA from post mortem lung tissue from trauma victims with no disease or with emphysema, asthma or COPD was purchased from Clinomics. Emphysema patients ranged in age from 40-70 and all were smokers, this age range was chosen to focus on patients with cigarette-linked emphysema and to avoid those patients with alpha-lanti-trypsin deficiencies. Asthma patients ranged in age from 36-75, and excluded smokers to prevent those patients that could also have COPD. COPD patients ranged in age from 35-80 and included both smokers and non-smokers. Most patients were taking corticosteroids, and bronchodilators.  
     [0611] In the labels employed to identify tissues in the AI_comprehensive panel_v1.0 panel, the following abbreviations are used:  
     [0612] AI=Autoimmunity  
     [0613] Syn=Synovial  
     [0614] Normal=No apparent disease  
     [0615] Rep22 /Rep20 =individual patients  
     [0616] RA=Rheumatoid arthritis  
     [0617] Backus=From Backus Hospital  
     [0618] OA=Osteoarthritis  
     [0619] (SS)(BA)(MF)=Individual patients  
     [0620] Adj=Adjacent tissue  
     [0621] Match control=adjacent tissues  
     [0622] -M=Male  
     [0623] -F=Female  
     [0624] COPD=Chronic obstructive pulmonary disease  
     [0625] Panels 5D and 5I  
     [0626] The plates for Panel 5D and 5I include two control wells and a variety of cDNAs isolated from human tissues and cell lines with an emphasis on metabolic diseases. Metabolic tissues were obtained from patients enrolled in the Gestational Diabetes study. Cells were obtained during different stages in the differentiation of adipocytes from human mesenchymal stem cells. Human pancreatic islets were also obtained.  
     [0627] In the Gestational Diabetes study subjects are young (18-40 years), otherwise healthy women with and without gestational diabetes undergoing routine (elective) Caesarean section. After delivery of the infant, when the surgical incisions were being repaired/closed, the obstetrician removed a small sample (&lt;1 cc) of the exposed metabolic tissues during the closure of each surgical level. The biopsy material was rinsed in sterile saline, blotted and fast frozen within 5 minutes from the time of removal. The tissue was then flash frozen in liquid nitrogen and stored, individually, in sterile screw-top tubes and kept on dry ice for shipment to or to be picked up by CuraGen. The metabolic tissues of interest include uterine wall (smooth muscle), visceral adipose, skeletal muscle (rectus) and subcutaneous adipose. Patient descriptions are as follows:  
     [0628] Patient 2: Diabetic Hispanic, overweight, not on insulin  
     [0629] Patient 7-9: Nondiabetic Caucasian and obese (BMI&gt;30)  
     [0630] Patient 10: Diabetic Hispanic, overweight, on insulin  
     [0631] Patient 11: Nondiabetic African American and overweight  
     [0632] Patient 12: Diabetic Hispanic on insulin  
     [0633] Adiocyte differentiation was induced in donor progenitor cells obtained from Osirus (a division of Clonetics/BioWhittaker) in triplicate, except for Donor 3U which had only two replicates. Scientists at Clonetics isolated, grew and differentiated human mesenchymal stem cells (HuMSCs) for CuraGen based on the published protocol found in Mark F. Pittenger, et al., Multilineage Potential of Adult Human Mesenchymal Stem Cells Science Apr. 2, 1999: 143-147. Clonetics provided Trizol lysates or frozen pellets suitable for mRNA isolation and ds cDNA production. A general description of each donor is as follows:  
     [0634] Donor 2 and 3 U: Mesenchymal Stem cells, Undifferentiated Adipose  
     [0635] Donor 2 and 3 AM: Adipose, AdiposeMidway Differentiated  
     [0636] Donor 2 and 3 AD: Adipose, Adipose Differentiated  
     [0637] Human cell lines were generally obtained from ATCC (American Type Culture Collection), NCI or the German tumor cell bank and fall into the following tissue groups: kidney proximal convoluted tubule, uterine smooth muscle cells, small intestine, liver HepG2 cancer cells, heart primary stromal cells, and adrenal cortical adenoma cells. These cells are all cultured under standard recommended conditions and RNA extracted using the standard procedures. All samples were processed at CuraGen to produce single stranded cDNA.  
     [0638] Panel 5I contains all samples previously described with the addition of pancreatic islets from a 58 year old female patient obtained from the Diabetes Research Institute at the University of Miami School of Medicine. Islet tissue was processed to total RNA at an outside source and delivered to CuraGen for addition to panel 5I.  
     [0639] In the labels employed to identify tissues in the 5D and 5I panels, the following abbreviations are used:  
     [0640] GO Adipose=Greater Omentum Adipose  
     [0641] SK=Skeletal Muscle  
     [0642] UT=Uterus  
     [0643] PL=Placenta  
     [0644] AD=Adipose Differentiated  
     [0645] AM=Adipose Midway Differentiated  
     [0646] U=Undifferentiated Stem Cells  
     [0647] Panel CNSD.01  
     [0648] The plates for Panel CNSD.01 include two control wells and 94 test samples comprised of cDNA isolated from postmortem human brain tissue obtained from the Harvard Brain Tissue Resource Center. Brains are removed from calvaria of donors between 4 and 24 hours after death, sectioned by neuroanatomists, and frozen at −80° C. in liquid nitrogen vapor. All brains are sectioned and examined by neuropathologists to confirm diagnoses with clear associated neuropathology.  
     [0649] Disease diagnoses are taken from patient records. The panel contains two brains from each of the following diagnoses: Alzheimer&#39;s disease, Parkinson&#39;s disease, Huntington&#39;s disease, Progressive Supernuclear Palsy, Depression, and “Normal controls”. Within each of these brains, the following regions are represented: cingulate gyrus, temporal pole, globus palladus, substantia nigra, Brodman Area 4 (primary motor strip), Brodman Area 7 (parietal cortex), Brodman Area 9 (prefrontal cortex), and Brodman area 17 (occipital cortex). Not all brain regions are represented in all cases; e.g., Huntington&#39;s disease is characterized in part by neurodegeneration in the globus palladus, thus this region is impossible to obtain from confirmed Huntington&#39;s cases. Likewise Parkinson&#39;s disease is characterized by degeneration of the substantia nigra making this region more difficult to obtain. Normal control brains were examined for neuropathology and found to be free of any pathology consistent with neurodegeneration.  
     [0650] In the labels employed to identify tissues in the CNS panel, the following abbreviations are used:  
     [0651] PSP=Progressive supranuclear palsy  
     [0652] Sub Nigra=Substantia nigra  
     [0653] Glob Palladus=Globus palladus  
     [0654] Temp Pole=Temporal pole  
     [0655] Cing Gyr=Cingulate gyrus  
     [0656] BA 4 =Brodman Area 4  
     [0657] Panel CNS_Neurodegeneration_V1.0  
     [0658] The plates for Panel CNS_Neurodegeneration_V1.0 include two control wells and 47 test samples comprised of cDNA isolated from postmortem human brain tissue obtained from the Harvard Brain Tissue Resource Center (McLean Hospital) and the Human Brain and Spinal Fluid Resource Center (VA Greater Los Angeles Healthcare System). Brains are removed from calvaria of donors between 4 and 24 hours after death, sectioned by neuroanatomists, and frozen at −80° C. in liquid nitrogen vapor. All brains are sectioned and examined by neuropathologists to confirm diagnoses with clear associated neuropathology.  
     [0659] Disease diagnoses are taken from patient records. The panel contains six brains from Alzheimer&#39;s disease (AD) patients, and eight brains from “Normal controls” who showed no evidence of dementia prior to death. The eight normal control brains are divided into two categories: Controls with no dementia and no Alzheimer&#39;s like pathology (Controls) and controls with no dementia but evidence of severe Alzheimer&#39;s like pathology, (specifically senile plaque load rated as level 3 on a scale of 0-3; 0=no evidence of plaques, 3 =severe AD senile plaque load). Within each of these brains, the following regions are represented: hippocampus, temporal cortex (Brodman Area 21), parietal cortex (Brodman area 7), and occipital cortex (Brodman area 17). These regions were chosen to encompass all levels of neurodegeneration in AD. The hippocampus is a region of early and severe neuronal loss in AD; the temporal cortex is known to show neurodegeneration in AD after the hippocampus; the parietal cortex shows moderate neuronal death in the late stages of the disease; the occipital cortex is spared in AD and therefore acts as a “control” region within AD patients. Not all brain regions are represented in all cases.  
     [0660] In the labels employed to identify tissues in the CNS_Neurodegeneration_V1.0 panel, the following abbreviations are used:  
     [0661] AD=Alzheimer&#39;s disease brain; patient was demented and showed AD-like pathology upon autopsy  
     [0662] Control=Control brains; patient not demented, showing no neuropathology  
     [0663] Control (Path)=Control brains; patient not demented but showing sever AD-like pathology  
     [0664] SupTemporal Ctx=Superior Temporal Cortex  
     [0665] Inf Temporal Ctx=Inferior Temporal Cortex  
     [0666] A. NOV1a and NOV1b (CG113254-01 and CG113254-02): Fibulin  
     [0667] Expression of gene CG113254-01 and CG113254-02 was assessed using the primer-probe sets Ag1294b, Ag746, Ag905, Ag4470 and Ag4726, described in Tables AA, AB, AC, AD and AE. Results of the RTQ-PCR runs are shown in Tables AF, AG, AH, AI, AJ, AK, AL and AM. Please note that CG113254-02 represents a full-length physical clone and is recognized only by two probes and primer sets: Ag4470 and Ag4726.  
                   TABLE AA                          Probe Name Ag1294b                                                     Start                Primers    Sequences    Length    Position    SEQ ID No                                             Forward    5′-cattggcagctacaagtgttc-3′   21    691    205                   Probe    TET-5′-ctgtcgaactggcttccaccttcat-3′-    25    712    206               TAMRA                                        Reverse    5′-cctccgacactcgtttacatc-3′   21    758    207                  
 
     [0668]                   TABLE AB                          Probe Name Ag746                                                     Start                Primers    Sequences    Length    Position    SEQ ID No                                             Forward    5′-gcattggcagctacaagtgt-3′   20    690    208                   Probe    TET-5′-ctgtcgaactggcttccaccttcat-3′-    25    712    209               TAMRA                                        Reverse    5′-cctccgacactcgtttacatc-3′   21    758    210                    
     [0669]                   TABLE AC                          Probe Name Ag905                                                     Start                Primers    Sequences    Length    Position    SEQ ID No                                             Forward    5′-cattggcagctacaagtgttc-3′   21    691    211                   Probe    TET-5′-ctgtcgaactggcttccaccttcat-3′-    25    712    212               Reverse    5′-cctccgacactcgtttacatc-3′   21    758    213                    
     [0670]                   TABLE AD                          Probe Name Ag4470                                                             Start                Primers    Sequences    Length    Position    SEQ ID No                                             Forward    5′-gcatcaggtgtacagaeattga-3′   22    510    214                   Probe    TET-5′-cgaatgtgtaacctcctcctgcgag-3′-    25    532    215               TAMRA                                        Reverse    5′-acaaacccaccttctgtgttc-3′   21    568    216                    
     [0671]                   TABLE AL                          Probe Name Ag4726                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gtgtctgtctggctggaaac-3′   20   1497   217                   Probe   TET-5′-tgcatctctcctgagtgtccttctgg-3′-   26   1523   218           TAMRA               Reverse   5′-acaagtacaqcaatccgtctgt-3′   22   1567   219                    
     [0672]               TABLE AF                          AI_comprehensive panel_v1.0                             Rel. Exp. (%)   Rel. Exp. (%)           Ag1294b, Run   Ag4470, Run       Tissue Name   249007981   249008358                                 110967 COPD-F   6.6   3.0       110980 COPD-F   16.6   8.7       110968 COPD-M   3.9   3.4       110977 COPD-M   31.6   38.2       110989 Emphysema-F   45.1   31.4       110992 Emphysema-F   7.2   3.3       110993 Emphysema-F   5.8   5.5       110994 Emphysema-F   3.3   2.1       110995 Emphysema-F   2.0   15.4       110996 Emphysema-F   3.1   2.0       110997 Asthma-M   3.7   0.8       111001 Asthma-F   2.8   7.7       111002 Asthma-F   5.3   5.5       111003 Atopic Asthma-F   6.1   6.0       111004 Atopic Asthma-F   3.4   12.4       111005 Atopic Asthma-F   3.9   5.6       111006 Atopic Asthma-F   2.4   1.4       111417 Allergy-M   6.6   3.5       112347 Allergy-M   3.3   5.8       112349 Normal Lung-F   3.2   6.1       112357 Normal Lung-F   100.0   100.0       112354 Normal Lung-M   58.6   69.3       112374 Crohns-F   7.5   9.4       112389 Match Control Crohns-F   3.5   7.1       112375 Crohns-F   5.1   7.4       112732 Match Control Crohns-F   0.5   6.7       112725 Crohns-M   10.6   5.8       112387 Match Control Crohns-M   3.5   0.0       112378 Crohns-M   1.7   4.7       112390 Match Control Crohns-M   55.5   52.5       112726 Crohns-M   3.6   7.9       112731 Match Control Crohns-M   13.9   13.1       112380 Ulcer Col-F   13.7   13.2       112734 Match Control Ulcer Col-F   5.6   8.4       112384 Ulcer Col-F   3.9   2.8       112737 Match Control Ulcer Col-F   3.3   2.8       112386 Ulcer Col-F   0.0   0.0       112738 Match Control Ulcer Col-F   0.0   1.6       112381 Ulcer Col-M   4.2   9.4       112735 Match Control Ulcer Col-M   18.2   25.2       112382 Ulcer Col-M   4.2   7.6       112394 Match Control Ulcer Col-M   0.0   0.0       112383 Ulcer Col-M   12.2   6.6       112736 Match Control Ulcer Col-M   2.0   2.4       112423 Psoriasis-F   3.9   4.5       112427 Match Control Psoriasis-F   30.8   25.7       112418 Psoriasis-M   4.6   4.3       112723 Match Control Psoriasis-M   23.8   27.5       112419 Psoriasis-M   2.7   2.6       112424 Match Control Psoriasis-M   1.9   4.0       112420 Psoriasis-M   4.9   13.7       112425 Match Control Psoriasis-M   25.9   25.7       104689 (MF) OA Bone-Backus   12.9   7.3       104690 (MF) Adj “Normal” Bone-   3.7   1.2       Backus       104691 (MF) OA Synovium-Backus   6.9   11.3       104692 (BA) OA Cartilage-Backus   21.3   7.4       104694 (BA) OA Bone-Backus   6.6   2.0       104695 (BA) Adj “Normal” Bone-   2.3   5.3       Backus       104696 (BA) OA Synovium-Backus   5.7   6.3       104700 (SS) OA Bone-Backus   6.2   5.6       104701 (SS) Adj “Normal” Bone-   3.8   5.8       Backus       104702 (SS) OA Synovium-Backus   15.4   15.1       117093 OA Cartilage Rep7   18.0   12.2       112672 OA Bone5   90.1   97.3       112673 OA Synovium5   63.7   46.0       112674 OA Synovial Fluid cells5   32.3   32.5       117100 OA Cartilage Rep14   3.3   0.0       112756 OA Bone9   7.0   14.8       112757 OA Synovium9   12.2   17.4       112758 OA Synovial Fluid Cells9   3.9   5.2       117125 RA Cartilage Rep2   4.6   7.9       113492 Bone2 RA   2.4   1.5       113493 Synovium2 RA   1.1   0.0       113494 Syn Fluid Cells RA   1.4   0.0       113499 Cartilage4 RA   1.4   2.0       113500 Bone4 RA   0.5   1.7       113501 Synovium4 RA   1.7   2.3       113502 Syn Fluid Cells4 RA   1.8   0.7       113495 Cartilage3 RA   1.6   1.2       113496 Bone3 RA   1.1   2.3       113497 Synovium3 RA   0.0   0.0       113498 Syn Fluid Cells3 RA   0.6   0.8       117106 Normal Cartilage Rep20   4.5   5.7       113663 Bone3 Normal   6.7   0.9       113664 Synovium3 Normal   1.2   1.6       113665 Syn Fluid Cells3 Normal   0.9   3.3       117107 Normal Cartilage Rep22   1.3   3.5       113667 Bone4 Normal   11.8   8.7       113668 Synovium4 Normal   12.0   12.8       113669 Syn Fluid Cells4 Normal   10.7   24.3                    
     [0673]               TABLE AG                          CNS_neurodegeneration_v1.0                                 Rel.   Rel.   Rel.           Exp. (%)   Exp. (%)   Exp. (%)           Ag1294b,   Ag4470,   Ag4726,       Tissue   Run   Run   Run       Name   206231468   224535165   224706360                                     AD 1 Hippo   11.2   13.7   11.6       AD 2 Hippo   22.5   22.2   23.5       AD 3 Hippo   4.7   6.3   0.0       AD 4 Hippo   8.7   10.7   15.2       AD 5 Hippo   37.6   35.1   35.6       AD 6 Hippo   100.0   95.9   100.0       Control 2 Hippo   28.7   15.8   21.9       Control 4 Hippo   30.4   23.7   40.3       Control (Path) 3 Hippo   6.9   0.0   3.6       AD 1 Temporal Ctx   16.3   15.0   26.1       AD 2 Temporal Ctx   31.6   14.8   25.2       AD 3 Temporal Ctx   3.8   2.6   5.6       AD 4 Temporal Ctx   10.9   23.7   36.1       AD 5 Inf Temporal Ctx   34.6   38.4   35.8       AD 5 Sup Temporal Ctx   19.6   29.7   55.9       AD 6 Inf Temporal Ctx   73.7   85.3   76.8       AD 6 Sup Temporal Ctx   81.2   100.0   97.9       Control 1 Temporal Ctx   1.2   7.7   5.1       Control 2 Temporal Ctx   15.5   28.5   42.9       Control 3 Temporal Ctx   5.9   16.7   18.4       Control 4 Temporal Ctx   7.9   14.5   17.2       Control (Path) 1 Temporal   41.8   32.3   43.5       Ctx       Control (Path) 2 Temporal   26.2   34.9   36.6       Ctx       Control (Path) 3 Temporal   1.5   2.8   11.4       Ctx       Control (Path) 4 Temporal   19.2   31.6   20.3       Ctx       AD 1 Occipital Ctx   15.8   17.8   17.4       AD 2 Occipital Ctx   0.0   0.0   0.0       (Missing)       AD 3 Occipital Ctx   1.2   7.9   3.6       AD 4 Occipital Ctx   17.8   11.3   7.9       AD 5 Occipital Ctx   8.7   9.3   17.6       AD 6 Occipital Ctx   12.3   20.3   30.8       Control 1 Occipital Ctx   0.0   5.8   3.0       Control 2 Occipital Ctx   27.4   36.3   34.6       Control 3 Occipital Ctx   5.4   9.4   2.8       Control 4 Occipital Ctx   6.7   10.7   15.4       Control (Path) 1 Occipital   56.3   54.7   85.3       Ctx       Control (Path) 2 Occipital   10.4   10.0   21.8       Ctx       Control (Path) 3 Occipital   1.2   0.0   0.0       Ctx       Control (Path) 4 Occipital   6.3   18.3   5.0       Ctx       Control 1 Parietal Ctx   6.4   7.4   9.7       Control 2 Parietal Ctx   39.5   33.2   55.9       Control 3 Parietal Ctx   4.4   9.6   11.2       Control (Path) 1 Parietal   17.6   22.4   45.4       Ctx       Control (Path) 2 Parietal   17.6   28.1   12.1       Ctx       Control (Path) 3 Parietal   0.0   2.2   4.2       Ctx       Control (Path) 4 Parietal   26.4   44.1   30.1       Ctx                    
     [0674]               TABLE AH                          General_screening_panel_v1.4                             Rel. Exp. (%)   Rel. Exp. (%)           Ag4470, Run   Ag4726, Run       Tissue Name   222655825   222842378                                 Adipose   4.8   3.3       Melanoma* Hs688(A).T   3.3   2.7       Melanoma* Hs688(B).T   3.1   2.7       Melanoma* M14   2.8   4.8       Melanoma* LOXIMVI   0.2   0.1       Melanoma* SK-MEL-5   0.8   0.4       Squamous cell carcinoma SCC-4   0.6   0.2       Testis Pool   5.5   4.3       Prostate ca.* (bone met) PC-3   3.0   1.6       Prostate Pool   1.1   0.5       Placenta   10.0   7.7       Uterus Pool   2.3   0.1       Ovarian ca. OVCAR-3   0.8   0.7       Ovarian ca. SK-OV-3   0.4   0.6       Ovarian ca. OVCAR-4   0.3   0.3       Ovarian ca. OVCAR-5   1.6   1.1       Ovarian ca. IGROV-1   0.5   1.4       Ovarian ca. OVCAR-8   0.9   0.7       Ovary   7.7   5.0       Breast ca. MCF-7   0.9   0.4       Breast ca. MDA-MB-231   1.2   0.5       Breast ca. BT 549   1.8   0.7       Breast ca. T47D   4.9   4.2       Breast ca. MDA-N   0.3   0.2       Breast Pool   2.4   0.8       Trachea   4.5   1.3       Lung   7.9   5.5       Fetal Lung   3.8   1.8       Lung ca. NCI-N417   3.9   3.6       Lung ca. LX-I   0.9   0.7       Lung ca. NCI-H146   0.8   0.8       Lung ca. SHP-77   2.3   0.3       Lung ca. A549   0.9   0.8       Lung ca. NCI-H526   2.9   2.1       Lung ca. NCI-H23   1.4   0.8       Lung ca. NCI-H460   2.2   1.2       Lung ca. HOP-62   2.0   0.5       Lung ca. NCI-H522   31.6   20.2       Liver   20.7   11.6       Fetal Liver   63.7   61.1       Liver ca. HepG2   100.0   100.0       Kidney Pool   11.2   6.7       Fetal Kidney   5.3   2.0       Renal ca. 786-0   1.6   1.7       Renal ca. A498   0.8   1.3       Renal ca. ACHN   2.2   2.5       Renal ca. UO-31   12.9   10.6       Renal ca. TK-10   54.0   41.8       Bladder   2.9   1.8       Gastric ca. (liver met.) NCI-N87   2.3   2.0       Gastric ca. KATO III   0.8   0.6       Colon ca. SW-948   0.5   0.6       Colon ca. SW480   3.3   0.7       Colon ca.* (SW480 met) SW620   16.2   12.8       Colon ca. HT29   0.0   0.1       Colon ca. HCT-116   4.4   3.7       Colon ca. CaCo-2   94.0   31.9       Colon cancer tissue   16.5   7.9       Colon ca. SW1116   0.6   1.0       Colon ca. Colo-205   0.0   0.0       Colon ca. SW-48   0.2   0.0       Colon Pool   2.6   1.0       Small Intestine Pool   10.8   4.9       Stomach Pool   2.4   3.4       Bone Marrow Pool   1.0   0.0       Fetal Heart   2.6   0.7       Heart Pool   1.7   0.7       Lymph Node Pool   2.7   2.6       Fetal Skeletal Muscle   2.3   1.6       Skeletal Muscle Pool   0.8   1.0       Spleen Pool   0.6   0.4       Thymus Pool   16.3   7.9       CNS cancer (glio/astro) U87-MG   5.7   6.4       CNS cancer (glio/astro) U-118-MG   2.7   1.6       CNS cancer (neuro; met) SK-N-AS   4.8   4.4       CNS cancer (astro) SF-539   0.0   0.2       CNS cancer (astro) SNB-75   5.2   4.4       CNS cancer (glio) SNB-19   0.5   1.1       CNS cancer (glio) SF-295   8.3   5.1       Brain (Amygdala) Pool   2.9   2.5       Brain (cerebellum)   5.9   7.3       Brain (fetal)   25.3   12.2       Brain (Hippocampus) Pool   3.7   1.9       Cerebral Cortex Pool   4.6   2.6       Brain (Substantia nigra) Pool   4.7   2.1       Brain (Thalamus) Pool   3.8   3.9       Brain (whole)   9.2   8.5       Spinal Cord Pool   3.6   1.9       Adrenal Gland   4.2   2.6       Pituitary gland Pool   0.8   0.6       Salivary Gland   1.0   0.9       Thyroid (female)   2.0   1.8       Pancreatic ca. CAPAN2   0.0   0.0       Pancreas Pool   3.0   1.1                    
     [0675]               TABLE AI                          Panel 1.2                             Rel. Exp. (%)   Rel. Exp. (%)           Ag746, Run   Ag746, Run       Tissue Name   115163442   119442272                                 Endothelial cells   12.3   5.9       Heart (Fetal)   0.0   0.0       Pancreas   0.0   0.0       Pancreatic ca. CAPAN 2   0.0   0.0       Adrenal Gland   0.0   0.2       Thyroid   0.1   0.0       Salivary gland   0.0   0.0       Pituitary gland   0.2   0.1       Brain (fetal)   2.4   16.0       Brain (whole)   0.0   0.3       Brain (amygdala)   0.0   0.0       Brain (cerebellum)   0.0   0.0       Brain (hippocampus)   0.0   0.0       Brain (thalamus)   0.0   0.0       Cerebral Cortex   0.0   0.0       Spinal cord   0.0   0.0       glio/astro U87-MG   0.0   0.0       glio/astro U-118-MG   0.0   0.0       astrocytoma SW1783   0.0   0.0       neuro*; met SK-N-AS   0.0   0.2       astrocytoma SF-539   0.0   0.0       astrocytoma SNB-75   0.0   0.0       glioma SNB-19   0.0   0.0       glioma U251   0.0   0.0       glioma SF-295   0.0   0.0       Heart   0.0   0.0       Skeletal Muscle   0.0   0.0       Bone marrow   0.0   0.0       Thymus   1.2   2.8       Spleen   0.0   0.0       Lymph node   0.0   0.0       Colorectal Tissue   0.0   0.0       Stomach   0.0   0.0       Small intestine   0.0   0.0       Colon ca. SW480   0.0   0.0       Colon ca.* SW620 (SW480 met)   1.1   1.9       Colon ca. HT29   0.0   0.0       Colon ca. HCT-116   0.0   0.0       Colon ca. CaCo-2   46.3   56.6       Colon ca. Tissue (ODO3866)   0.0   0.0       Colon ca. HCC-2998   0.0   0.0       Gastric ca.* (liver met) NCI-N87   0.0   0.0       Bladder   0.0   0.0       Trachea   0.0   0.0       Kidney   0.0   0.0       Kidney (fetal)   0.1   0.9       Renal ca. 786-0   0.0   0.0       Renal ca. A498   0.0   0.0       Renal ca. RXF 393   0.0   0.0       Renal ca. ACHN   0.0   0.0       Renal ca. UO-31   0.0   0.0       Renal ca. TK-10   0.0   0.0       Liver   32.8   51.2       Liver (fetal)   7.2   100.0       Liver ca. (hepatoblast) HepG2   100.0   94.0       Lung   0.0   0.0       Lung (fetal)   0.0   0.0       Lung ca. (small cell) LX-1   0.0   0.0       Lung ca. (small cell) NCI-H69   0.0   0.0       Lung ca. (s. cell var.) SHP-77   0.0   0.0       Lung ca. (large cell) NCI-H460   0.0   0.0       Lung ca. (non-sm. cell) A549   0.0   0.0       Lung ca. (non-s. cell) NCI-H23   0.0   0.0       Lung ca. (non-s. cell) HOP-62   0.0   0.0       Lung ca. (non-s. cl) NCI-H522   63.7   90.1       Lung ca. (squam.) SW 900   0.0   0.0       Lung ca. (squam.) NCI-H596   0.0   0.0       Mammary gland   0.7   3.6       Breast ca.* (pl. ef) MCF-7   0.0   0.0       Breast ca.* (pl. ef) MDA-MB-231   0.0   0.0       Breast ca.* (pl. ef) T47D   0.0   0.0       Breast ca. BT-549   0.0   0.0       Breast ca. MDA-N   0.0   0.0       Ovary   0.5   11.7       Ovarian ca. OVCAR-3   0.0   0.0       Ovarian ca. OVCAR-4   0.0   0.0       Ovarian ca. OVCAR-5   0.0   0.0       Ovarian ca. OVCAR-8   0.0   0.0       Ovarian ca. IGROV-1   0.0   0.0       Ovarian ca. (ascites) SK-OV-3   0.0   0.0       Uterus   0.0   0.0       Placenta   34.4   39.5       Prostate   0.0   0.0       Prostate ca.* (bone met) PC-3   0.0   0.0       Testis   1.0   3.5       Melanoma Hs688(A).T   0.0   0.0       Melanoma* (met) Hs688(B).T   0.0   0.0       Melanoma UACC-62   0.0   0.0       Melanoma M14   0.0   0.0       Melanoma LOX IMVI   0.0   0.0       Melanoma* (met) SK-MEL-5   0.0   0.0                    
     [0676]               TABLE AJ                          Panel 2D                             Rel. Exp. (%)   Rel. Exp. (%)           Ag746, Run   Ag746, Run       Tissue Name   147127131   148019631                                 Normal Colon   18.3   21.8       CC Well to Mod Diff (ODO3866)   16.5   21.7       CC Margin (ODO3866)   3.1   0.0       CC Gr.2 rectosigmoid (ODO3868)   0.0   0.8       CC Margin (ODO3868)   0.5   2.0       CC Mod Diff (ODO3920)   1.2   2.3       CC Margin (ODO3920)   1.3   2.6       CC Gr.2 ascend colon (ODO3921)   3.4   4.4       CC Margin (ODO3921)   1.3   0.0       CC from Partial Hepatectomy   8.4   1.9       (ODO4309) Mets       Liver Margin (ODO4309)   49.7   41.5       Colon mets to lung (OD04451-01)   0.3   5.3       Lung Margin (OD04451-02)   0.0   1.8       Normal Prostate 6546-1   9.1   12.1       Prostate Cancer (OD04410)   2.0   9.7       Prostate Margin (OD04410)   16.8   20.3       Prostate Cancer (OD04720-01)   13.5   14.4       Prostate Margin (OD04720-02)   14.0   22.4       Normal Lung 061010   6.8   11.7       Lung Met to Muscle (ODO4286)   1.8   0.7       Muscle Margin (ODO4286)   11.5   13.1       Lung Malignant Cancer (OD03126)   1.5   6.0       Lung Margin (OD03126)   4.8   2.4       Lung Cancer (OD04404)   4.2   2.3       Lung Margin (OD04404)   9.0   10.4       Lung Cancer (OD04565)   0.3   0.0       Lung Margin (OD04565)   0.4   0.3       Lung Cancer (OD04237-01)   10.7   11.1       Lung Margin (OD04237-02)   4.9   5.4       Ocular Mel Met to Liver (ODO4310)   10.5   11.9       Liver Margin (ODO4310)   22.4   32.8       Melanoma Mets to Lung (OD04321)   0.0   0.0       Lung Margin (OD04321)   0.6   0.0       Normal Kidney   5.3   5.3       Kidney Ca, Nuclear grade 2   39.8   43.8       (OD04338)       Kidney Margin (OD04338)   4.8   6.4       Kidney Ca Nuclear grade 1/2   3.0   0.3       (OD04339)       Kidney Margin (OD04339)   5.4   10.0       Kidney Ca, Clear cell type   18.2   19.2       (OD04340)       Kidney Margin (OD04340)   9.0   10.4       Kidney Ca, Nuclear grade 3   5.2   8.3       (OD04348)       Kidney Margin (OD04348)   6.9   4.7       Kidney Cancer (OD04622-01)   41.8   45.4       Kidney Margin (OD04622-03)   1.9   1.4       Kidney Cancer (OD04450-01)   9.2   6.2       Kidney Margin (OD04450-03)   10.2   9.0       Kidney Cancer 8120607   2.2   1.7                         Kidney Margin 8120608   6.5   6.4       Kidney Cancer 8120613   2.2   0.7       Kidney Margin 8120614   6.3   3.0       Kidney Cancer 9010320   10.9   16.5       Kidney Margin 9010321   9.0   11.3       Normal Uterus   4.3   6.3       Uterus Cancer 064011   13.4   17.7       Normal Thyroid   9.1   14.9       Thyroid Cancer 064010   6.4   5.9       Thyroid Cancer A302152   4.4   5.1       Thyroid Margin A302153   12.0   22.1       Normal Breast   9.9   14.3                         Breast Cancer (OD04566)   0.4   0.2       Breast Cancer (OD04590-01)   5.3   3.9       Breast Cancer Mets (OD04590-03)   4.0   10.4       Breast Cancer Metastasis (OD04655-05)   7.2   4.4       Breast Cancer 064006   5.2   3.3       Breast Cancer 1024   12.1   18.6       Breast Cancer 9100266   2.7   5.3       Breast Margin 9100265   5.0   5.8       Breast Cancer A209073   0.5   1.8       Breast Margin A209073   1.7   0.4       Normal Liver   39.5   47.0       Liver Cancer 064003   4.2   0.6       Liver Cancer 1025   66.4   74.2       Liver Cancer 1026   36.1   42.6       Liver Cancer 6004-T   100.0   100.0       Liver Tissue 6004-N   22.8   34.4       Liver Cancer 6005-T   39.2   35.4       Liver Tissue 6005-N   33.2   38.2       Normal Bladder   6.6   4.9       Bladder Cancer 1023   1.0   4.8       Bladder Cancer A302173   2.6   0.7       Bladder Cancer (OD04718-01)   0.0   0.7       Bladder Normal Adjacent   3.5   14.4       (OD04718-03)       Normal Ovary   50.7   47.3       Ovarian Cancer 064008   10.2   7.4       Ovarian Cancer (OD04768-07)   73.7   80.7       Ovary Margin (OD04768-08)   2.6   0.8       Normal Stomach   2.9   2.9       Gastric Cancer 9060358   0.0   1.1       Stomach Margin 9060359   2.4   0.3       Gastric Cancer 9060395   0.5   1.1       Stomach Margin 9060394   5.2   2.0       Gastric Cancer 9060397   3.4   7.0       Stomach Margin 9060396   1.4   0.0       Gastric Cancer 064005   1.3   6.0                    
     [0677]               TABLE AK                          Panel 4.1D                                 Rel.   Rel.   Rel.           Exp. (%)   Exp. (%)   Exp. (%)           Ag1294b,   Ag4470,   Ag4726,           Run   Run   Run       Tissue Name   200065765   191882058   204150067                                     Secondary Th1 act   15.3   21.8   8.4       Secondary Th2 act   7.2   14.9   0.4       Secondary Tr1 act   5.5   11.3   3.1       Secondary Th 1 rest   6.7   5.3   0.5       Secondary Th2 rest   1.0   1.8   2.6       Secondary Tr1 rest   1.3   2.3   0.5       Primary Th1 act   26.6   42.0   24.8       Primary Th2 act   34.2   37.6   19.8       Primary Tr1 act   40.3   42.3   27.9       Primary Th1 rest   0.3   1.1   0.0       Primary Th2 rest   0.5   1.3   0.0       Primary Tr1 rest   0.0   0.0   1.1       CD45RA CD4 lymphocyte   7.7   5.9   2.2       act       CD45RO CD4 lymphocyte   10.9   9.9   16.5       act       CD8 lymphocyte act   11.0   19.2   9.9       Secondary CD8   11.8   10.4   8.9       lymphocyte rest       Secondary CD8   4.7   4.5   1.9       lymphocyte act       CD4 lymphocyte none   0.0   0.6   0.0       2ry Th1/Th2/Tr1_anti-   1.7   4.9   2.5       CD95 CH11       LAK cells rest   0.0   1.1   1.4       LAK cells IL-2   3.1   3.5   1.7       LAK cells IL-2 + IL-   2.9   1.4   1.1       12       LAK cells IL-2 + IFN   0.5   0.0   1.3       gamma       LAK ceils IL-2 + IL-   0.5   2.3   1.1       18       LAK cells PMA/   1.0   3.3   4.2       ionomycin       NK Cells IL-2 rest   1.4   3.9   2.0       Two Way MLR 3 day   3.1   4.8   1.8       Two Way MLR 5 day   5.0   9.3   4.2       Two Way MLR 7 day   4.7   9.4   4.0       PBMC rest   0.6   0.0   0.0       PBMC PWM   11.5   20.6   9.9       PBMC PHA-L   7.2   18.3   14.1       Ramos (B cell) none   1.8   4.5   2.0       Ramos (B cell)   3.4   9.2   2.7       ionomycin       B lymphocytes PWM   20.2   20.3   17.6       B lymphocytes CD40L and   12.2   10.4   11.0       IL-4       EOL-1 dbcAMP   1.5   1.9   3.2       EOL-1 dbcAMP PMA/   1.1   2.7   0.5       ionomycin       Dendritic cells none   8.5   5.1   4.0       Dendritic cells LPS   6.4   6.7   5.9       Dendritic cells anti-   8.7   7.9   4.7       CD40       Monocytes rest   0.0   1.0   0.0       Monocytes LPS   1.1   1.6   2.2       Macrophages rest   8.8   13.0   4.8       Macrophages LPS   0.0   0.0   0.0       HUVEC none   10.1   18.3   8.5       HUVEC starved   7.6   11.5   11.4       HUVEC IL-1beta   5.6   11.1   10.2       HUVEC IFN gamma   21.9   29.9   11.3       HUVEC TNFalpha + IFN   3.5   4.5   1.1       gamma       HUVEC TNFalpha + IL4   31.2   45.7   19.1       HUVEC IL-11   17.7   28.3   20.7       Lung Microvascular EC   65.1   71.2   61.6       none       Lung Microvascular EC   34.4   27.7   30.4       TNFalpha + IL-1beta       Microvascular Dermal   42.3   38.4   29.9       EC none       Microvascular Dermal   16.7   24.1   7.6       EC TNFalpha + IL-       1beta       Bronchial epithelium   2.4   5.0   4.4       TNFalpha + IL-1beta       Small airway   1.7   6.6   4.2       epithelium none       Small airway   2.5   1.3   2.4       epithelium TNFalpha +       IL-1beta       Coronery artery SMC   9.0   10.3   2.1       rest       Coronery artery SMC   5.2   1.8   4.1       TNFalpha + IL-1beta       Astrocytes rest   2.1   1.4   0.8       Astrocytes TNFalpha +   2.2   3.1   1.2       IL-1beta       KU-812 (Basophil) rest   10.2   29.5   14.9       KU-812 (Basophil)   11.1   18.9   8.6       PMA/ionomycin       CCD1106   0.0   2.3   0.9       (Keratinocytes) none       CCD1106 (Keratinocytes)   0.6   0.0   0.0       TNFalpha + IL-1beta       Liver cirrhosis   6.8   10.2   6.0       NCI-H292 none   21.3   16.6   10.3       NCI-H292 IL-4   11.5   9.0   7.3       NCI-H292 IL-9   13.8   32.5   17.4       NCI-H292 IL-13   19.9   5.3   6.7       NCI-H292 IFN gamma   7.3   15.5   13.8       HPAEC none   20.4   37.9   28.9       HPAEC TNFalpha +   21.5   17.4   15.4       IL-1beta       Lung fibroblast none   23.5   22.7   15.7       Lung fibroblast TNF   8.8   11.7   9.2       alpha + IL-1 beta       Lung fibroblast IL-4   21.2   17.7   24.7       Lung fibroblast IL-9   16.8   36.1   18.2       Lung fibroblast IL-13   33.2   36.1   19.8       Lung fibrobast IFN   19.1   11.7   7.8       gamma       Dermal fibroblast   2.9   1.3   0.1       CCD1070 rest       Dermal fibroblast   0.0   0.8   0.2       CCD1070 TNF alpha       Dermal fibroblast   1.5   1.6   4.5       CCD1070 IL-1 beta       Dermal fibroblast IFN   45.1   5.4   32.8       gamma       Dermal fibroblast IL-4   100.0   100.0   100.0       Dermal Fibroblast rest   53.6   39.5   39.2       Neutrophils TNFa +   1.5   0.0   0.6       LPS       Neutrophils rest   10.2   0.5   0.1       Colon   1.5   0.5   1.6       Lung   1.7   0.7   1.3       Thymus   40.1   59.9   25.0       Kidney   1.5   0.7   0.0                    
     [0678]               TABLE AL                          Panel 4D                             Rel. Exp. (%)   Rel. Exp. (%)           Ag1294b, Run   Ag1294b, Run       Tissue Name   138944262   139408252                                 Secondary Th1 act   10.9   7.7       Secondary Th2 act   6.4   8.0       Secondary Tr1 act   11.3   9.3       Secondary Th1 rest   3.4   2.7       Secondary Th2 rest   1.5   2.5       Secondary Tr1 rest   1.4   2.0       Primary Th1 act   48.0   46.0       Primary Th2 act   38.7   27.7       Primary Tr1 act   72.2   55.5       Primary Th1 rest   3.1   2.3       Primary Th2 rest   1.0   0.8       Primary Tr1 rest   1.1   0.5       CD45RA CD4 lymphocyte act   2.9   1.8       CD45RO CD4 lymphocyte act   18.6   12.2       CD8 lymphocyte act   17.8   6.8       Secondary CD8 lymphocyte rest   6.8   6.0       Secondary CD8 lymphocyte act   5.5   4.1       CD4 lymphocyte none   0.0   0.2       2ry Th1/Th2/Tr1_anti-CD95 CH11   2.9   3.1       LAK cells rest   1.4   0.3       LAK cells IL-2   3.8   2.2       LAK cells IL-2 + IL-12   3.0   0.8       LAK ceils IL-2 + IFN gamma   2.0   1.7       LAK cells IL-2 + IL-18   0.5   0.2       LAK cells PMA/ionomycin   0.7   1.3       NK Cells IL-2 rest   0.7   0.7       Two Way MLR 3 day   1.1   2.5       Two Way MLR 5 day   2.5   2.8       Two Way MLR 7 day   4.5   5.0       PBMC rest   0.0   0.0       PBMC PWM   41.8   29.1       PBMC PHA-L   34.4   21.8       Ramos (B cell) none   4.7   2.4       Ramos (B cell) ionomycin   9.2   5.8       B lymphocytes PWM   51.8   51.4       B lymphocytes CD40L and IL-4   10.2   12.3       EOL-1 dbcAMP   0.3   0.2       EOL-1 dbcAMP PMA/ionomycin   0.4   1.8       Dendritic cells none   6.7   3.8       Dendritic cells LPS   4.7   3.1       Dendritic cells anti-CD40   6.0   5.6       Monocytes rest   0.0   0.0       Monocytes LPS   0.7   0.8       Macrophages rest   19.8   9.9       Macrophages LPS   0.7   0.5       HUVEC none   9.3   10.2       HUVEC starved   19.2   13.1       HUVEC IL-1beta   4.1   1.7       HUVEC IFN gamma   21.0   13.7       HUVEC TNF alpha + IFN gamma   2.8   0.6       HUVEC TNF alpha + IL4   30.8   25.7       HUVEC IL-11   11.6   7.3       Lung Microvascular EC none   24.1   20.0       Lung Microvascular EC TNFalpha +   8.0   12.2       IL-1beta       Microvascular Dermal EC none   64.6   45.7       Microvascular Dermal EC TNFalpha +   18.4   11.7       IL-1beta       Bronchial epithelium TNFalpha +   5.2   5.4       IL1beta       Small airway epithelium none   4.0   3.2       Small airway epithelium TNFalpha +   8.2   4.5       IL-1beta       Coronery artery SMC rest   5.8   6.3       Coronery artery SMC TNFalpha +   4.5   5.1       IL-1beta       Astrocytes rest   0.8   0.5       Astrocytes TNFalpha + IL-1beta   3.6   1.9       KU-812 (Basophil) rest   16.0   11.1       KU-812 (Basophil) PMA/ionomycin   12.3   9.5       CCD1106 (Keratinocytes) none   0.0   0.5       CCD1106 (Keratinocytes) TNFalpha +   0.7   0.4       IL-1beta       Liver cirrhosis   8.4   3.8       Lupus kidney   2.0   3.2       NCI-H292 none   21.9   25.7       NCI-H292 IL-4   15.7   12.3       NCI-H292 1L-9   20.6   14.7       NCI-H292 IL-13   8.3   5.7       NCI-H292 IFN gamma   5.1   8.2       HPAEC none   18.7   23.8       HPAEC TNFalpha + IL-1beta   11.9   12.9       Lung fibroblast none   15.7   13.5       Lung fibroblast TNF alpha + IL-1   6.9   4.7       beta       Lung fibroblast IL-4   25.0   16.6       Lung fibroblast IL-9   14.7   15.8       Lung fibroblast IL-13   40.3   32.5       Lung fibroblast IFN gamma   15.4   17.4       Dermal fibroblast CCD1070 rest   0.5   0.9       Dermal fibroblast CCD1070 TNF alpha   0.9   0.8       Dermal fibroblast CCD1070 IL-1 beta   0.6   0.6       Dermal fibroblast IFN gamma   32.1   18.4       Dermal fibroblast IL-4   100.0   100.0       IBD Colitis 2   0.0   0.0       IBD Crohn&#39;s   0.3   0.8       Colon   1.4   0.5       Lung   0.5   0.8       Thymus   2.9   4.3       Kidney   65.5   47.3                    
     [0679]               TABLE AM                          general oncology screening panel_v_2.4                                 Rel. Exp. (%)               Ag4470, Run           Tissue Name   260280484                                         Colon cancer 1   1.0           Colon NAT 1   0.3           Colon cancer 2   0.0           Colon NAT 2   0.3           Colon cancer 3   1.1           Colon NAT 3   0.0           Colon malignant cancer 4   2.2           Colon NAT 4   0.0           Lung cancer 1   0.4           Lung NAT 1   0.2           Lung cancer 2   58.2           Lung NAT 2   0.0           Squamous cell carcinoma 3   1.3           Lung NAT 3   46.3           Metastatic melanoma 1   28.9           Melanoma 2   1.4           Melanoma 3   0.3           Metastatic melanoma 4   26.2           Metastatic melanoma 5   16.3           Bladder cancer 1   0.3           Bladder NAT 1   0.0           Bladder cancer 2   1.0           Bladder NAT 2   0.1           Bladder NAT 3   0.0           Bladder NAT 4   1.1           Prostate adenocarcinoma 1   4.3           Prostate adenocarcinoma 2   1.5           Prostate adenocarcinoma 3   1.8           Prostate adenocarcinoma 4   4.4           Prostate NAT 5   1.0           Prostate adenocarcinoma 6   0.5           Prostate adenocarcinoma 7   0.2           Prostate adenocarcinoma 8   0.7           Prostate adenocarcinoma 9   1.7           Prostate NAT 10   0.6           Kidney cancer 1   9.5           Kidney NAT 1   3.7           Kidney cancer 2   100.0           Kidney NAT 2   2.2           Kidney cancer 3   71.7           Kidney NAT 3   1.9           Kidney cancer 4   75.8           Kidney NAT 4   0.9                        
     [0680] AI_comprehensive panel_v1.0 Summary: Ag1294b/Ag4470 Two experiments with two different probe and primer sets Expression of this gene in this panel confirms expression of this gene in cells involved in the immune response. Highest expression of this gene is seen in normal lung (CT=30.5). Please see Panel 4D for discussion of utility of this gene in inflammation.  
     [0681] CNS_neurodegeneration_v1.0 Summary: Ag1294b/Ag4470/Ag4726 Three experiments with different probe and primer sets produce results that are in reasonable agreement. This panel does not show differential expression of this gene in Alzheimer&#39;s disease. However, this profile confirms the expression of this gene at low but significant levels in the brain. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurologic disorders, such as Alzheimer&#39;s disease, Parkinson&#39;s disease, schizophrenia, multiple sclerosis, stroke and epilepsy.  
     [0682] General_screening_panel_v1.4 Summary: Ag4470/Ag4726 Two experiments with different probe and primer sets produce results that are in excellent agreement. Highest expression of this gene is seen in a liver cancer cell line (CTs=30), with moderate levels of expression seen in fetal and adult liver, and cell lines derived from colon, renal and lung cancers. Thus, expression of this gene could be used to differentiate liver derived tissue from other samples on this panel.  
     [0683] Panel 1.2 Summary: Ag746 Two experiments with the same probe and primer set produce results that are in excellent agreement, with highest expression of this gene in a liver cancer cell line (CTs=27). High levels of expression are also seen in fetal and adult liver tissue, a colon cancer cell line and a lung cancer cell line. Thus, expression of this gene could be used to differentiate liver derived samples, the colon cancer cell line and the lung cancer cell line from other samples on this panel. Expression of this gene could also be used as a diagnostic marker to detect the presence of colon and lung cancers.  
     [0684] Moderate expression is also seen in the fetal brain, placenta, and endothelial cells.  
     [0685] Panel 2D Summary: Ag746 Two experiments with the same probe and primer set produce results that are in excellent agreement, with highest expression of this gene in liver cancer (CTs=31). The prominent expression in liver derived tissue is consistent with the results in Panel 1.2. Moderate levels of expression are also evident in samples from ovarian cancer and kidney cancer. Furthermore, expression of this gene is higher in these cancers than in the normal adjacent tissue. Thus, expression of this gene could be used to differentiate between liver derived samples and other samples on this panel and as a marker to detect the presence of liver, kidney, and ovarian cancer. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of liver, kidney, and ovarian cancers.  
     [0686] Panel 4.1D Summary: Ag1294b/Ag4470/Ag4726 Results from three experiments with three different probe and primer sets are in agreement with the expression profile in Panel 4D, with highest expression of this gene in this experiment in IL-4 treated dermal fibroblasts (CTs=30). In addition, this experiment shows low but significant levels of expression in resting neutrophils (CT-33.2), a sample absent in Panel 4D. Please see Panel 4D for discussion of utility of this gene in inflammation.  
     [0687] Panel 4D Summary: Ag1294b Two experiments with the same probe and primer set produce results that are in excellent agreement, with highest expression of this gene in IL-4 treated dermal fibroblasts (CTs=30). In addition, this gene is expressed at moderate levels in IFN gamma stimulated dermal fibroblasts, activated lung fibroblasts, HPAECs, lung and dermal microvasculature, activated small airway and bronchial epithelium, activated NCI-H1292 cells, acutely activated T cells, and activated B cells.  
     [0688] Based on these levels of expression in T cells, activated B cells and cells in lung and skin, therapeutics that block the function of this gene product may be useful as therapeutics that reduce or eliminate the symptoms in patients with autoimmune and inflammatory diseases in which activated B cells present antigens in the generation of the aberrant immune response and in treating T-cell mediated diseases, including Crohn&#39;s disease, ulcerative colitis, multiple sclerosis, chronic obstructive pulmonary disease, asthma, allergy, emphysema, rheumatoid arthritis, or psoriasis.  
     [0689] general oncology screening panel_v — 2.4 Summary: Ag4470 Highest expression of this gene is seen in kidney cancer (CT=30). In addition, this gene is more highly expressed in lung and kidney cancer than in the corresponding normal adjacent tissue. Thus, expression of this gene could be used as a marker of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene product may be useful in the treatment of lung and kidney cancer.  
     [0690] B. NOV2a (CG122729-01): Novel SPTM Protein.  
     [0691] Expression of gene CG122729-01 was assessed using the primer-probe sets Ag1441, Ag1447 and Ag4533, described in Tables BA, BB and BC. Results of the RTQ-PCR runs are shown in Tables BD, BE and BF.  
                   TABLE BA                          Probe Name Ag1441                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-acttctacggtgacagaatgga-3′   22   2804   220                   Probe   TET-5′-cctcatcaaaagcaccatcctggg-3′-   24   2847   221           TAMRA               Reverse   5′-ctgtccaaagttgctgacaaac-3′   22   2871   222                  
 
     [0692]                   TABLE BB                          Probe Name Ag1447                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gatcggagtaaggcctttaaaa-3′   22   1969   223                   Probe   TET-5′-ctgctctttccaacccagcctgaag-3′-   25   1995   224           TAMRA               Reverse   5′-cggggtatctccttagattgag-3′   22   2044   225                    
     [0693]                   TABLE 13L                          Probe Name Ag433                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-ccaaatgaagacgtgaaagaaa-3′   22   757   226                   Probe   TET-5′-accaagtttgagtgatgtccaacaca-3′-   26   792   227           TAMRA               Reverse   5′-tctgcactgtcttctggatgt-3′   21   818   228                    
     [0694]               TABLE BD                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%)               Ag4533, Run           Tissue Name   224702760                                         AD 1 Hippo   26.2           AD 2 Hippo   2.2           AD 3 Hippo   25.2           AD 4 Hippo   16.3           AD 5 Hippo   25.3           AD 6 Hippo   100.0           Control 2 Hippo   48.3           Control 4 Hippo   29.1           Control (Path) 3 Hippo   8.6           AD 1 Temporal Ctx   9.2           AD 2 Temporal Ctx   30.4           AD 3 Temporal Ctx   12.9           AD 4 Temporal Ctx   25.9           AD 5 Inf Temporal Ctx   27.9           AD 5 Sup Temporal Ctx   43.5           AD 6 Inf Temporal Ctx   28.9           AD 6 Sup Temporal Ctx   58.6           Control 1 Temporal Ctx   17.1           Control 2 Temporal Ctx   18.4           Control 3 Temporal Ctx   12.2           Control 3 Temporal Ctx   16.8           Control (Path) 1 Temporal Ctx   17.4           Control (Path) 2 Temporal Ctx   13.0           Control (Path) 3 Temporal Ctx   3.2           Control (Path) 4 Temporal Ctx   19.9           AD 1 Occipital Ctx   5.1           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   13.7           AD 4 Occipital Ctx   26.4           AD 5 Occipital Ctx   12.8           AD 6 Occipital Ctx   7.3           Control 1 Occipital Ctx   19.2           Control 2 Occipital Ctx   27.2           Control 3 Occipital Ctx   13.6           Control 4 Occipital Ctx   14.9           Control (Path) 1 Occipital Ctx   24.5           Control (Path) 2 Occipital Ctx   5.0           Control (Path) 3 Occipital Ctx   2.0           Control (Path) 4 Occipital Ctx   15.6           Control 1 Parietal Ctx   17.3           Control 2 Parietal Ctx   40.9           Control 3 Parietal Ctx   6.1           Control (Path) 1 Parietal Ctx   17.7           Control (Path) 2 Parietal Ctx   12.7           Control (Path) 3 Parietal Ctx   3.7           Control (Path) 4 Parietal Ctx   26.1                        
     [0695]               TABLE BE                          General_screening_panel_v1.4                                 Rel. Exp. (%)               Ag4533, Run           Tissue Name   222735045                                         Adipose   13.9           Melanoma* Hs688(A).T   0.0           Melanoma* Hs688(B).T   0.0           Melanoma* M14   0.0           Melanoma* LOXIMVI   0.0           Melanoma* SK-MEL-5   0.0           Squamous cell carcinoma SCC-4   0.0           Testis Pool   2.1           Prostate ca.* (bone met) PC-3   0.0           Prostate Pool   1.9           Placenta   3.4           Uterus Pool   0.9           Ovarian ca. OVCAR-3   0.1           Ovarian ca. SK-OV-3   1.2           Ovarian ca. OVCAR-4   0.0           Ovarian ca. OVCAR-5   0.0           Ovarian ca. IGROV-1   0.0           Ovarian ca. OVCAR-8   0.0           Ovary   4.0           Breast ca. MCF-7   0.1           Breast ca. MDA-MB-231   0.0           Breast ca. BT 549   0.0           Breast ca. T47D   0.1           Breast ca. MDA-N   0.0           Breast Pool   10.4           Trachea   13.1           Lung   1.2           Fetal Lung   21.6           Lung ca. NCI-N417   0.0           Lung ca. LX-1   0.0           Lung ca. NCI-H146   0.2           Lung ca. SHP-77   0.3           Lung ca. A549   0.0           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   0.0           Lung ca. NCI-H460   0.0           Lung ca. HOP-62   0.0           Lung ca. NCI-H522   0.0           Liver   1.3           Fetal Liver   11.9           Liver ca. HepG2   0.0           Kidney Pool   8.2           Fetal Kidney   3.4           Renal ca. 786-0   0.0           Renal ca. A498   0.0           Renal ca. ACHN   0.0           Renal ca. UO-31   0.0           Renal ca. TK-10   0.0           Bladder   25.3           Gastric ca. (liver met.) NCI-N87   0.2           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.0           Colon ca. SW480   0.0           Colon ca.* (SW480 met) SW620   0.3           Colon ca. HT29   0.0           Colon ca. HCT-116   0.0           Colon ca. CaCo-2   0.2           Colon cancer tissue   13.6           Colon ca. SW1116   0.0           Colon ca. Colo-205   0.0           Colon ca. SW-48   0.0           Colon Pool   12.2           Small Intestine Pool   4.3           Stomach Pool   3.3           Bone Marrow Pool   3.2           Fetal Heart   2.9           Heart Pool   2.5           Lymph Node Pool   7.6           Fetal Skeletal Muscle   3.5           Skeletal Muscle Pool   0.7           Spleen Pool   100.0           Thymus Pool   32.1           CNS cancer (glio/astro) U87-MG   0.0           CNS cancer (glio/astro) U-118-MG   0.0           CNS cancer (neuro; met) SK-N-AS   0.0           CNS cancer (astro) SF-539   0.0           CNS cancer (astro) SNB-75   0.0           CNS cancer (glio) SNB-19   0.0           CNS cancer (glio) SF-295   0.3           Brain (Amygdala) Pool   6.7           Brain (cerebellum)   4.8           Brain (fetal)   2.6           Brain (Hippocampus) Pool   8.2           Cerebral Cortex Pool   6.1           Brain (Substantia nigra) Pool   6.1           Brain (Thalamus) Pool   11.5           Brain (whole)   12.0           Spinal Cord Pool   15.5           Adrenal Gland   9.2           Pituitary gland Pool   1.8           Salivary Gland   6.9           Thyroid (female)   1.7           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   7.7                        
     [0696]               TABLE BF                          Panel 4.1D                                 Rel. Exp. (%)               Ag4533, Run           Tissue Name   198383974                                         Secondary Th1 act   0.1           Secondary Th2 act   0.1           Secondary Tr1 act   0.1           Secondary Th1 rest   0.1           Secondary Th2 rest   0.1           Secondary Tr1 rest   0.1           Primary Th1 act   0.1           Primary Th2 act   0.4           Primary Tr1 act   0.2           Primary Th1 rest   0.3           Primary Th2 rest   0.3           Primary Tr1 rest   1.3           CD45RA CD4 lymphocyte act   3.6           CD45RO CD4 lymphocyte act   1.9           CD8 lymphocyte act   1.2           Secondary CD8 lymphocyte rest   0.5           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   1.4           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.1           LAK cells rest   33.7           LAK cells IL-2   2.2           LAK cells IL-2 + IL-12   3.6           LAK cells IL-2 + IFN gamma   3.3           LAK cells IL-2 + IL-18   4.0           LAK cells PMA/ionomycin   22.5           NK Cells IL-2 rest   3.6           Two Way MLR 3 day   20.4           Two Way MLR 5 day   12.2           Two Way MLR 7 day   4.1           PBMC rest   6.9           PBMC PWM   5.7           PBMC PHA-L   10.7           Ramos (B cell) none   33.2           Ramos (B cell) ionomycin   41.2           B lymphocytes PWM   17.9           B lymphocytes CD40L and IL-4   100.0           EOL-1 dbcAMP   20.0           EOL-1 dbcAMP PMA/ionomycin   52.5           Dendritic cells none   46.7           Dendritic cells LPS   26.1           Dendritic cells anti-CD40   53.6           Monocytes rest   15.2           Monocytes LPS   15.6           Macrophages rest   42.0           Macrophages LPS   12.4           HUVEC none   0.0           HUVEC starved   0.1           HUVEC IL-1beta   0.0           HUVEC IFN gamma   0.1           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.7           Lung Microvascular EC none   0.0           Lung Microvascular EC TNFalpha +   0.0           IL-1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   0.0           IL1beta           Small airway epithelium none   0.1           Small airway epithelium TNFalpha +   0.2           IL-1beta           Coronery artery SMC rest   0.0           Coronery artery SMC TNFalpha +   0.0           IL-1beta           Astrocytes rest   0.1           Astrocytes TNFalpha + IL-1beta   0.0           KU-812 (Basophil) rest   0.1           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   0.0           CCD1106 (Keratinocytes) TNFalpha +   0.0           IL-1beta           Liver cirrhosis   0.5           NCI-H292 none   0.0           NCI-H292 IL-4   0.0           NCI-H292 IL-9   0.0           NCI-H292 IL-13   0.0           NCI-H292 IFN gamma   0.0           HPAEC none   0.0           HPAEC TNF alpha + IL-1beta   0.1           Lung fibroblast none   0.0           Lung fibroblast TNF alpha + IL-1   0.0           beta           Lung fibroblast IL-4   0.0           Lung fibroblast IL-9   0.0           Lung fibroblast IL-13   0.0           Lung fibroblast IFN gamma   0.0           Dermal fibroblast CCD1070 rest   0:0           Dermal fibroblast CCD1070 TNF alpha   0.0           Dermal fibroblast CCD1070 IL-1 beta   0.1           Dermal fibroblast IFN gamma   0.2           Dermal fibroblast IL-4   1.8           Dermal Fibroblasts rest   0.6           Neutrophils TNFa + LPS   6.3           Neutrophils rest   22.4           Colon   3.0           Lung   2.2           Thymus   11.6           Kidney   1.2                        
     [0697] CNS_neurodegeneration_v1.0 Summary: Ag4533 This panel does not show differential expression of this gene in Alzheimer&#39;s disease. However, this profile confirms the expression of this gene at low levels in the brain. Please see Panel 1.4 for discussion of utility of this gene in the central nervous system.  
     [0698] General_screening_panel_v1.4 Summary: Ag4533 Highest expression of this gene is seen in the spleen (CT=28.4). In addition, low to moderate levels of expression are seen in all regions of the CNS examined, including the hippocampus, thalamus, substantia nigra, amygdala, cerebellum and cerebral cortex.  
     [0699] Among tissues with metabolic function, this gene is expressed at moderate to low levels in pituitary, adipose, adrenal gland, pancreas, thyroid, and adult and fetal skeletal muscle, heart, and liver. This widespread expression among these tissues suggests that this gene product may play a role in normal neuroendocrine and metabolic function and that disregulated expression of this gene may contribute to neuroendocrine disorders or metabolic diseases, such as obesity and diabetes.  
     [0700] Panel 4.1D Summary: Ag4553 Highest expression of this gene is seen in CD40/IL-40 treated B lymphocytes (CT=27.3). In addition, prominent levels of expression are seen in dendritic cells, eosinophils, macrophages, monocytes, and PBMCs. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.  
     [0701] C. NOV3a (CG122777-01): P-type Trefoil Domain Containing Protein  
     [0702] Expression of gene CG122777-01 was assessed using the primer-probe set Ag4528, described in Table CA. Results of the RTQ-PCR runs are shown in Tables CB and CC.  
                   TABLE CA                          Probe Name Ag4528                                                         SEQ ID           Primers   Sequences   Length   Start Position   No                                             Forward   5′-cagcatctgcttgttctggt-3′   20   302   229                   Probe   TET-5′-gtgctgcatatgcccggtttcct-3′-   23   339   230           TAMRA               Reverse   5′-gacggacttggacatgtcac-3′   20   373   231                  
 
     [0703]               TABLE CB                          General_screening_panel_v1.4                                 Rel. Exp. (%)               Ag4528, Run           Tissue Name   222262771                                         Adipose   0.0           Melanoma* Hs688(A).T   1.6           Melanoma* Hs688(B).T   0.0           Melanoma* M14   0.0           Melanoma* LOXIMVI   0.0           Melanoma* SK-MEL-5   0.0           Squamous cell carcinoma SCC-4   1.0           Testis Pool   31.4           Prostate ca.* (bone met) PC-3   0.5           Prostate Pool   0.0           Placenta   0.0           Uterus Pool   0.0           Ovarian ca. OVCAR-3   1.3           Ovarian ca. SK-OV-3   0.0           Ovarian ca. OVCAR-4   3.8           Ovarian ca. OVCAR-5   2.3           Ovarian ca. IGROV-1   1.2           Ovarian ca. OVCAR-8   3.7           Ovary   0.4           Breast ca. MCF-7   1.1           Breast ca. MDA-MB-231   0.4           Breast ca. BT 549   0.0           Breast ca. T47D   8.7           Breast ca. MDA-N   0.0           Breast Pool   0.9           Trachea   100.0           Lung   0.0           Fetal Lung   19.3           Lung ca. NCI-N417   0.0           Lung ca. LX-1   2.9           Lung ca. NCI-H146   0.9           Lung ca. SHP-77   0.4           Lung ca. A549   5.5           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   4.2           Lung ca. NCI-H460   0.0           Lung ca. HOP-62   9.5           Lung ca. NCI-H522   6.0           Liver   0.0           Fetal Liver   0.8           Liver ca. HepG2   15.2           Kidney Pool   0.0           Fetal Kidney   0.0           Renal ca. 786-0   2.1           Renal ca. A498   0.0           Renal ca. ACHN   0.0           Renal ca. UO-31   7.2           Renal ca. TK-10   3.7           Bladder   0.0           Gastric ca. (liver met.) NCI-N87   8.3           Gastric ca. KATO III   1.1           Colon ca. SW-948   1.5           Colon ca. SW480   1.5           Colon ca.* (SW480 met) SW620   0.3           Colon ca. HT29   0.4           Colon ca. HCT-116   1.0           Colon ca. CaCo-2   1.7           Colon cancer tissue   0.4           Colon ca. SW1116   1.4           Colon ca. Colo-205   2.5           Colon ca. SW-48   2.7           Colon Pool   0.0           Small Intestine Pool   1.1           Stomach Pool   0.5           Bone Marrow Pool   0.0           Fetal Heart   0.0           Heart Pool   0.0           Lymph Node Pool   0.3           Fetal Skeletal Muscle   0.5           Skeletal Muscle Pool   0.0           Spleen Pool   0.0           Thymus Pool   1.8           CNS cancer (glio/astro) U87-MG   1.3           CNS cancer (glio/astro) U-118-MG   4.0           CNS cancer (neuro; met) SK-N-AS   1.5           CNS cancer (astro) SF-539   2.2           CNS cancer (astro) SNB-75   1.9           CNS cancer (glio) SNB-19   1.2           CNS cancer (glio) SF-295   0.4           Brain (Amygdala) Pool   0.0           Brain (cerebellum)   1.2           Brain (fetal)   0.4           Brain (Hippocampus) Pool   0.0           Cerebral Cortex Pool   0.0           Brain (Substantia nigra) Pool   0.6           Brain (Thalamus) Pool   0.0           Brain (whole)   0.0           Spinal Cord Pool   1.5           Adrenal Gland   0.8           Pituitary gland Pool   6.7           Salivary Gland   0.0           Thyroid (female)   0.0           Pancreatic ca. CAPAN2   0.5           Pancreas Pool   1.8                        
     [0704]               TABLE CC                          Panel 4.1D                                 Rel. Exp. (%)               Ag4528, Run           Tissue Name   198361170                                         Secondary Th1 act   0.0           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.0           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.0           Primary Th1 rest   0.0           Primary Th2 rest   0.0           Primary Tr1 rest   0.0           CD45RA CD4 lymphocyte act   0.0           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.0           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   0.0           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0           LAK cells rest   0.0           LAK cells IL-2   0.0           LAK cells IL-2 + IL-12   0.0           LAK cells IL-2 + IFN gamma   0.0           LAK cells IL-2 + IL-18   0.0           LAK cells PMA/ionomycin   0.0           NK Cells IL-2 rest   0.0           Two Way MLR 3 day   0.0           Two Way MLR 5 clay   0.0           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   0.0           PBMC PHA-L   0.0           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   0.0           EOL-1 dbcAMP   2.2           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   0.0           Dendritic cells LPS   0.0           Dendritic cells anti-CD40   0.0           Monocytes rest   0.0           Monocytes LPS   0.0           Macrophages rest   0.0           Macrophages LPS   0.0           HUVEC none   0.0           HUVEC starved   0.0           HUVEC IL-1beta   0.0           HUVEC IFN gamma   0.0           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.0           Lung Microvascular EC none   0.0           Lung Microvascular EC TNFalpha +   0.0           IL-1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   3.1           IL1beta           Small airway epithelium none   0.0           Small airway epithelium TNFalpha +   0.0           IL-1beta           Coronery artery SMC rest   0.0           Coronery artery SMC TNFalpha +   0.0           IL-1beta           Astrocytes rest   0.0           Astrocytes TNFalpha + IL-1beta   5.3           KU-812 (Basophil) rest   0.0           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   3.1           CCD1106 (Keratinocytes) TNFalpha +   0.0           IL-1beta           Liver cirrhosis   0.0           NCI-H292 none   49.0           NCI-H292 IL-4   45.1           NCI-H292 IL-9   50.0           NCI-H292 IL-13   7.7           NCI-H292 IFN gamma   20.3           HPAEC none   0.0           HPAEC TNF alpha + IL-1 beta   0.0           Lung fibroblast none   2.6           Lung fibroblast TNF alpha + IL-1   3.3           beta           Lung fibroblast IL-4   0.0           Lung fibroblast IL-9   0.0           Lung fibroblast IL-13   0.0           Lung fibroblast IFN gamma   0.0           Dermal fibroblast CCD1070 rest   0.0           Dermal fibroblast CCD1070 TNF alpha   0.0           Dermal fibroblast CCD1070 IL-1 beta   9.9           Dermal fibroblast IFN gamma   0.0           Dermal fibroblast IL-4   0.0           Dermal Fibroblasts rest   2.2           Neutrophils TNFa + LPS   0.0           Neutrophils rest   0.0           Colon   0.0           Lung   0.0           Thymus   2.8           Kidney   100.0                        
     [0705] CNS_neurodegeneration_v1.0 Summary: Ag4528 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0706] General_screening_panel_v1.4 Summary: Ag4528 Highest expression of this gene is seen in the trachea (CT=30.5). Thus, expression of this gene could be used to differentiate between this sample and other samples on this panel and as a marker of this tissue. Low but significant levels of expression are also seen in testis, fetal lung and cell lines derived from gastric, renal, breast, liver and lung cancers.  
     [0707] Panel 4.1D Summary: Ag4528 This gene is only expressed at detectable levels in the kidney (CT=34). Thus, expression of this gene could be used to differentiate the kidney derived sample from other samples on this panel and as a marker of kidney tissue. In addition, therapeutic targeting of the expression or function of this gene may modulate kidney function and be important in the treatment of inflammatory or autoimmune diseases that affect the kidney, including lupus and glomerulonephiritis.  
     [0708] D. NOV4a (CG124229-01): Insulin Like Growth Factor Binding Protein 3  
     [0709] Expression of gene CG124229-01 was assessed using the primer-probe set Ag6776, described in Table DA. Results of the RTQ-PCR runs are shown in Tables DB, DC, DD and DE.  
                   TABLE DA                          Probe Name Ag6776                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-atatggtccctgccgtagag-3′   201   703   232                   Probe   TET-5′-tgaatcacctgaagttcctcaatgtgc-3′-   27   738   233           TAMRA               Reverse   5′-tgtacacccctgggactca-3′   19   765   234                  
 
     [0710]               TABLE DB                          AI_comprehensive panel_v1.0                                 Rel. Exp. (%)               Ag6776, Run           Tissue Name   283839691                                         110967 COPD-F   2.0           110980 COPD-F   18.6           110968 COPD-M   1.2           110977 COPD-M   41.8           110989 Emphysema-F   14.0           110992 Emphysema-F   3.7           110993 Emphysema-F   1.4           110994 Emphysema-F   1.7           110995 Emphysema-F   9.5           110996 Emphysema-F   1.3           110997 Asthma-M   2.5           111001 Asthma-F   6.3           111002 Asthma-F   8.1           111003 Atopic Asthma-F   7.9           111004 Atopic Asthma-F   6.3           111005 Atopic Asthma-F   4.2           111006 Atopic Asthma-F   0.6           111417 Allergy-M   5.9           112347 Allergy-M   0.1           112349 Normal Lung-F   0.1           112357 Normal Lung-F   4.6           112354 Normal Lung-M   9.9           112374 Crohns-F   2.5           112389 Match Control Crohns-F   3.9           112375 Crohns-F   2.5           112732 Match Control Crohns-F   0.5           112725 Crohns-M   2.4           112387 Match Control Crohns-M   16.4           112378 Crohns-M   0.2           112390 Match Control Crohns-M   25.7           112726 Crohns-M   1.3           1112731 Match Control Crohns-M   12.0           112380 Ulcer Col-F   8.8           112734 Match Control Ulcer Col-F   1.4           112384 Ulcer Col-F   12.5           112737 Match Control Ulcer Col-F   0.6           112386 Ulcer Col-F   4.8           112738 Match Control Ulcer Col-F   0.8           112381 Ulcer Col-M   0.2           112735 Match Control Ulcer Col-M   0.5           112382 Ulcer Col-M   6.9           112394 Match Control Ulcer Col-M   2.8           112383 Ulcer Col-M   9.9           112736 Match Control Ulcer Col-M   5.1           112423 Psoriasis-F   1.5           112427 Match Control Psoriasis-F   100.0           112418 Psoriasis-M   2.4           112723 Match Control Psoriasis-M   0.3           112419 Psoriasis-M   4.0           112424 Match Control Psoriasis-M   6.5           112420 Psoriasis-M   35.8           112425 Match Control Psoriasis-M   79.6           104689 (MF) OA Bone-Backus   15.8           104690 (MF) Adj “Normal” Bone-Backus   11.0           104691 (MF) OA Synovium-Backus   1.7           104692 (BA) OA Cartilage-Backus   0.0           104694 (BA) OA Bone-Backus   4.2           104695 (BA) Adj “Normal” Bone-Backus   4.3           104696 (BA) OA Synovium-Backus   3.6           104700 (SS) OA Bone-Backus   3.2           104701 (SS) Adj “Normal” Bone-Backus   7.5           104702 (SS) OA Synovium-Backus   3.7           117093 OA Cartilage Rep7   17.7           112672 OA Bone5   21.8           112673 OA Synovium5   9.2           112674 OA Synovial Fluid cells5   12.7           117100 OA Cartilage Rep14   2.8           112756 OA Bone9   1.7           112757 OA Synovium9   0.2           112758 OA Synovial Fluid Cells9   1.3           117125 RA Cartilage Rep2   1.8           113492 Bone2 RA   0.6           113493 Synovium2 RA   0.3           113494 Syn Fluid Cells RA   0.5           113499 Cartilage4 RA   0.6           113500 Bone4 RA   0.6           113501 Synovium4 RA   0.4           113502 Syn Fluid Cells4 RA   0.4           113495 Cartilage3 RA   0.4           113496 Bone3 RA   0.5           113497 Synovium3 RA   0.3           113498 Syn Fluid Cells3 RA   0.6           117106 Normal Cartilage Rep20   2.0           113663 Bone3 Normal   0.0           113664 Synovium3 Normal   0.0           113665 Syn Fluid Cells3 Normal   0.1           117107 Normal Cartilage Rep22   2.7           113667 Bone4 Normal   24.1           113668 Synovium4 Normal   31.6           113669 Syn Fluid Cells4 Normal   36.1                        
     [0711]               TABLE DC                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%) Ag6776,           Tissue Name   Run 278368013                                         AD 1 Hippo   16.6           AD 2 Hippo   26.8           AD 3 Hippo   11.3           AD 4 Hippo   4.6           AD 5 Hippo   83.5           AD 6 Hippo   100.0           Control 2 Hippo   32.1           Control 4 Hippo   14.3           Control (Path) 3 Hippo   44.8           AD 1 Temporal Ctx   26.8           AD 2 Temporal Ctx   30.6           AD 3 Temporal Ctx   9.2           AD 4 Temporal Ctx   14.3           AD 5 Inf Temporal Ctx   45.4           AD 5 Sup Temporal Ctx   41.5           AD 6 Inf Temporal Ctx   55.9           AD 6 Sup Temporal Ctx   80.1           Control 1 Temporal Ctx   2.4           Control 2 Temporal Ctx   25.3           Control 3 Temporal Ctx   23.5           Control 3 Temporal Ctx   8.2           Control (Path) 1 Temporal Ctx   40.6           Control (Path) 2 Temporal Ctx   31.0           Control (Path) 3 Temporal Ctx   52.9           Control (Path) 4 Temporal Ctx   23.5           AD 1 Occipital Ctx   13.5           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   13.8           AD 4 Occipital Ctx   19.6           AD 5 Occipital Ctx   61.6           AD 6 Occipital Ctx   48.6           Control 1 Occipital Ctx   3.6           Control 2 Occipital Ctx   87.7           Control 3 Occipital Ctx   35.6           Control 4 Occipital Ctx   13.4           Control (Path) 1 Occipital Ctx   43.5           Control (Path) 2 Occipital Ctx   7.5           Control (Path) 3 Occipital Ctx   56.6           Control (Path) 4 Occipital Ctx   10.9           Control 1 Parietal Ctx   4.1           Control 2 Parietal Ctx   26.1           Control 3 Parietal Ctx   16.4           Control (Path) 1 Parietal Ctx   37.9           Control (Path) 2 Parietal Ctx   25.5           Control (Path) 3 Parietal Ctx   69.3           Control (Path) 4 Parietal Ctx   28.5                        
     [0712]               TABLE DD                          General_screening_panel_v1.6                                 Rel. Exp. (%) Ag6776,           Tissue Name   Run 277729935                                         Adipose   2.0           Melanoma* Hs688(A).T   68.8           Melanoma* Hs688(B).T   41.8           Melanoma* M14   0.7           Melanoma* LOXIMVI   1.1           Melanoma* SK-MEL-5   0.2           Squamous cell carcinoma SCC-4   0.5           Testis Pool   0.3           Prostate ca.* (bone met) PC-3   0.8           Prostate Pool   0.9           Placenta   10.2           Uterus Pool   1.3           Ovarian ca. OVCAR-3   4.1           Ovarian ca. SK-OV-3   11.4           Ovarian ca. OVCAR-4   10.0           Ovarian ca. OVCAR-5   0.0           Ovarian ca. IGROV-1   2.9           Ovarian ca. OVCAR-8   0.4           Ovary   0.7           Breast ca. MCF-7   0.7           Breast ca. MDA-MB-231   0.6           Breast ca. BT 549   1.7           Breast ca. T47D   0.0           Breast ca. MDA-N   0.0           Breast Pool   3.6           Trachea   1.5           Lung   0.9           Fetal Lung   0.9           Lung ca. NCI-N417   0.0           Lung ca. LX-1   1.0           Lung ca. NCI-H146   0.0           Lung ca. SHP-77   0.0           Lung ca. A549   6.2           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   0.3           Lung ca. NCI-H460   5.8           Lung ca. HOP-62   0.3           Lung ca. NCI-H522   0.3           Liver   1.3           Fetal Liver   8.7           Liver ca. HepG2   0.0           Kidney Pool   6.8           Fetal Kidney   0.6           Renal ca. 786-0   29.9           Renal ca. A498   51.8           Renal ca. ACHN   0.3           Renal ca. UO-31   0.2           Renal ca. TK-10   2.6           Bladder   0.7           Gastric ca. (liver met.) NCI-N87   1.8           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.3           Colon ca. SW480   1.3           Colon ca.* (SW480 met) SW620   0.0           Colon ca. HT29   0.0           Colon ca. HCT-116   0.0           Colon ca. CaCo-2   0.1           Colon cancer tissue   2.0           Colon ca. SW1116   0.0           Colon ca. Colo-205   0.1           Colon ca. SW-48   0.0           Colon Pool   2.5           Small Intestine Pool   8.0           Stomach Pool   3.0           Bone Marrow Pool   1.7           Fetal Heart   1.6           Heart Pool   0.8           Lymph Node Pool   2.2           Fetal Skeletal Muscle   1.6           Skeletal Muscle Pool   0.1           Spleen Pool   1.5           Thymus Pool   1.6           CNS cancer (glio/astro) U87-MG   8.5           CNS cancer (glio/astro) U-118-MG   100.0           CNS cancer (neuro; met) SK-N-AS   0.1           CNS cancer (astro) SF-539   4.6           CNS cancer (astro) SNB-75   51.1           CNS cancer (glio) SNB-19   2.9           CNS cancer (glio) SF-295   58.6           Brain (Amygdala) Pool   0.1           Brain (cerebellum)   0.1           Brain (fetal)   0.5           Brain (Hippocampus) Pool   0.2           Cerebral Cortex Pool   0.2           Brain (Substantia nigra) Pool   0.0           Brain (Thalamus) Pool   0.1           Brain (whole)   0.3           Spinal Cord Pool   0.1           Adrenal Gland   0.2           Pituitary gland Pool   0.6           Salivary Gland   0.1           Thyroid (female)   0.1           Pancreatic ca. CAPAN2   5.4           Pancreas Pool   0.3                        
     [0713]               TABLE DE                          Panel 4.1D                                 Rel. Exp. (%)               Ag6776, Run           Tissue Name   277729707                                         Secondary Th1 act   0.0           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.0           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.0           Primary Th1 rest   0.0           Primary Th2 rest   0.0           Primary Tr1 rest   0.0           CD45RA CD4 lymphocyte act   38.4           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.0           Secondary CD8 lymphocyte act   0.1           CD4 lymphocyte none   0.1           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0           LAK cells rest   0.0           LAK cells IL-2   0.0           LAK cells IL-2 + IL-12   0.0           LAK cells IL-2 + IFN gamma   0.0           LAK cells IL-2 + IL-18   0.1           LAK cells PMA/ionomycin   0.1           NK Cells IL-2 rest   0.2           Two Way MLR 3 day   0.0           Two Way MLR 5 day   0.0           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   0.0           PBMC PHA-L   0.0           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   0.1           EOL-1 dbcAMP   0.0           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   0.0           Dendritic cells LPS   0.0           Dendritic cells anti-CD40   0.0           Monocytes rest   0.0           Monocytes LPS   0.0           Macrophages rest   0.0           Macrophages LPS   0.0           HUVEC none   0.2           HUVEC starved   0.1           HUVEC IL-1beta   0.2           HUVEC IFN gamma   0.2           HUVEC TNF alpha + IFN gamma   0.1           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.1           Lung Microvascular EC none   0.1           Lung Microvascular EC TNFalpha +   0.0           IL-1beta           Microvascular Dermal EC none   0.2           Microsvasular Dermal EC TNFalpha +   0.1           IL-1beta           Bronchial epithelium TNFalpha +   0.5           IL1beta           Small airway epithelium none   0.3           Small airway epithelium TNFalpha +   2.2           IL-1beta           Coronery artery SMC rest   37.4           Coronery artery SMC TNFalpha +   31.4           IL-1beta           Astrocytes rest   13.5           Astrocytes TNFalpha + IL-1beta   7.8           KU-812 (Basophil) rest   0.0           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   0.3           CCD1106 (Keratinocytes) TNFalpha +   0.1           IL-1beta           Liver cirrhosis   3.6           NCI-H292 none   14.5           NCI-H292 IL-4   4.8           NCI-H292 IL-9   17.7           NCI-H292 IL-13   5.6           NCI-H292 IFN gamma   5.3           HPAEC none   0.3           HPAEC TNF alpha + IL-1 beta   1.0           Lung fibroblast none   0.3           Lung fibroblast TNF alpha + IL-1   1.4           beta           Lung fibroblast IL-4   0.2           Lung fibroblast IL-9   0.5           Lung fibroblast IL-13   0.2           Lung fibroblast IFN gamma   0.3           Dermal fibroblast CCD1070 rest   93.3           Dermal fibroblast CCD1070 TNF alpha   100.0           Dermal fibroblast CCD1070 IL-1 beta   56.6           Dermal fibroblast IFN gamma   22.8           Dermal fibroblast IL-4   69.3           Dermal Fibroblasts rest   14.6           Neutrophils TNFa + LPS   0.0           Neutrophils rest   0.0           Colon   0.5           Lung   1.4           Thymus   0.2           Kidney   3.0                        
     [0714] AI_comprehensive panel_v1.0 Summary: Ag6776 Highest expression of this gene is seen in normal tissue adjacent to psoriasis (CT=19.7). Overall, this gene is highly expressed in many samples on this panel, including clusters of samples derived from psoriasis derived tissue. Please see Panel 4.1 D for discussion of utility of this gene in autoimmune disease.  
     [0715] CNS_neurodegeneration_v1.0 Summary: Ag6776 This panel does not show differential expression of this gene in Alzheimer&#39;s disease. However, this expression profile confirms the presence of this gene at moderate levels in the brain. The insulin and insulin-like growth factors belong to a family of polypeptides essential for proper regulation of physiologic processes such as energy metabolism, cell proliferation, development, and differentiation. The insulin-like growth factors bind to IGF with high affinity and compete with the IGF receptor for IGF binding. Transgenic mice overexpressing insulin-like growth factor binding proteins (IGFBPs) tend to show brain developmental abnormalities, suggesting a role for these proteins in neurodevelopment. Furthermore, treatment with glycosaminoglycans (which increases muscle re-innervation after motor neuron death) upregulates serum levels of both IGF and IGFBP. Thus, on the basis of its homology to other established IGFBPs, the novel IGFBP encoded by this gene may be useful in the treatment of diseases such as ALS, multiple sclerosis, and peripheral nerve injury on the basis of its homology to other established IGFBPs. [Dave Stone] 
     [0716] General_screening_panel_v1.6 Summary: Ag6776 Highest expression of this gene is seen in a brain cancer cell line (CT=20.5). In addition, high levels of expression are seen in a cluster of brain cancer cell lines, melanoma cell lines, renal cancer cell lines, and ovarian cancer cell lines. This gene encodes a putative insulin like growth factor binding protein 3 (IGFBP3). IGFBP-3 enhances the p53-dependent apoptotic response of colorectal cells to DNA damage and is inversely associated with risk for colorectal cancer. Expression of IGFBP-3 induces growth inhibition and differentiation of the human colon carcinoma cell line, Caco-2. Thus, therapeutic targeting modulation of this gene product may be useful in the treatment of cancer, especially in those cancer types, like brain and renal tumors where the gene is overexpressed in the tumor cell line compared to the normal tissue sample.  
     [0717] This gene is also expressed at moderate levels in all regions of the CNS examined. Please see Panel CNS_neurodegeneration_v1.0 for discussion of utility of this gene in the CNS.  
     [0718] Among tissues with metabolic function, this gene is expressed at high to moderate levels in pituitary, adipose, adrenal gland, pancreas, thyroid, and adult and fetal skeletal muscle, heart, and liver. Cortizo et. al has suggested that alterations in IGFBP3 levels may result in diabetic complications (Acta Diabetol 1998 July;35(2):85-90). This expression among these tissues suggests that this gene product may play a role in normal neuroendocrine and metabolic function and that disregulated expression of this gene may contribute to neuroendocrine disorders or metabolic diseases, such as obesity and diabetes.  
     [0719] Panel 4.1D Summary: Ag6776 Highest expression of this gene is seen in TNF-alpha stimulated dermal fibroblasts (CT=25.3). In addition, high levels of expression are seen in a cluster of treated and untreated samples derived from dermal fibroblasts. Miura has suggested that dermal fibroblasts promote IGFBP mediated keratinocyte proliferation and may contribute to the epidermal hyperplasia manifest in psoriasis (Arch Dermatol Res 2000 December;292(12):590-7). Thus, based on the homology of this gene to IGFBP3 and the expression in dermal fibroblasts and psoriasis related tissue on AI_comprehensive panel_v1.0, modulation of the expression or function of this gene may be useful in the clinical management of this disease.  
     [0720] E. NOV5a (CG124445-02): Transmembrane Kuzbanian  
     [0721] Expression of gene CG124445-02 was assessed using the primer-probe set Ag7026, described in Table EA.  
                   TABLE EA                          Probe Name Ag/7026                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gattatcttacaatgtggattcattacac-3′   29   330   235                   Probe   TET-5′-accagcgtgccaaaagagcagtctct-3′-   26   366   236           TAMRA               Reverse   5′-aacttcgtgagcaaaagtaatgtg-3′   24   392   237                  
 
     [0722] CNS_neurodegeneration_v1.0 Summary: Ag7026 Expression of the CG124445-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0723] General_screening_panel_v1.6 Summary: Ag7026 Expression of the CG124445-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0724] Panel 4.1D Summary: Ag7026 Expression of the CG124445-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0725] F. NOV6a (CG124590-02): Integrin Beta-4 Precursor  
     [0726] Expression of gene CG124590-02 was assessed using the primer-probe set Ag6832, described in Table FA. Results of the RTQ-PCR runs are shown in Tables FB and EC. Please note that CG124590-02 represents a full-length physical clone.  
                   TABLE FA                          Probe Name Ag6832                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-atgatctggacaacctcaagaa-3′   22   493   238                   Probe   TET-5′-ctcaggacccgagccaggttctgc-3′-   24   521   239           TAMRA               Reverse   5′-gtggcgctggtgagct-3′   16   547   240                  
 
     [0727]               TABLE FB                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%) Ag6832,           Tissue Name   Run 278022742                                         AD 1 Hippo   14.4           AD 2 Hippo   45.1           AD 3 Hippo   8.4           AD 4 Hippo   22.4           AD 5 Hippo   19.5           AD 6 Hippo   100.0           Control 2 Hippo   18.9           Control 4 Hippo   50.0           Control (Path) 3 Hippo   8.4           AD 1 Temporal Ctx   16.8           AD 2 Temporal Ctx   26.1           AD 3 Temporal Ctx   5.0           AD 4 Temporal Ctx   20.2           AD 5 Inf Temporal Ctx   44.4           AD 5 Sup Temporal Ctx   45.7           AD 6 Inf Temporal Ctx   67.4           AD 6 Sup Temporal Ctx   74.2           Control 1 Temporal Ctx   7.2           Control 2 Temporal Ctx   12.9           Control 3 Temporal Ctx   9.1           Control 3 Temporal Ctx   17.2           Control (Path) 1 Temporal Ctx   11.5           Control (Path) 2 Temporal Ctx   7.4           Control (Path) 3 Temporal Ctx   10.4           Control (Path) 4 Temporal Ctx   12.9           AD 1 Occipital Ctx   6.3           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   4.8           AD 4 Occipital Ctx   16.2           AD 5 Occipital Ctx   12.4           AD 6 Occipital Ctx   13.7           Control 1 Occipital Ctx   4.6           Control 2 Occipital Ctx   11.0           Control 3 Occipital Ctx   9.0           Control 4 Occipital Ctx   14.7           Control (Path) 1 Occipital Ctx   23.3           Control (Path) 2 Occipital Ctx   4.0           Control (Path) 3 Occipital Ctx   4.1           Control (Path) 4 Occipital Ctx   4.3           Control 1 Parietal Ctx   10.8           Control 2 Parietal Ctx   33.9           Control 3 Parietal Ctx   9.4           Control (Path) 1 Parietal Ctx   15.5           Control (Path) 2 Parietal Ctx   9.2           Control (Path) 3 Parietal Ctx   7.4           Control (Path) 4 Parietal Ctx   12.7                        
     [0728]               TABLE FC                          Panel 4.1D                                 Rel. Exp. (%)               Ag6832, Run           Tissue Name   278022641                                         Secondary Th1 act   0.0           Secondary Th2 act   0.1           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.0           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.0           Primary Th1 rest   0.0           Primary Th2 rest   0.0           Primary Tr1 rest   0.0           CD45RA CD4 lymphocyte act   0.0           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.0           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   0.0           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0           LAK cells rest   0.0           LAK cells IL-2   0.0           LAK cells IL-2 + IL-12   0.0           LAK cells IL-2 + IFN gamma   0.0           LAK cells IL-2 + IL-18   0.0           LAK cells PMA/ionomycin   0.0           NK Cells IL-2 rest   0.0           Two Way MLR 3 day   0.0           Two Way MLR 5 day   0.0           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   0.0           PBMC PHA-L   0.1           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   0.1           EOL-1 dbcAMP   0.0           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   0.0           Dendritic cells LPS   0.0           Dendritic cells anti-CD40   0.0           Monocytes rest   0.0           Monocytes LPS   0.0           Macrophages rest   0.0           Macrophages LPS   0.0           HUVEC none   0.3           HUVEC starved   0.2           HUVEC IL-1beta   0.1           HUVEC IFN gamma   0.4           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.7           Lung Microvascular EC none   4.9           Lung Microvascular EC TNFalpha +   0.3           IL-1beta           Microvascular Dermal EC none   1.5           Microsvasular Dermal EC TNFalpha +   0.4           IL-1beta           Bronchial epithelium TNFalpha +   50.0           IL1beta           Small airway epithelium none   50.3           Small airway epithelium TNFalpha +   75.3           IL-1beta           Coronery artery SMC rest   0.0           Coronery artery SMC TNFalpha +   0.0           IL-1beta           Astrocytes rest   0.0           Astrocytes TNFalpha + IL-1beta   0.3           KU-812 (Basophil) rest   0.0           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   100.0           CCD1106 (Keratinocytes) TNFalpha +   33.4           IL-1beta           Liver cirrhosis   1.2           NCI-H292 none   20.7           NCI-H292 IL-4   34.6           NCI-H292 IL-9   25.2           NCI-H292 IL-13   40.9           NCI-H292 IFN gamma   17.2           HPAEC none   3.0           HPAEC TNF alpha + IL-1 beta   1.5           Lung fibroblast none   0.0           Lung fibroblast TNF alpha + IL-1   0.0           beta           Lung fibroblast IL-4   0.0           Lung fibroblast IL-9   0.0           Lung fibroblast IL-13   0.0           Lung fibroblast IFN gamma   0.0           Dermal fibroblast CCD1070 rest   0.0           Dermal fibroblast CCD1070 TNF alpha   0.0           Dermal fibroblast CCD1070 IL-1 beta   0.0           Dermal fibroblast IFN gamma   0.0           Dermal fibroblast IL-4   0.0           Dermal Fibroblasts rest   0.0           Neutrophils TNFa + LPS   0.1           Neutrophils rest   0.2           Colon   1.7           Lung   0.3           Thymus   0.4           Kidney   0.9                        
     [0729] CNS_neurodegeneration_v1.0 Summary: Ag6832 This panel confirms the expression of this gene at low levels in the brains of an independent group of individuals. However, no differential expression of this gene was detected between Alzheimer&#39;s diseased postmortem brains and those of non-demented controls in this experiment. Expression of this gene in the brain suggests that the protein encoded by this gene may play a role in central nervous system disorders such as Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0730] General_screening_panel_v1.6 Summary: Ag6832 Results from one experiment with the CG124590-02 gene are not included. The amp plot indicates that there were experimental difficulties with this run.  
     [0731] Panel 4.1D Summary: Ag6832 Highest expression of the CG124590-02 gene is detected in keratinocytes (CT=25). High levels of expression of this gene is also detected in small airway epithelium, cytokine treated bronchial epithelium, and NCI-H292 cells. Therefore, expression of this gene may be used to distinguish these samples from other samples in this panel. In addition, moderate levels of expression of this gene is also seen in HPAEC, HUVEC, lung microvascular EC, microvascular dermal EC and neutrophils. Therefore, therapeutic modulation of this gene may be useful in the treatment of autoimmune and inflammatory diseases that involve endothelial cells, such as lupus erythematosus, asthma, emphysema, Crohn&#39;s disease, ulcerative colitis, rheumatoid arthritis, osteoarthritis, and psoriasis.  
     [0732] Low to moderate levels of expression of this gene is also seen in normal tissues represented by colon, lung, thymus and kidney. Therefore, therapeutic modulation of the protein encoded this gene may be useful in the treatment of autoimmune and inflammatory diseases that affect these tissues.  
     [0733] G. NOV7a (CG124916-01): Selenoprotein P  
     [0734] Expression of gene CG124916-01 was assessed using the primer-probe set Ag7029, described in Table GA.  
                   TABLE GA                          Probe Name Ag7029                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-cagtgactgtggttgctcttct-3′   22   158   241                   Probe   TET-5′-tcaagcctcattttatgtatttcttccca-3′-   29   180   242           TAMRA               Reverse   5′-ttactcgcaggtcttctaatctaaaatat-3′   29   210   243                  
 
     [0735] CNS_neurodegeneration_v1.0 Summary: Ag7029 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0736] General_screening_panel_v1.6 Summary: Ag7029 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0737] Panel 4.1D Summary: Ag7029 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0738] H. NOV8a (CG126224-01): Novel Type II Membrane Protein with 3 C2 Domains  
     [0739] Expression of gene CG126224-01 was assessed using the primer-probe set Ag4713, described in Table HA. Results of the RTQ-PCR runs are shown in Tables HB, HC and HD.  
                   TABLE HA                          Probe Name Ag4713                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-agttaaacaggcccacagatgt-3′   22   551   244                   Probe   TET-5′-tctgaaagatcctcattatcctgacca-3′-   27   582   245           TAMRA               Reverse   5′-gagcaaaatgattccaagatca-3′   22   609   246                  
 
     [0740]               TABLE HB                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%) Ag4713,           Tissue Name   Run 224705458                                         AD 1 Hippo   7.2           AD 2 Hippo   22.5           AD 3 Hippo   9.9           AD 4 Hippo   3.4           AD 5 Hippo   91.4           AD 6 Hippo   51.4           Control 2 Hippo   42.0           Control 4 Hippo   4.6           Control (Path) 3 Hippo   4.8           AD 1 Temporal Ctx   8.9           AD 2 Temporal Ctx   29.3           AD 3 Temporal Ctx   4.8           AD 4 Temporal Ctx   11.5           AD 5 Inf Temporal Ctx   97.9           AD 5 Sup Temporal Ctx   3.4           AD 6 Inf Temporal Ctx   56.3           AD 6 Sup Temporal Ctx   50.7           Control 1 Temporal Ctx   5.4           Control 2 Temporal Ctx   69.3           Control 3 Temporal Ctx   13.3           Control 4 Temporal Ctx   7.3           Control (Path) 1 Temporal Ctx   82.4           Control (Path) 2 Temporal Ctx   28.1           Control (Path) 3 Temporal Ctx   4.0           Control (Path) 4 Temporal Ctx   35.1           AD 1 Occipital Ctx   8.4           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   4.2           AD 4 Occipital Ctx   8.2           AD 5 Occipital Ctx   20.7           AD 6 Occipital Ctx   61.6           Control 1 Occipital Ctx   20.7           Control 2 Occipital Ctx   52.5           Control 3 Occipital Ctx   8.7           Control 4 Occipital Ctx   2.4           Control (Path) 1 Occipital Ctx   100.0           Control (Path) 2 Occipital Ctx   6.0           Control (Path) 3 Occipital Ctx   2.6           Control (Path) 4 Occipital Ctx   11.4           Control 1 Parietal Ctx   4.7           Control 2 Parietal Ctx   42.3           Control 3 Parietal Ctx   15.2           Control (Path) 1 Parietal Ctx   98.6           Control (Path) 2 Parietal Ctx   18.3           Control (Path) 3 Parietal Ctx   4.0           Control (Path) 4 Parietal Ctx   41.2                        
     [0741]               TABLE HC                          General_screening_panel_v1.4                                 Rel. Exp. (%) Ag4713,           Tissue Name   Run 222825921                                         Adipose   18.8           Melanoma* Hs688(A).T   0.0           Melanoma* Hs688(B).T   0.0           Melanoma* M14   39.8           Melanoma* LOXIMVI   42.6           Melanoma* SK-MEL-5   65.5           Squamous cell carcinoma SCC-4   10.5           Testis Pool   4.3           Prostate ca.* (bone met) PC-3   72.7           Prostate Pool   2.8           Placenta   1.3           Uterus Pool   5.8           Ovarian ca. OVCAR-3   17.0           Ovarian ca. SK-OV-3   79.0           Ovarian ca. OVCAR-4   0.1           Ovarian ca. OVCAR-5   42.9           Ovarian ca. IGROV-1   1.1           Ovarian ca. OVCAR-8   5.1           Ovary   2.1           Breast ca. MCF-7   0.0           Breast ca. MDA-MB-231   11.1           Breast ca. BT 549   16.8           Breast ca. T47D   66.9           Breast ca. MDA-N   57.4           Breast Pool   9.6           Trachea   8.7           Lung   1.3           Fetal Lung   10.4           Lung ca. NCI-N417   0.0           Lung ca. LX-1   59.5           Lung ca. NCI-H146   10.5           Lung ca. SHP-77   7.2           Lung ca. A549   6.7           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   2.5           Lung ca. NCI-H460   29.9           Lung ca. HOP-62   21.2           Lung ca. NCI-H522   7.4           Liver   0.3           Fetal Liver   4.3           Liver ca. HepG2   0.1           Kidney Pool   18.0           Fetal Kidney   2.5           Renal ca. 786-0   17.0           Renal ca. A498   9.9           Renal ca. ACHN   39.2           Renal ca. UO-31   41.5           Renal ca. TK-10   30.4           Bladder   15.0           Gastric ca. (liver met.) NCI-N87   34.2           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.0           Colon ca. SW480   9.3           Colon ca.* (SW480 met) SW620   16.6           Colon ca. HT29   9.0           Colon ca. HCT-116   0.3           Colon ca. CaCo-2   0.9           Colon cancer tissue   20.6           Colon ca. SW1116   0.0           Colon ca. Colo-205   3.8           Colon ca. SW-48   0.0           Colon Pool   9.9           Small Intestine Pool   5.7           Stomach Pool   6.9           Bone Marrow Pool   4.0           Fetal Heart   1.0           Heart Pool   4.2           Lymph Node Pool   8.8           Fetal Skeletal Muscle   4.5           Skeletal Muscle Pool   4.8           Spleen Pool   10.3           Thymus Pool   9.4           CNS cancer (glio/astro) U87-MG   100.0           CNS cancer (glio/astro) U-118-MG   9.2           CNS cancer (neuro; met) SK-N-AS   1.9           CNS cancer (astro) SF-539   2.5           CNS cancer (astro) SNB-75   0.2           CNS cancer (glio) SNB-19   1.3           CNS cancer (glio) SF-295   0.9           Brain (Amygdala) Pool   20.4           Brain (cerebellum)   33.9           Brain (fetal)   30.1           Brain (Hippocampus) Pool   20.6           Cerebral Cortex Pool   34.6           Brain (Substantia nigra) Pool   26.8           Brain (Thalamus) Pool   40.3           Brain (whole)   28.5           Spinal Cord Pool   5.4           Adrenal Gland   2.4           Pituitary gland Pool   2.7           Salivary Gland   0.6           Thyroid (female)   1.3           Pancreatic ca. CAPAN2   11.0           Pancreas Pool   7.7                        
     [0742]               TABLE HD                          Panel 4.1D                                 Rel. Exp. (%)               Ag4713, Run           Tissue Name   202012796                                         Secondary Th1 act   0.2           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.2           Secondary Th2 rest   0.1           Secondary Tr1 rest   0.2           Primary Th1 act   0.9           Primary Th2 act   0.5           Primary Tr1 act   1.4           Primary Th1 rest   1.7           Primary Th2 rest   0.7           Primary Tr1 rest   1.0           CD45RA CD4 lymphocyte act   0.4           CD45RO CD4 lymphocyte act   0.2           CD8 lymphocyte act   0.1           Secondary CD8 lymphocyte rest   0.9           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   1.2           2ry Th1/Th2/Tr1_anti-CD95 CH11   1.5           LAK cells rest   20.0           LAK cells IL-2   0.7           LAK cells IL-2 + IL-12   2.5           LAK cells IL-2 + IFN gamma   1.3           LAK cells IL-2 + IL-18   0.7           LAK cells PMA/ionomycin   33.9           NK Cells IL-2 rest   0.4           Two Way MLR 3 day   27.2           Two Way MLR 5 day   12.0           Two Way MLR 7 day   1.8           PBMC rest   5.3           PBMC PWM   3.7           PBMC PHA-L   6.4           Ramos (B cell) none   0.2           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   2.6           B lymphocytes CD40L and IL-4   2.8           EOL-1 dbcAMP   35.4           EOL-1 dbcAMP PMA/ionomycin   41.8           Dendritic cells none   8.1           Dendritic cells LPS   12.7           Dendritic cells anti-CD40   6.8           Monocytes rest   41.8           Monocytes LPS   88.3           Macrophages rest   20.4           Macrophages LPS   22.4           HUVEC none   25.7           HUVEC starved   82.4           HUVEC IL-1beta   55.1           HUVEC IFN gamma   100.0           HUVEC TNF alpha + IFN gamma   63.3           HUVEC TNF alpha + IL4   91.4           HUVEC IL-11   33.7           Lung Microvascular EC none   50.3           Lung Microvascular EC TNFalpha +   58.2           IL-1beta           Microvascular Dermal EC none   11.8           Microsvasular Dermal EC TNFalpha +   20.7           IL-1beta           Bronchial epithelium TNFalpha +   6.3           IL1beta           Small airway epithelium none   1.2           Small airway epithelium TNFalpha +   1.8           IL-1beta           Coronery artery SMC rest   0.2           Coronery artery SMC TNFalpha +   1.2           IL-1beta           Astrocytes rest   1.2           Astrocytes TNFalpha + IL-1beta   0.7           KU-812 (Basophil) rest   2.8           KU-812 (Basophil) PMA/ionomycin   11.7           CCD1106 (Keratinocytes) none   0.2           CCD1106 (Keratinocytes) TNFalpha +   0.3           IL-1beta           Liver cirrhosis   3.5           NCI-H292 none   7.9           NCI-H292 IL-4   7.7           NCI-H292 IL-9   12.9           NCI-H292 IL-13   5.0           NCI-H292 IFN gamma   5.2           HPAEC none   7.1           HPAEC TNF alpha + IL-1 beta   15.1           Lung fibroblast none   0.7           Lung fibroblast TNF alpha + IL-1   1.5           beta           Lung fibroblast IL-4   1.2           Lung fibroblast IL-9   2.5           Lung fibroblast IL-13   1.5           Lung fibroblast IFN gamma   1.2           Dermal fibroblast CCD1070 rest   0.1           Dermal fibroblast CCD1070 TNF alpha   0.4           Dermal fibroblast CCD1070 IL-1 beta   0.6           Dermal fibroblast IFN gamma   0.4           Dermal fibroblast IL-4   0.4           Dermal Fibroblasts rest   0.2           Neutrophils TNFa + LPS   71.2           Neutrophils rest   18.0           Colon   1.3           Lung   5.9           Thymus   10.3           Kidney   1.3                        
     [0743] CNS_neurodegeneration_v1.0 Summary: Ag4713 This panel confirms the expression of the CG126224-01 gene at low levels in the brains of an independent group of individuals. However, no differential expression of this gene was detected between Alzheimer&#39;s diseased postmortem brains and those of non-demented controls in this experiment. Please see Panel 1.4 for a discussion of the potential utility of this gene in treatment of central nervous system disorders.  
     [0744] General_screening_panel_v1.4 Summary: Ag4713 Highest expression of the CG126224-01 gene is detected in CNS cancer U87-MG cell line (CT=28.8). Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, liver, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of pancreatic, gastric, colon, lung, liver, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.  
     [0745] Among tissues with metabolic or endocrine function, this gene is expressed at moderate to low levels in pancreas, adipose, adrenal gland, pituitary gland, skeletal muscle, heart, fetal liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0746] Interestingly, this gene is expressed at much higher levels in fetal (CT=32-33) when compared to adult lung and liver (CT=35-37). This observation suggests that expression of this gene can be used to distinguish fetal from adult lung and liver, respectively. In addition, the relative overexpression of this gene in fetal tissue suggests that the protein product may enhance liver and lung growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of liver and lung related diseases.  
     [0747] In addition, this gene is expressed at moderate levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0748] Panel 4.1D Summary: Ag4713 Highest expression of the CG126224-01 gene is detected in IFN gamma treated HUVEC cells (CT=28). High to moderate levels of expression in LAK cells, two way MLR, PBMC, B lymphocytes, eosinophils, dendritic cells, monocytes, macrophages, endothelial cells, small airway epithelium, basophils, NCI-H292, lung fibroblast and activated neutrophils. In addition, moderate to low levels of expression of this gene is also seen in liver cirrhosis and normal tissues represented by colon, lung, thymus and kidney. Therefore, therapeutic modulation of this gene may be useful in the treatment of inflammatory and autoimmune diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, osteoarthritis and liver cirrhosis.  
     [0749] I. NOV9a (CG126233-01): ctl2  
     [0750] Expression of gene CG 126233-01 was assessed using the primer-probe set Ag4722, described in Table IA. Results of the RTQ-PCR runs are shown in Tables IB, IC and ID.  
                   TABLE IA                          Probe Name Ag4722                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-gcatgtactttgaactgcaaca-3′   22   947   247                   Probe   TET-5′-catggttcacatttatgataatactctgca-   30   971   248           3′-TAMRA               Reverse   5′-agcatgaggatgacaatcactt-3′   22   1007   249                  
 
     [0751]               TABLE IB                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%) Ag4722,           Tissue Name   Run 224706358                                         AD 1 Hippo   4.2           AD 2 Hippo   11.7           AD 3 Hippo   2.5           AD 4 Hippo   4.1           AD 5 hippo   93.3           AD 6 Hippo   27.9           Control 2 Hippo   18.3           Control 4 Hippo   8.0           Control (Path) 3 Hippo   3.0           AD 1 Temporal Ctx   4.6           AD 2 Temporal Ctx   21.0           AD 3 Temporal Ctx   2.2           AD 4 Temporal Ctx   14.9           AD 5 Inf Temporal Ctx   35.8           AD 5 Sup Temporal Ctx   20.4           AD 6 Inf Temporal Ctx   35.4           AD 6 Sup Temporal Ctx   26.8           Control 1 Temporal Ctx   1.7           Control 2 Temporal Ctx   26.4           Control 3 Temporal Ctx   11.7           Control 4 Temporal Ctx   5.5           Control (Path) 1 Temporal Ctx   56.6           Control (Path) 2 Temporal Ctx   23.5           Control (Path) 3 Temporal Ctx   2.0           Control (Path) 4 Temporal Ctx   34.4           AD 1 Occipital Ctx   5.3           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   3.1           AD 4 Occipital Ctx   12.3           AD 5 Occipital Ctx   14.8           AD 6 Occipital Ctx   29.1           Control 1 Occipital Ctx   2.9           Control 2 Occipital Ctx   69.7           Control 3 Occipital Ctx   13.6           Control 4 Occipital Ctx   4.8           Control (Path) 1 Occipital Ctx   100.0           Control (Path) 2 Occipital Ctx   15.9           Control (Path) 3 Occipital Ctx   0.7           Control (Path) 4 Occipital Ctx   25.5           Control 1 Parietal Ctx   3.1           Control 2 Parietal Ctx   24.3           Control 3 Parietal Ctx   2.2           Control (Path) 1 Parietal Ctx   65.5           Control (Path) 2 Parietal Ctx   15.9           Control (Path) 3 Parietal Ctx   1.7           Control (Path) 4 Parietal Ctx   37.4                        
     [0752]               TABLE IC                          General_screening_panel_v1.4                                 Rel. Exp. (%) Ag4722,           Tissue Name   Run 222842372                                         Adipose   0.3           Melanoma* Hs688(A).T   0.0           Melanoma* Hs688(B).T   0.0           Melanoma* M14   0.0           Melanoma* LOXIMVI   0.4           Melanoma* SK-MEL-5   0.0           Squamous cell carcinoma SCC-4   9.0           Testis Pool   7.4           Prostate ca.* (bone met) PC-3   0.1           Prostate Pool   0.3           Placenta   4.7           Uterus Pool   0.2           Ovarian ca. OVCAR-3   6.4           Ovarian ca. SK-OV-3   1.7           Ovarian ca. OVCAR-4   0.2           Ovarian ca. OVCAR-5   8.8           Ovarian ca. IGROV-1   8.8           Ovarian ca. OVCAR-8   3.5           Ovary   1.9           Breast ca. MCF-7   0.0           Breast ca. MDA-MB-231   0.2           Breast ca. BT 549   0.3           Breast ca. T47D   11.3           Breast ca. MDA-N   0.2           Breast Pool   0.5           Trachea.   4.0           Lung   0.8           Fetal Lung   1.8           Lung ca. NCI-N417   3.6           Lung ca. LX-1   40.9           Lung ca. NCI-H146   17.3           Lung ca. SHP-77   42.9           Lung ca. A549   1.4           Lung ca. NCI-H526   10.7           Lung ca. NCI-H23   52.1           Lung ca. NCI-H460   6.1           Lung ca. HOP-62   5.2           Lung ca. NCI-H522   0.2           Liver   0.0           Fetal Liver   2.1           Liver ca. HepG2   12.4           Kidney Pool   1.2           Fetal Kidney   6.9           Renal ca. 786-0   0.1           Renal ca. A498   0.7           Renal ca. ACHN   0.3           Renal ca. UO-31   5.8           Renal ca. TK-10   5.0           Bladder   1.8           Gastric ca. (liver met.) NCI-N87   100.0           Gastric ca. KATO III   10.6           Colon ca. SW-948   3.2           Colon ca. SW480   4.8           Colon ca.* (SW480 met) SW620   13.2           Colon ca. HT29   8.0           Colon ca. HCT-116   4.9           Colon ca. CaCo-2   24.0           Colon cancer tissue   0.2           Colon ca. SW1116   2.9           Colon ca. Colo-205   0.4           Colon ca. SW-48   2.6           Colon Pool   0.4           Small Intestine Pool   0.5           Stomach Pool   0.6           Bone Marrow Pool   0.1           Fetal Heart   2.4           Heart Pool   0.1           Lymph Node Pool   0.4           Fetal Skeletal Muscle   0.2           Skeletal Muscle Pool   5.7           Spleen Pool   0.7           Thymus Pool   0.8           CNS cancer (glio/astro) U87-MG   0.4           CNS cancer (glio/astro) U-118-MG   0.6           CNS cancer (neuro; met) SK-N-AS   5.2           CNS cancer (astro) SF-539   2.2           CNS cancer (astro) SNB-75   0.9           CNS cancer (glio) SNB-19   10.2           CNS cancer (glio) SF-295   1.5           Brain (Amygdala) Pool   3.3           Brain (cerebellum)   0.4           Brain (fetal)   94.0           Brain (Hippocampus) Pool   2.8           Cerebral Cortex Pool   5.2           Brain (Substantia nigra) Pool   4.2           Brain (Thalamus) Pool   4.6           Brain (whole)   6.4           Spinal Cord Pool   2.1           Adrenal Gland   1.0           Pituitary gland Pool   1.9           Salivary Gland   0.2           Thyroid (female)   0.3           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   2.2                        
     [0753]               TABLE ID                          Panel 4.1D                                 Rel. Exp. (%)               Ag4722, Run           Tissue Name   204172542                                         Secondary Th1 act   0.0           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.7           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.0           Primary Th1 rest   0.9           Primary Th2 rest   0.8           Primary Tr1 rest   3.3           CD45RA CD4 lymphocyte act   0.0           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.6           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   1.5           2ry Th1/Th2/Tr1_anti-CD95 CH11   3.6           LAK cells rest   0.0           LAK cells IL-2   0.0           LAK cells IL-2 + IL-12   0.0           LAK cells IL-2 + IFN gamma   0.0           LAK cells IL-2 + IL-18   0.0           LAK cells PMA/ionomycin   0.0           NK Cells IL-2 rest   1.0           Two Way MLR 3 day   0.0           Two Way MLR 5 day   0.0           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   0.6           PBMC PHA-L   0.0           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   0.6           EOL-1 dbcAMP   0.0           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   0.0           Dendritic cells LPS   0.0           Dendritic cells anti-CD40   0.0           Monocytes rest   0.0           Monocytes LPS   0.0           Macrophages rest   0.8           Macrophages LPS   0.0           HUVEC none   3.8           HUVEC starved   7.7           HUVEC IL-1beta   2.0           HUVEC IFN gamma   9.3           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   4.2           HUVEC IL-11   6.3           Lung Microvascular EC none   16.2           Lung Microvascular EC TNFalpha +   6.3           IL-1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   0.0           IL1beta           Small airway epithelium none   6.8           Small airway epithelium TNFalpha +   5.7           IL-1beta           Coronery artery SMC rest   0.8           Coronery artery SMC TNFalpha + IL-   2.5           1beta           Astrocytes rest   5.7           Astrocytes TNFalpha + IL-1beta   4.6           KU-812 (Basophil) rest   0.0           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   0.0           CCD1106 (Keratinocytes) TNFalpha +   0.0           IL-1beta           Liver cirrhosis   0.0           NCI-H292 none   50.0           NCI-H292 IL-4   53.6           NCI-H292 IL-9   100.0           NCI-H292 IL-13   71.2           NCI-H292 IFN gamma   39.8           HPAEC none   7.4           HPAEC TNF alpha + IL-1 beta   9.5           Lung fibroblast none   0.0           Lung fibroblast TNF alpha + IL-1   0.0           beta           Lung fibroblast IL-4   0.0           Lung fibroblast IL-9   0.6           Lung fibroblast IL-13   0.0           Lung fibroblast IFN gamma   0.0           Dermal Fibroblast CCD1070 rest   0.0           Dermal fibroblast CCD1070 TNF alpha   0.9           Dermal fibroblast CCD1070 IL-1 beta   0.6           Dermal fibroblast IFN gamma   0.0           Dermal fibroblast IL-4   0.0           Dermal Fibroblasts rest   0.0           Neutrophils TNFa + LPS   0.0           Neutrophils rest   0.0           Colon   0.0           Lung   0.0           Thymus   4.0           Kidney   0.7                        
     [0754] CNS_neurodegeneration_v1.0 Summary: Ag4722 This panel does not show differential expression of this gene in Alzheimer&#39;s disease. However, this expression profile confirms the presence of this gene in the brain. Please see Panel 1.4 for discussion of utility of this gene in the central nervous system.  
     [0755] General_screening_panel_v1.4 Summary: Ag4722 This gene is expressed at moderate levels throughout many of the samples in this panel. Highest expression is detected in an gastric cancer cell line (CT=29). In addition, this gene is also expressed in a cluster of samples derived from lung cancer cell lines and at low but significant levels in cell lines derived from ovarian, colon and brain cancers. Therefore, therapeutic modulation of this gene or its protein product, through the use of antibodies, might be useful in the treatment of these cancers.  
     [0756] Among tissues involved in metabolic function, this gene is expressed in the pancreas, pituitary, fetal liver, fetal heart and skeletal muscle. Therefore, this gene or its protein product may be important in the pathogenesis and/or treatment of disease of obesity and diabetes.  
     [0757] There is widespread moderate expression of this gene across many of the samples derived from the CNS, including the amygdala, hippocampus, thalamus, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of the expression or function of this gene may be useful in the treatment of neurologic disorders, such as Alzheimer&#39;s disease, Parkinson&#39;s disease, schizophrenia, multiple sclerosis, stroke and epilepsy.  
     [0758] Panel 4.1D Summary: Ag4722 This transcript is most highly expressed in NCI-H292 cells stimulated by IL-9 (CT=32.5). The gene is also expressed in a cluster of treated and untreated samples derived from the NCI-H292 cell line, a human airway epithelial cell line that produces mucins. Mucus overproduction is an important feature of bronchial asthma and chronic obstructive pulmonary disease samples. The transcript is also expressed at lower but still significant levels in small airway epithelium treated with IL-1 beta and TNF-alpha. The expression of the transcript in this mucoepidermoid cell line that is often used as a model for airway epithelium (NCI-H292 cells) suggests that this transcript may be important in the proliferation or activation of airway epithelium. Therefore, therapeutics designed with the protein encoded by the transcript may reduce or eliminate symptoms caused by inflammation in lung epithelia in chronic obstructive pulmonary disease, asthma, allergy, and emphysema.  
     [0759] J. NOV10a (CG126600-01): Fibronectin Type III Domain-Membrane Protein  
     [0760] Expression of gene CG126600-01 was assessed using the primer-probe set Ag7030, described in Table JA. Results of the RTQ-PCR runs are shown in Tables JB, JC and JD.  
                   TABLE IA                          Probe Name Ag7030                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-acatccaccactactqgatacaa-3′   23   89   250                   Probe   TET-5′-ttctcttttgtctgcccctattgtaagtgc-   30   134   251           3′-TAMRA               Reverse   5′-cagaataacctgttgtgttccat-3′   23   166   252                  
 
     [0761]               TABLE JB                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%)               Ag7030, Run           Tissue Name   282263009                                         AD 1 Hippo   12.9           AD 2 Hippo   33.2           AD 3 Hippo   9.3           AD 4 Hippo   8.2           AD 5 hippo   59.0           AD 6 Hippo   100.0           Control 2 Hippo   32.1           Control 4 Hippo   11.3           Control (Path) 3 Hippo   5.9           AD 1 Temporal Ctx   19.8           AD 2 Temporal Ctx   26.4           AD 3 Temporal Ctx   4.9           AD 4 Temporal Ctx   29.3           AD 5 Inf Temporal Ctx   62.4           AD 5 Sup Temporal Ctx   40.9           AD 6 Inf Temporal Ctx   57.8           AD 6 Sup Temporal Ctx   67.4           Control 1 Temporal Ctx   4.6           Control 2 Temporal Ctx   32.5           Control 3 Temporal Ctx   13.1           Control 4 Temporal Ctx   8.0           Control (Path) 1 Temporal Ctx   47.0           Control (Path) 2 Temporal Ctx   38.4           Control (Path) 3 Temporal Ctx   4.4           Control (Path) 4 Temporal Ctx   25.3           AD 1 Occipital Ctx   12.5           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   5.1           AD 4 Occipital Ctx   11.5           AD 5 Occipital Ctx   31.9           AD 6 Occipital Ctx   33.0           Control 1 Occipital Ctx   7.5           Control 2 Occipital Ctx   38.2           Control 3 Occipital Ctx   7.6           Control 4 Occipital Ctx   5.8           Control (Path) 1 Occipital Ctx   64.2           Control (Path) 2 Occipital Ctx   10.6           Control (Path) 3 Occipital Ctx   2.5           Control (Path) 4 Occipital Ctx   11.4           Control 1 Parietal Ctx   4.8           Control 2 Parietal Ctx   32.3           Control 3 Parietal Ctx   18.0           Control (Path) 1 Parietal Ctx   45.4           Control (Path) 2 Parietal Ctx   18.4           Control (Path) 3 Parietal Ctx   2.8           Control (Path) 4 Parietal Ctx   34.4                        
     [0762]               TABLE JC                          General_screening_panel_v1.6                                 Rel. Exp. (%)               Ag7030, Run           Tissue Name   281813484                                         Adipose   10.0           Melanoma* Hs688(A).T   8.7           Melanoma* Hs688(B).T   9.5           Melanoma* M14   14.3           Melanoma* LOXIMVI   13.1           Melanoma* SK-MEL-5   100.0           Squamous cell carcinoma SCC-4   6.9           Testis Pool   21.8           Prostate ca.* (bone met) PC-3   13.5           Prostate Pool   14.4           Placenta   75.3           Uterus Pool   6.4           Ovarian ca. OVCAR-3   4.5           Ovarian ca. SK-OV-3   57.8           Ovarian ca. OVCAR-4   4.4           Ovarian ca. OVCAR-5   34.9           Ovarian ca. IGROV-1   25.7           Ovarian ca. OVCAR-8   20.6           Ovary   16.2           Breast ca. MCF-7   18.8           Breast ca. MDA-MB-231   24.8           Breast ca. BT 549   55.9           Breast ca. T47D   2.1           Breast ca. MDA-N   4.9           Breast Pool   24.1           Trachea   29.1           Lung   5.8           Fetal Lung   38.4           Lung ca. NCI-N417   4.8           Lung ca. LX-I   58.6           Lung ca. NCI-H146   8.9           Lung ca. SHP-77   19.1           Lung ca. A549   13.6           Lung ca. NCI-H526   4.8           Lung ca. NCI-H23   52.9           Lung ca. NCI-H460   45.4           Lung ca. HOP-62   6.8           Lung ca. NCI-H522   8.3           Liver   2.6           Fetal Liver   17.7           Liver ca. HepG2   9.8           Kidney Pool   39.0           Fetal Kidney   19.2           Renal ca. 786-0   22.1           Renal ca. A498   3.7           Renal ca. ACHN   14.0           Renal ca. UO-31   27.0           Renal ca. TK-10   27.7           Bladder   42.9           Gastric ca. (liver met.) NCI-N87   53.6           Gastric ca. KATO III   22.8           Colon ca. SW-948   4.6           Colon ca. SW480   26.8           Colon ca.* (SW480 met) SW620   18.7           Colon ca. HT29   5.1           Colon ca. HCT-116   17.9           Colon ca. CaCo-2   18.8           Colon cancer tissue   13.9           Colon ca. SW1116   3.7           Colon ca. Colo-205   4.5           Colon ca. SW-48   5.3           Colon Pool   19.2           Small Intestine Pool   24.3           Stomach Pool   19.6           Bone Marrow Pool   9.9           Fetal Heart   8.2           Heart Pool   11.7           Lymph Node Pool   38.7           Fetal Skeletal Muscle   4.2           Skeletal Muscle Pool   1.5           Spleen Pool   13.5           Thymus Pool   21.9           CMS cancer (glio/astro) U87-MG   14.3           CNS cancer (glio/astro) U-118-MG   73.2           CNS cancer (neuro; met) SK-N-AS   34.6           CNS cancer (astro) SF-539   5.8           CNS cancer (astro) SNB-75   17.0           CNS cancer (glio) SNB-19   27.5           CNS cancer (glio) SF-295   55.9           Brain (Amygdala) Pool   5.8           Brain (cerebellum)   13.1           Brain (fetal)   14.5           Brain (Hippocampus) Pool   9.9           Cerebral Cortex Pool   11.8           Brain (Substantia nigra) Pool   6.0           Brain (Thalamus) Pool   14.7           Brain (whole)   6.0           Spinal Cord Pool   8.0           Adrenal Gland   19.1           Pituitary gland Pool   9.7           Salivary Gland   7.2           Thyroid (female)   9.3           Pancreatic ca. CAPAN2   18.3           Pancreas Pool   33.7                        
     [0763]               TABLE JD                          Panel 4.1D                                 Rel. Exp. (%)               Ag7030, Run           Tissue Name   281810532                                         Secondary Th1 act   9.1           Secondary Th2 act   13.5           Secondary Tr1 act   6.6           Secondary Th1 rest   0.9           Secondary Th2 rest   1.9           Secondary Tr1 rest   1.6           Primary Th1 act   2.8           Primary Th2 act   8.0           Primary Tr1 act   7.7           Primary Th1 rest   1.1           Primary Th2 rest   0.9           Primary Tr1 rest   1.6           CD45RA CD4 lymphocyte act   100.0           CD45RO CD4 lymphocyte act   11.0           CD8 lymphocyte act   3.1           Secondary CD8 lymphocyte rest   5.8           Secondary CD8 lymphocyte act   1.0           CD4 lymphocyte none   1.4           2ry Th1/Th2/Tr1_anti-CD95 CH11   2.1           LAK cells rest   9.8           LAK cells IL-2   3.2           LAK cells IL-2 + IL-12   1.9           Lak cells IL-2 + IFN gamma   2.2           LAK cells IL-2 + IL-18   2.5           Lak cells PMA/ionomycin   42.3           NK Cells IL-2 rest   8.5           Two Way MLR 3 day   3.4           Two Way MLR 5 day   1.1           Two Way MLR 7 day   2.2           PBMC rest   1.1           PBMC PWM   2.2           PBMC PHA-L   1.9           Ramos (B cell) none   8.5           Ramos (B cell) ionomycin   16.8           B lymphocytes PWM   3.6           B lymphocytes CD40L and IL-4   4.4           EOL-1 dbcAMP 1   5.7           EOL-1 dbcAMP PMA/ionomycin   7.7           Dendritic cells none   12.1           Dendritic cells LPS   10.2           Dendritic cells anti-CD40   7.0           Monocytes rest   2.5           Monocytes LPS   21.2           Macrophages rest   3.3           Macrophages LPS   8.1           HUVEC none   2.9           HUVEC starved   3.7           HUVEC IL-1beta   7.0           HUVEC IFN gamma   6.8           HUVEC TNF alpha + IFN gamma   3.0           HUVEC TNF alpha + IL4   1.7           HUVEC IL-11   2.7           Lung Microvascular EC none   12.0           Lung Microvascular EC TNFalpha + IL-   4.1           1beta           Microvascular Dermal EC none   1.7           Microsvasular Dermal EC TNFalpha + IL-   1.3           1beta           Bronchial epithelium TNFalpha + IL1beta   2.0           Small airway epithelium none   1.4           Small airway epithelium TNFalpha + IL-   2.1           1beta           Coronery artery SMC rest   3.7           Coronery artery SMC TNFalpha + IL-1beta   6.2           Astrocytes rest   3.6           Astrocytes TNFalpha + IL-1beta   0.7           KU-812 (Basophil) rest   1.8           KU-812 (Basophil) PMA/ionomycin   11.1           CCD1106 (Keratinocytes) none   2.5           CCD1106 (Keratinocytes) TNFalpha + IL-   3.7           1beta           Liver cirrhosis   1.4           NCI-H292 none   6.8           NCI-H292 IL-4   17.1           NCI-H292 IL-9   10.8           NCI-H292 IL-13   22.8           NCI-H292 IFN gamma   7.5           HPAEC none   2.2           HPAEC TNF alpha + IL-1 beta   8.4           Lung fibroblast none   8.2           Lung fibroblast TNF alpha + IL-1 beta   16.8           Lung fibroblast IL-4   2.4           Lung fibroblast IL-9   8.6           Lung fibroblast IL-13   4.0           Lung fibroblast IFN gamma   12.7           Dermal fibroblast CCD1070 rest   12.8           Dermal fibroblast CCD1070 TNF alpha   17.9           Dermal fibroblast CCD1070 IL-1 beta   16.2           Dermal fibroblast IFN gamma   8.3           Dermal fibroblast IL-4   20.4           Dermal Fibroblasts rest   6.8           Neutrophils TNFa + LPS   8.5           Neutrophils rest   7.6           Colon   2.2           Lung   1.5           Thymus   3.9           Kidney   10.0                        
     [0764] CNS_neurodegeneration v1.0 Summary: Ag7030 This panel confirms the expression of the CG1 26600-01 gene at low levels in the brains of an independent group of individuals. However, no differential expression of this gene was detected between Alzheimer&#39;s diseased postmortem brains and those of non-demented controls in this experiment. Please see Panel 1.6 for a discussion of the potential utility of this gene in treatment of central nervous system disorders.  
     [0765] General_screening_panel_v1.6 Summary: Ag7030 1lighest expression of the CG126600-01 gene is detected in melanoma SK-MEL-5 cell line (CT=25.7). High levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.  
     [0766] Among tissues with metabolic or endocrine function, this gene is expressed at high levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0767] In addition, this gene is expressed at high levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0768] Panel 4.1D Summary: Ag7030 Highest expression of the CG126600-01 gene is detected in activated CD45RA CD4 lymphocyte (CT=26.6). This gene is expressed at high to moderate levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This pattern is in agreement with the expression profile in General_screening_panel_v1.6 and also suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.  
     [0769] K. NOV11a (CG127888-01): Novel Secretory Protein  
     [0770] Expression of gene CG127888-01 was assessed using the primer-probe set Ag4756, described in Table KA. Results of the RTQ-PCR runs are shown in Table KB.  
                   TABLE KA                          Probe Name Ag4756                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-ctttcagaataatggcaaatgg-3′   22   989   253                   Probe   TET-5′-ccagtaacatcttccaaagaaattcgga-3′-   28   1018   254           TAMRA               Reverse   tctcccagattcatgttgactt-3′   22   1050   255                  
 
     [0771]               TABLE KB                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%)               Ag4756, Run           Tissue Name   224721730                                         AD 1 Hippo   0.0           AD 2 Hippo   0.0           AD 3 Hippo   0.0           AD 4 Hippo   0.0           AD 5 hippo   0.0           AD 6 Hippo   0.0           Control 2 Hippo   0.0           Control 4 Hippo   0.0           Control (Path) 3 Hippo   0.0           AD 1 Temporal Ctx   0.0           AD 2 Temporal Ctx   0.0           AD 3 Temporal Ctx   0.0           AD 4 Temporal Ctx   0.0           AD 5 Inf Temporal Ctx   0.0           AD 5 Sup Temporal Ctx   0.0           AD 6 Inf Temporal Ctx   0.0           AD 6 Sup Temporal Ctx   0.0           Control 1 Temporal Ctx   100.0           Control 2 Temporal Ctx   0.0           Control 3 Temporal Ctx   0.0           Control 4 Temporal Ctx   0.0           Control (Path) 1 Temporal Ctx   0.0           Control (Path) 2 Temporal Ctx   0.0           Control (Path) 3 Temporal Ctx   0.0           Control (Path) 4 Temporal Ctx   0.0           AD 1 Occipital Ctx   0.0           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   0.0           AD 4 Occipital Ctx   0.0           AD 5 Occipital Ctx   0.0           AD 6 Occipital Ctx   0.0           Control 1 Occipital Ctx   0.0           Control 2 Occipital Ctx   0.0           Control 3 Occipital Ctx   0.0           Control 4 Occipital Ctx   0.0           Control (Path) 1 Occipital Ctx   0.0           Control (Path) 2 Occipital Ctx   0.0           Control (Path) 3 Occipital Ctx   0.0           Control (Path) 4 Occipital Ctx   0.0           Control 1 Parietal Ctx   0.0           Control 2 Parietal Ctx   0.0           Control 3 Parietal Ctx   0.0           Control (Path) 1 Parietal Ctx   0.0           Control (Path) 2 Parietal Ctx   0.0           Control (Path) 3 Parietal Ctx   0.0           Control (Path) 4 Parietal Ctx   0.0                        
     [0772] CNS_neurodegeneration_v1.0 Summary: Ag4756 Low expression of this gene is seen in control temporal cortex (CT=34.6). Therefore, expression of this gene may be used to distinguish this sample from other samples used in this panel. In addition, therapeutic modulation of this gene may be useful for the treatment of neurological disorders.  
     [0773] General_screening_panel_v1.4 Summary: Ag4756 Expression of the CG127888-01 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0774] Panel 4.1D Summary: Ag4756 Expression of the CG 127888-01 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0775] L. NOV12a (CG128249-02): Ephrin-A4 Precursor  
     [0776] Expression of gene CG128249-02 was assessed using the primer-probe set Ag6833, described in Table LA. Results of the RTQ-PCR runs are shown in Table LB. Please note that CG128249-02 represents a full-length physical clone.  
                   TABLE LA                          Probe Name Ag6833                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gccatgttcaattctcagagaa-3′   22   338   256                   Probe   TET-5′-cttcacacccttctccctcggctt3′-   24   369   257           TAMRA               Reverse   5′-gccactctctccaggtaagaa-3′   21   397   258                  
 
     [0777]               TABLE LB                          General_screening_panel_v1.6                                 Rel. Exp. (%)               Ag6833, Run           Tissue Name   278019620                                         Adipose   0.9           Melanoma* Hs688(A).T   4.5           Melanoma* Hs688(B).T   4.5           Melanoma* M14   3.8           Melanoma* LOXIMVI   8.0           Melanoma* SK-MEL-5   16.5           Squamous cell carcinoma SCC-4   6.7           Testis Pool   3.6           Prostate ca.* (bone met) PC-3   22.1           Prostate Pool   7.2           Placenta   10.2           Uterus Pool   0.0           Ovarian ca. OVCAR-3   75.3           Ovarian ca. SK-OV-3   34.2           Ovarian ca. OVCAR-4   13.9           Ovarian ca. OVCAR-5   100.0           Ovarian ca. IGROV-1   32.3           Ovarian ca. OVCAR-8   3.1           Ovary   10.7           Breast ca. MCF-7   48.6           Breast ca. MDA-MB-231   17.4           Breast ca. BT 549   40.6           Breast ca. T47D   26.4           Breast ca. MDA-N   18.9           Breast Pool   7.2           Trachea   13.8           Lung   2.1           Fetal Lung   17.0           Lung ca. NCI-N417   1.3           Lung ca. LX-1   10.7           Lung ca. NCI-H146   0.0           Lung ca. SHP-77   2.0           Lung ca. A549   9.5           Lung ca. NCI-H526   3.7           Lung ca. NCI-H23   15.4           Lung ca. NCI-H460   31.9           Lung ca. HOP-62   10.0           Lung ca. NCI-H522   25.0           Liver   0.8           Fetal Liver   0.0           Liver ca. HepG2   10.1           Kidney Pool   7.0           Fetal Kidney   6.6           Renal ca. 786-0   37.9           Renal ca. A498   9.8           Renal ca. ACHN   18.8           Renal ca. UO-31   16.6           Renal ca. TK-10   46.0           Bladder   12.9           Gastric ca. (liver met.) NCI-N87   32.1           Gastric ca. KATO III   79.0           Colon ca. SW-948   10.5           Colon ca. SW480   65.1           Colon ca.* (SW480 met) SW620   0.0           Colon ca. HT29   31.0           Colonca. HCT-116   30.6           Colon ca. CaCo-2   21.8           Colon cancer tissue   26.2           Colon ca. SW1116   14.7           Colon ca. Colo-205   10.4           Colon ca. SW-48   43.5           Colon Pool   4.7           Small Intestine Pool   5.9           Stomach Pool   5.1           Bone Marrow Pool   2.7           Fetal Heart   7.7           Heart Pool   2.5           Lymph Node Pool   7.4           Fetal Skeletal Muscle   1.5           Skeletal Muscle Pool   0.0           Spleen Pool   3.8           Thymus Pool   9.8           CNS cancer (glio/astro) U87-MG   4.1           CNS cancer (glio/astro) U-118-MG   13.7           CNS cancer (neuro; met) SK-N-AS   33.2           CNS cancer (astro) SF-539   13.3           CNS cancer (astro) SNB-75   37.6           CNS cancer (glio) SNB-19   36.3           CNS cancer (glio) SF-295   40.1           Brain (Amygdala) Pool   1.0           Brain (cerebellum)   2.0           Brain (fetal)   1.9           Brain (Hippocampus) Pool   0.0           Cerebral Cortex Pool   0.0           Brain (Substantia nigra) Pool   0.0           Brain (Thalamus) Pool   0.0           Brain (whole)   4.6           Spinal Cord Pool   2.6           Adrenal Gland   8.7           Pituitary gland Pool   0.0           Salivary Gland   12.7           Thyroid (female)   4.0           Pancreatic ca. CAPAN2   34.4           Pancreas Pool   10.4                        
     [0778] CNS_neurodegeneration_v1.0 Summary: Ag6833 Expression of the CG128249-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0779] General_screening_panel_v1.6 Summary: Ag6833 Highest expression of the CG128249-02 gene is detected in ovarian OVCAR-5 cell line (CT=32.8). Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Interestingly, this gene is expressed at low/undectactable levels in normal tissues (CTs&gt;35). Thus, expression of this gene could be used to distinguish cancer cell lines from the normal tissue samples in this panel and also as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.  
     [0780] Panel 4.1 D Summary: Ag6833 Expression of the CG128249-02 (gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0781] M. NOV13a (CGt28785-01): alt Spliced SPUF  
     [0782] Expression of gene CG128785-01 was assessed using the primer-probe set Ag5883, described in Table MA.  
                   TABLE MA                          Probe Name Ag5883                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gcttttcaccgaggaggag-3′   19   135   259                   Probe   TET-5′-agcttctcccctgctttctaggaaga-3′-   26   176   260           TAMRA               Reverse   5′-ttcactgccaagtagatggg-3′   20   206   261                  
 
     [0783] General_screening_panel_v1.5 Summary: Ag5883 Expression of the CG128785-01 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0784] Panel 4.1D Summary: Ag5883 Expression of the CG128785-01 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0785] N. NOV14a (CG129005-01): 54TM Splice Variant.  
     [0786] Expression of gene CG129005-01 was assessed using the primer-probe set Ag4799, described in Table NA. Results of the RTQ-PCR runs are shown in Tables NB and NC.  
                   TABLE NA                          Probe Name Ag4799                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-tgcagtacagtcgtgatgct-3′   20   373   262                   Probe   TET-5′-aagacctcaacqcccctgacctctat-3′-   26   409   263           TAMRA               Reverse   5′-ccaggagcacgtaagtaatgaa-3′   22   450   264                  
 
     [0787]               TABLE NB                          General_screening_panel_v1.4                                 Rel. Exp. (%)               Ag4799, Run           Tissue Name   223203328                                         Adipose   0.6           Melanoma* Hs688(A).T   21.0           Melanoma* Hs688(B).T   21.8           Melanoma* M14   18.6           Melanoma* LOXIMVI   18.8           Melanoma* SK-MEL-5   15.8           Squamous cell carcinoma SCC-4   12.2           Testis Pool   1.6           Prostate ca.* (bone met) PC-3   39.8           Prostate Pool   1.5           Placenta   4.8           Uterus Pool   1.2           Ovarian ca. OVCAR-3   11.4           Ovarian ca. SK-OV-3   19.8           Ovarian ca. OVCAR-4   18.2           Ovarian ca. OVCAR-5   41.5           Ovarian ca. IGROV-1   21.8           Ovarian ca. OVCAR-8   14.2           Ovary   2.3           Breast ca. MCF-7   17.7           Breast ca. MDA-MB-231   21.3           Breast ca. BT 549   20.4           Breast ca. T47D   100.0           Breast ca. MDA-N   9.9           Breast Pool   2.7           Trachea   3.1           Lung   0.7           Fetal Lung   3.1           Lung ca. NCI-N417   16.4           Lung ca. LX-1   8.7           Lung ca. NCI-H146   3.5           Lung ca. SHP-77   14.3           Lung ca. A549   15.9           Lung ca. NCI-H526   9.6           Lung ca. NCI-H23   8.8           Lung ca. NCI-H460   8.2           Lung ca. HOP-62   9.5           Lung ca. NCI-H522   11.4           Liver   3.0           Fetal Liver   8.4           Liver ca. HepG2   10.9           Kidney Pool   3.4           Fetal Kidney   1.3           Renal ca. 786-0   14.6           Renal ca. A498   4.9           Renal ca. ACHN   8.2           Renal ca. UO-31   15.5           Renal ca TK-10   11.8           Bladder   4.6           Gastric ca. (liver met.) NCI-N87   22.7           Gastric ca. KATO III   38.2           Colon ca. SW-948   12.6           Colon ca. SW480   28.1           Colon ca.* (SW480 met) SW620   12.9           Colon ca. HT29   14.7           Colon ca. HCT-116   9.9           Colon ca. CaCo-2   21.5           Colon cancer tissue   7.6           Colon ca. SW1116   4.0           Colon ca. Colo-205   7.4           Colon ca. SW-48   9.7           Colon Pool   3.4           Small Intestine Pool   1.5           Stomach Pool   1.2           Bone Marrow Pool   1.3           Fetal Heart   1.4           Heart Pool   1.4           Lymph Node Pool   3.5           Fetal Skeletal Muscle   1.0           Skeletal Muscle Pool   4.4           Spleen Pool   1.3           Thymus Pool   1.9           CNS cancer (glio/astro) U87-MG   36.3           CNS cancer (glio/astro) U-118-MG   31.9           CNS cancer (neuro; met) SK-N-AS   7.6           CNS cancer (astro) SF-539   15.9           CNS cancer (astro) SNB-75   41.5           CNS cancer (glio) SNB-19   18.0           CNS cancer (glio) SF-295   22.4           Brain (Amygdala) Pool   2.5           Brain (cerebellum)   4.7           Brain (fetal)   1.4           Brain (Hippocampus) Pool   1.9           Cerebral Cortex Pool   1.4           Brain (Substantia nigra) Pool   3.0           Brain (Thalamus) Pool   1.9           Brain (whole)   2.6           Spinal Cord Pool   2.7           Adrenal Gland   4.0           Pituitary gland Pool   1.5           Salivary Gland   2.6           Thyroid (female)   4.4           Pancreatic ca. CAPAN2   15.4           Pancreas Pool   4.2                        
     [0788]               TABLE NC                          Panel 4.1D                                 Rel. Exp. (%)               Ag4799, Run           Tissue Name   223235948                                         Secondary Th1 act   23.0           Secondary Th2 act   25.7           Secondary Tr1 act   24.0           Secondary Th1 rest   4.3           Secondary Th2 rest   6.0           Secondary Tr1 rest   3.2           Primary Th1 act   15.2           Primary Th2 act   23.2           Primary Tr1 act   24.5           Primary Th1 rest   4.0           Primary Th2 rest   1.7           Primary Tr1 rest   6.9           CD45RA CD4 lymphocyte act   37.4           CD45RO CD4 lymphocyte act   26.4           CD8 lymphocyte act   22.5           Secondary CD8 lymphocyte rest   14.1           Secondary CD8 lymphocyte act   12.9           CD4 lymphocyte none   1.5           2ry Th1/Th2/Tr1_anti-CD95 CH11   5.2           LAK cells rest   10.7           LAK cells IL-2   11.4           LAK cells IL-2 + IL-12   8.2           LAK cells IL-2 + IFN gamma   7.9           LAK cells IL-2 + IL-18   16.5           LAK cells PMA/ionomycin   10.1           NK Cells IL-2 rest   13.5           Two Way MLR 3 day   8.7           Two Way MLR 5 day   12.1           Two Way MLR 7 day   7.3           PBMC rest   2.5           PBMC PWM   20.7           PBMC PHA-L   16.7           Ramos (B cell) none   35.1           Ramos (B cell) ionomycin   55.9           B lymphocytes PWM   12.7           B lymphocytes CD40L and IL-4   9.9           EOL-1 dbcAMP   17.1           EOL-1 dbcAMP PMA/ionomycin   6.9           Dendritic cells none   14.8           Dendritic cells LPS   7.1           Dendritic cells anti-CD40   14.6           Monocytes rest   5.7           Monocytes LPS   12.4           Macrophages rest   17.3           Macrophagcs LPS   5.6           HUVEC none   23.7           HUVEC starved   39.8           HUVEC IL-1beta   42.0           HUVEC IFN gamma   25.7           HUVEC TNF alpha + IFN gamma   44.8           HUVEC TNF alpha + IL4   46.3           HUVEC IL-11   12.8           Lung Microvascular EC none   100.0           Lung Microvascular EC TNFalpha + IL-   69.3           1beta           Microvascular Dermal EC none   24.0           Microsvasular Dermal EC TNFalpha + IL-   34.9           1beta           Bronchial epithelium TNFalpha + IL1beta   26.1           Small airway epithelium none   17.0           Small airway epithelium TNFalpha + IL-   31.6           1beta           Coronery artery SMC rest   39.0           Coronery artery SMC TNFalpha + IL-1beta   48.0           Astrocytes rest   15.4           Astrocytes TNFalpha + IL-1beta   16.7           KU-812 (Basophil) rest   25.2           KU-812 (Basophil) PMA/ionomycin   45.7           CCD1106 (Keratinocytes) none   44.4           CCD1106 (Keratinocytes) TNFalpha + IL-   24.0           1beta           Liver cirrhosis   2.3           NCI-H292 none   20.4           NCI-H292 IL-4   38.2           NCI-H292 IL-9   40.6           NCI-H292 IL-13   39.0           NCI-H292 IFN gamma   44.8           HPAEC none   13.4           HPAEC TNF alpha + IL-1 beta   54.7           Lung fibroblast none   30.6           Lung fibroblast TNF alpha + IL-1 beta   33.0           Lung fibroblast IL-4   33.4           Lung fibroblast IL-9   45.4           Lung fibroblast IL-13   37.1           Lung fibroblast IFN gamma   41.8           Dermal fibroblast CCD1070 rest   55.9           Dermal fibroblast CCD1070 TNF alpha   40.9           Dermal fibroblast CCD1070 IL-1 beta   35.8           Dermal fibroblast IFN gamma   20.9           Dermal fibroblast IL-4   26.6           Dermal Fibroblasts rest   38.7           Neutrophils TNFa + LPS   0.3           Neutrophils rest   0.9           Colon   7.6           Lung   12.2           Thymus   3.0           Kidney   17.3                        
     [0789] General_screening_panel_v1.4 Summary: Ag4799 Highest expression of the CG129005-01 gene is detected in breast cancer T47D cell line (CT=23.9). High levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.  
     [0790] Among tissues with metabolic or endocrine function, this gene is expressed at high to moderate levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0791] In addition, this gene is expressed at high levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0792] Panel 4.1D Summary: Ag4799 Highest expression of the CG129005-01 gene is detected in lung microvascular EC cells (CT=27.3). This gene is expressed at high to moderate levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This pattern is in agreement with the expression profile in General_screening_panel v1.4 and also suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.  
     [0793] O. NOV15a (CG132086-01): Novel Membrane Protein  
     [0794] Expression of gene CG132086-01 was assessed using the primer-probe set Ag4809, described in Table OA. Results of the RTQ-PCR runs are shown in Table OB.  
                   TABLE GA                          Probe Name Ag4809                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gatgccacagaggagttcatt-3′   21   6986   265                   Probe   TET-5′-tccctqgactctactacagatgaagaaga-3′-   29   7010   266               Reverse   5′-ccatcacaccagccatttta-3′   20   7057   267                  
 
     [0795]               TABLE OB                          Panel 4.1D                                 Rel. Exp. (%)               Ag4809, Run           Tissue Name   223273407                                         Secondary Th1 act   49.7           Secondary Th2 act   55.5           Secondary Tr1 act   36.3           Secondary Th1 rest   12.0           Secondary Th2 rest   24.7           Secondary Tr1 rest   14.1           Primary Th1 act   20.6           Primary Th2 act   32.1           Primary Tr1 act   34.2           Primary Th1 rest   9.8           Primary Th2 rest   8.0           Primary Tr1 rest   18.2           CD45RA CD4 lymphocyte act   50.7           CD45RO CD4 lymphocyte act   48.3           CD8 lymphocyte act   38.4           Secondary CD8 lymphocyte rest   35.4           Secondary CD8 lymphocyte act   16.0           CD4 lymphocyte none   9.9           2ry Th1/Th2/Tr1_anti-CD95 CH11   27.2           LAK cells rest   24.8           LAK cells IL-2   25.9           LAK cells IL-2 + IL-12   14.7           LAK cells IL-2 + IFN gamma   16.6           LAK cells IL-2 + IL-18   23.2           LAK cells PMA/ionomycin   33.9           NK Cells IL-2 rest   30.1           Two Way MLR 3 day   29.3           Two Way MLR 5 day   32.1           Two Way MLR 7 day   18.7           PBMC rest   8.5           PBMC PWM   31.6           PBMC PHA-L   33.0           Ramos (B cell) none   29.1           Ramos (B cell) ionomycin   36.9           B lymphocytes PWM   41.8           B lymphocytes CD40L and IL-4   37.6           EOL-1 dbcAMP   21.0           EOL-1 dbcAMP PMA/ionomycin   27.7           Dendritic cells none   29.3           Dendritic cells LPS   24.5           Dendritic cells anti-CD40   21.2           Monocytes rest   15.4           Monocytes LPS   100.0           Macrophages rest   22.7           Macrophages LPS   21.9           HUVEC none   17.3           HUVEC starved   30.8           HUVEC IL-1beta   27.2           HUVEC IFN gamma   34.6           HUVEC TNF alpha + IFN gamma   24.8           HUVEC TNF alpha + IL4   26.4           HUVEC IL-11   19.9           Lung Microvascular EC none   36.6           Lung Microvascular EC TNFalpha + IL-   29.9           1beta           Microvascular Dermal EC none   26.6           Microsvasular Dermal EC TNFalpha + IL-   24.8           1beta           Bronchial epithelium TNFalpha +   31.2           IL1beta           Small airway epithelium none   16.8           Small airway epithelium TNFalpha + IL-   27.0           1beta           Coronery artery SMC rest   17.7           Coronery artery SMC TNFalpha + IL-   26.2           1beta           Astrocytes rest   13.4           Astrocytes TNFalpha + IL-1beta   13.3           KU-812 (Basophil) rest   59.0           KU-812 (Basophil) PMA/ionomycin   97.9           CCD1106 (Keratinocytes) none   25.3           CCD1106 (Keratinocytes) TNFalpha + IL-   29.3           1beta           Live cirrhosis   6.7           NCI-H292 none   12.5           NCI-H292 IL-4   20.6           NCI-H292 IL-9   22.1           NCI-H292 IL-13   22.1           NCI-H292 IFN gamma   12.7           HPAEC none   15.5           HPAEC TNF alpha + IL-1 beta   51.4           Lung fibroblast none   37.9           Lung fibroblast TNF alpha + IL-1 beta   36.9           Lung fibroblast IL-4   14.7           Lung fibroblast IL-9   15.8           Lung fibroblast IL-13   18.6           Lung fibroblast IFN gamma   25.3           Dermal fibroblast CCD1070 rest   51.4           Dermal fibroblast CCD1070 TNF alpha   84.1           Dermal fibroblast CCD1070 IL-1 beta   52.1           Dermal fibroblast IFN gamma   15.0           Dermal fibroblast IL-4   33.2           Dermal Fibroblasts rest   17.7           Neutrophils TNFa + LPS   11.7           Neutrophils rest   12.5           Colon   6.8           Lung   11.6           Thymus   32.8           Kidney   9.8                        
     [0796] General_screening_panel_v1.4 Summary: Ag4809 Results from one experiment with the CG132086-01 gene are not included. The amp plot indicates that there were experimental difficulties with this run.  
     [0797] Panel 4.1D Summary: Ag4809 Highest expression of the CG132086-01 gene is detected in LPS treated monocytes and PMA/ionomycin treated basophils (CTs=29.5). This gene is expressed at high to moderate levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This expression pattern suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.  
     [0798] P. NOV16a and NOV16b (CG132297-01 and CG132297-02): Elastin  
     [0799] Expression of gene CG132297-01 and CG132297-02 was assessed using the primer-probe set Ag7016, described in Table PA. Results of the RTQ-PCR runs are shown in Tables PB, PC and PD. Please note that CG132297-01 represents a full-length physical clone.  
                   TABLE PA                          Probe Name Ag7016                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gctgccactccgtatttagct-3′   21   101   268                   Probe   TET-5′-agctggaggtatacctccaaggcccc-3′-   26   136   269           TAMRA               Reverse   5′-ggagggcttggagttcc-3′   17   170   270                  
 
     [0800]               TABLE PB                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%)               Ag7016, Run           Tissue Name   282263005                                         AD 1 Hippo   29.3           AD 2 Hippo   50.3           AD 3 Hippo   13.8           AD 4 Hippo   39.8           AD 5 Hippo   43.2           AD 6 Hippo   77.9           Control 2 Hippo   42.9           Control 4 Hippo   55.9           Control (Path) 3 Hippo   19.8           AD 1 Temporal Ctx   30.1           AD 2 Temporal Ctx   55.1           AD 3 Temporal Ctx   7.2           AD 4 Temporal Ctx   55.1           AD 5 Inf Temporal Ctx   57.8           AD 5 Sup Temporal Ctx   68.8           AD 6 Inf Temporal Ctx   68.3           AD 6 Sup Temporal Ctx   100.0           Control 1 Temporal Ctx   14.7           Control 2 Temporal Ctx   34.2           Control 3 Temporal Ctx   11.6           Control 3 Temporal Ctx   45.7           Control (Path) 1 Temporal Ctx   71.2           Control (Path) 2 Temporal Ctx   31.2           Control (Path) 3 Temporal Ctx   24.5           Control (Path) 4 Temporal Ctx   24.1           AD 1 Occipital Ctx   31.4           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   9.2           AD 4 Occipital Ctx   59.5           AD 5 Occipital Ctx   77.9           AD 6 Occipital Ctx   81.2           Control 1 Occipital Ctx   14.7           Control 2 Occipital Ctx   26.8           Control 3 Occipital Ctx   21.3           Control 4 Occipital Ctx   66.4           Control (Path) 1 Occipital Ctx   36.3           Control (Path) 2 Occipital Ctx   22.7           Control (Path) 3 Occipital Ctx   18.6           Control (Path) 4 Occipital Ctx   29.3           Control 1 Parietal Ctx   30.1           Control 2 Parietal Ctx   67.4           Control 3 Parietal Ctx   20.3           Control (Path) 1 Parietal Ctx   35.6           Control (Path) 2 Parietal Ctx   47.6           Control (Path) 3 Parietal Ctx   27.2           Control (Path) 4 Parietal Ctx   58.6                        
     [0801]               TABLE PC                          General_screening_panel_v1.6                                 Rel. Exp. (%)               Ag7016, Run           Tissue Name   282263474                                         Adipose   9.9           Melanoma* Hs688(A).T   42.0           Melanoma* Hs688(B).T   21.8           Melanoma* M14   0.0           Melanoma* LOXIMVI   0.0           Melanoma* SK-MEL-5   0.0           Squamous cell carcinoma SCC-4   0.0           Testis Pool   5.3           Prostate ca.* (bone met) PC-3   0.0           Prostate Pool   4.4           Placenta   6.9           Uterus Pool   2.7           Ovarian ca. OVCAR-3   0.0           Ovarian ca. SK-OV-3   0.0           Ovarian ca. OVCAR-4   0.0           Ovarian ca. OVCAR-5   0.1           Ovarian ca. IGROV-1   0.0           Ovarian ca. OVCAR-8   0.1           Ovary   3.8           Breast ca. MCF-7   0.0           Breast ca. MDA-MB-231   0.0           Breast ca. BT 549   0.0           Breast ca. T47D   0.0           Breast ca. MDA-N   0.0           Breast Pool   4.6           Trachea   7.0           Lung   1.3           Fetal Lung   100.0           Lung ca. NCI-N417   27.9           Lung ca. LX-1   0.1           Lung ca. NCI-H146   0.2           Lung ca. SHP-77   1.3           Lung ca. A549   0.1           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   0.0           Lung ca. NCI-H460   0.0           Lung ca. HOP-62   0.0           Lung ca. NCI-H522   0.0           Liver   0.2           Fetal Liver   2.9           Liver ca. HepG2   0.1           Kidney Pool   10.2           Fetal Kidney   5.3           Renal ca. 786-0   0.0           Renal ca. A498   0.0           Renal ca. ACHN   0.0           Renal ca. UO-31   0.0           Renal ca. TK-10   0.1           Bladder   6.0           Gastric ca. (liver met.) NCI-N87   0.1           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.0           Colon ca. SW480   0.0           Colon ca.* (SW480 met) SW620   0.0           Colon ca. HT29   0.1           Colon ca. HCT-116   0.0           Colon ca. CaCo-2   0.0           Colon cancer tissue   7.6           Colon ca. SW1116   0.0           Colon ca. Colo-205   0.2           Colon ca. SW-48   0.2           Colon Pool   7.6           Small Intestine Pool   6.7           Stomach Pool   3.7           Bone Marrow Pool   6.2           Fetal heart   21.0           Heart Pool   3.3           Lymph Node Pool   8.5           Fetal Skeletal Muscle   10.6           Skeletal Muscle Pool   1.1           Spleen Pool   3.2           Thymus Pool   3.0           CNS cancer (glio/astro) U87-MG   0.0           CNS cancer (glio/astro) U-118-MG   6.9           CNS cancer (neuro; met) SK-N-AS   0.8           CNS cancer (astro) SF-539   0.0           CNS cancer (astro) SNB-75   0.1           CNS cancer (glio) SNB-19   0.0           CNS cancer (glio) SF-295   0.0           Brain (Amygdala) Pool   0.4           Brain (cerebellum)   5.1           Brain (fetal)   2.6           Brain (Hippocampus) Pool   1.3           Cerebral Cortex Pool   0.7           Brain (Substantia nigra) Pool   0.6           Brain (Thalamus) Pool   0.6           Brain (whole)   1.2           Spinal Cord Pool   2.5           Adrenal Gland   1.9           Pituitary gland Pool   0.7           Salivary Gland   1.4           Thyroid (female)   0.6           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   1.7                        
     [0802]               TABLE PD                          Panel 4.1D                                 Rel. Exp. (%)               Ag7016, Run           Tissue Name   282263182                                         Secondary Th1 act   0.0           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.0           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.0           Primary Th1 rest   0.0           Primary Th2 rest   0.0           Primary Tr1 rest   0.0           CD45RA CD4 lymphocyte act   15.6           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.0           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   0.0           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0           LAK cells rest   0.0           LAK cells IL-2   0.0           LAK cells IL-2 + IL-12   0.0           LAK cells IL-2 + IFN gamma   0.0           LAK cells IL-2 + IL-18   0.0           LAK cells PMA/ionomycin   0.0           NK Cells IL-2 rest   0.0           Two Way MLR 3 day   0.0           Two Way MLR 5 day   0.0           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   0.0           PBMC PHA-L   0.0           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   0.2           EOL-1 dbcAMP   0.0           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   0.0           Dendritic cells LPS   0.0           Dendritic cells anti-CD40   0.0           Monocytes rest   0.0           Monocytes LPS   0.0           Macrophages rest   0.0           Macrophages LPS   0.0           HUVEC none   0.0           HUVEC starved   0.1           HUVEC IL-1beta   0.0           HUVEC IFN gamma   0.0           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.0           Lung Microvascular EC none   0.5           Lung Microvascular EC TNFalpha + IL-   0.0           1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   0.0           IL1beta           Small airway epithelium none   0.2           Small airway epithelium TNFalpha +   0.0           IL-1beta           Coronery artery SMC rest   0.4           Coronery artery SMC TNFalpha + IL-   0.1           1beta           Astrocytes rest   7.9           Astrocytes TNFalpha + IL-1beta   27.4           KU-812 (Basophil) rest   0.0           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   0.0           CCD1106 (Keratinocytes) TNFalpha +   0.0           IL-1beta           Liver cirrhosis   2.4           NCI-H292 none   0.0           NCI-H292 IL-4   0.0           NCI-H292 IL-9   0.0           NCI-H292 IL-13   0.0           NCI-H292 IFN gamma   0.0           HPAEC none   0.1           HPAEC TNF alpha + IL-1beta   0.1           Lung fibroblast none   4.5           Lung fibroblast TNF alpha + IL-1 beta   22.2           Lung fibroblast IL-4   6.0           Lung fibroblast IL-9   6.8           Lung fibroblast IL-13   7.9           Lung fibroblast IFN gamma   7.9           Dermal fibroblast CCD1070 rest   47.0           Dermal fibroblast CCD1070 TNF alpha   46.0           Dermal fibroblast CCD1070 IL-1 beta   100.0           Dermal fibroblast IFN gamma   0.6           Dermal fibroblast IL-4   1.6           Dermal Fibroblasts rest   1.1           Neutrophils TNFa + LPS   0.0           Neutrophils rest   0.0           Colon   0.7           Lung   6.4           Thymus   0.2           Kidney   0.5                        
     [0803] CNS_neurodegeneration_v1.0 Summary: Ag7016 This panel confirms the expression of the CG 132297-01 gene at low levels in the brains of an independent group of individuals. However, no differential expression of this gene was detected between Alzheimer&#39;s diseased postmortem brains and those of non-demented controls in this experiment. Please see Panel 1.6 for a discussion of the potential utility of this gene in treatment of central nervous system disorders.  
     [0804] General_screening_panel_v1.6 Summary: Ag7016 Highest expression of the CG132297-01 gene of this gene is detected in fetal lung (CT=26.3). Interestingly, this gene is expressed at much higher levels in fetal (CTs=26-31) when compared to adult lung and liver (CT=32-35). This observation suggests that expression of this gene can be used to distinguish fetal from adult lung and liver, respectively. In addition, the relative overexpression of this gene in fetal tissues suggests that the elastin encoded by this gene may enhance growth or development of lung and liver in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the elastin encoded by this gene could be useful in treatment of lung and liver related diseases.  
     [0805] Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0806] In addition, this gene is expressed at moderate levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0807] Moderate levels of expression of this gene is also seen in colon cancer and in number of cancer cell lines derived from melanoma, brain, and lung cancer cell lines. Therefore, therapeutic modulation of the elastin encoded by this gene may be useful in the treatment of melanoma, colon, brain and lung cancer.  
     [0808] Panel 4.1D Summary: Ag7016 Highest expression of the CG132297-01 gene of this gene is detected in IL-1 beta treated dermal fibroblasts CCD1070 (CT=28.1). In addition, moderate to low levels of expression of this gene is also seen in dermal and lung fibroblasts, activated CD45RA CD4 lymphocyte and lung. CD45RA CD4 lymphocytes represent activated naive T cells. In activated memory cells (CD45RO CD4 lymphocyte) or CD4 Th1 or Th2 cells, resting CD4 cells (CTs=40), the expression of this gene is strongly down regulated suggesting a role for this putative protein in differentiation or activation of naive T cells. Therefore, modulation of the expression and/or activity of this putative protein encoded by this gene might be beneficial for the control of autoimmune diseases and T cell mediated diseases such as COPD, emphysema, atopic asthma, asthma, arthritis, psoriasis, IBD and allergy.  
     [0809] Q. NOV17a (CG132343-01): Novel Transmembrane Protein.  
     [0810] Expression of gene CGI132343-01 was assessed using the primer-probe set Ag4819, described in Table QA. Results of the RTQ-PCR runs are shown in Tables QB and QC.  
                   TABLE PA                          Probe Name Ag4819                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gagttacccatacaccggctat-3′   22   88   271                   Probe   TET-5′-atttcacggccaggagagtcctcttt-3′-   26   110   272           TAMRA               Reverse   5′-taaqgatgatgcccatacaaag-3′   22   163   273                  
 
     [0811]               TABLE QB                          General_screening_panel_v1.5                                 Rel. Exp. (%)               Ag4819, Run           Tissue Name   228783855                                         Adipose   0.2           Melanoma* Hs688(A).T   0.8           Melanoma* Hs688(B).T   1.0           Melanoma* M14   1.3           Melanoma* LOXIMVI   0.0           Melanoma* SK-MEL-5   0.1           Squamous cell carcinoma SCC-4   0.1           Testis Pool   12.8           Prostate ca.* (bone met) PC-3   0.3           Prostate Pool   0.0           Placenta   0.0           Uterus Pool   0.2           Ovarian ca. OVCAR-3   1.0           Ovarian ca. SK-OV-3   2.3           Ovarian ca. OVCAR-4   0.4           Ovarian ca. OVCAR-5   0.7           Ovarian ca. IGROV-1   0.0           Ovarian ca. OVCAR-8   0.0           Ovary   0.6           Breast ca. MCF-7   0.6           Breast ca. MDA-MB-231   2.0           Breast ca. BT 549   1.0           Breast ca. T47D   100.0           Breast ca. MDA-N   1.1           Breast Pool   0.0           Trachea   0.0           Lung   0.7           Fetal Lung   0.7           Lung ca. NCI-N417   0.3           Lung ca. LX-I   2.4           Lung ca. NCI-H146   0.3           Lung ca. SHP-77   1.0           Lung ca. A549   0.9           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   2.1           Lung ca. NCI-H460   2.9           Lung ca. HOP-62   0.6           Lung ca. NCI-H522   1.2           Liver   0.2           Fetal Liver   0.7           Liver ca. HepG2   1.2           Kidney Pool   2.1           Fetal Kidney   0.6           Renal ca. 786-0   0.4           Renal ca. A498   0.9           Renal ca. ACHN   0.0           Renal ca. UO-31   0.5           Renal ca. TK-10   2.5           Bladder   0.5           Gastric ca. (liver met.) NCI-N87   2.9           Gastric ca. KATO III   0.6           Colon ca. SW-948   0.0           Colon ca. SW480   1.1           Colon ca.* (SW480 met) SW620   2.1           Colon ca. HT29   0.2           Colon ca. HCT-116   2.3           Colon ca. CaCo-2   4.4           Colon cancer tissue   0.9           Colon ca. SW1116   1.5           Colon ca. Colo-205   0.0           Colon ca. SW-48   0.0           Colon Pool   0.9           Small Intestine Pool   0.2           Stomach Pool   0.5           Bone Marrow Pool   0.0           Fetal Heart   0.5           Heart Pool   0.5           Lymph Node Pool   0.6           Fetal Skeletal Muscle   0.5           Skeletal Muscle Pool   0.1           Spleen Pool   0.5           Thymus Pool   0.7           CNS cancer (glio/astro) U87-MG   1.1           CNS cancer (glio/astro) U-118-MG   3.9           CNS cancer (neuro; met) SK-N-AS   2.5           CNS cancer (astro) SF-539   1.0           CNS cancer (astro) SNB-75   5.0           CNS cancer (glio) SNB-19   0.3           CNS cancer (glio) SF-295   4.7           Brain (Amygdala) Pool   0.0           Brain (cerebellum)   2.4           Brain (fetal)   0.5           Brain (Hippocampus) Pool   0.0           Cerebral Cortex Pool   0.2           Brain (Substantia nigra) Pool   0.0           Brain (Thalamus) Pool   1.6           Brain (whole)   0.2           Spinal Cord Pool   0.3           Adrenal Gland   0.3           Pituitary gland Pool   0.3           Salivary Gland   0.0           Thyroid (female)   0.0           Pancreatic ca. CAPAN2   0.6           Pancreas Pool   0.8                        
     [0812]               TABLE QC                          Panel 4.1D                                 Rel. Exp. (%)               Ag4819, Run           Tissue Name   223302997                                         Secondary Th1 act   57.4           Secondary Th2 act   25.7           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.0           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   26.1           Primary Th1 rest   7.6           Primary Th2 rest   0.0           Primary Tr1 rest   0.0           CD45RA CD4 lymphocyte act   28.7           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   70.7           Secondary CD8 lymphocyte rest   64.6           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   19.5           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0           LAK cells rest   14.5           LAK cells IL-2   45.1           LAK cells IL-2 + IL-12   22.1           LAK cells IL-2 + IFN gamma   40.1           LAK cells IL-2 + IL-18   0.0           LAK cells PMA/ionomycin   20.3           NK Cells IL-2 rest   50.7           Two Way MLR 3 day   0.0           Two Way MLR 5 day   32.1           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   44.1           PBMC PHA-L   0.0           Ramos (B cell) none   15.5           Ramos (B cell) ionomycin   50.7           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   8.8           EOL-1 dbcAMP   46.7           EOL-1 dbcAMP PMA/ionomycin   27.2           Dendritic cells none   38.7           Dendritic cells LPS   34.2           Dendritic cells anti-CD40   15.2           Monocytes rest   18.9           Monocytes LPS   8.8           Macrophages rest   29.5           Macrophages LPS   0.0           HUVEC none   0.0           HUVEC starved   0.0           HUVEC IL-1beta   33.7           HUVEC IFN gamma   55.9           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   13.4           HUVEC IL-11   0.0           Lung Microvascular EC none   51.4           Lung Microvascular EC TNFalpha + IL-   0.0           1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   15.4           IL1beta           Small airway epithelium none   15.2           Small airway epithelium TNFalpha +   61.6           IL-1beta           Coronery artery SMC rest   0.0           Coronery artery SMC TNFalpha + IL-   0.0           1beta           Astrocytes rest   51.1           Astrocytes TNFalpha + IL-1beta   14.4           KU-812 (Basophil) rest   25.3           KU-812 (Basophil) PMA/ionomycin   51.1           CCD1106 (Keratinocytes) none   18.2           CCD1106 (Keratinocytes) TNFalpha +   55.1           IL-1beta           Liver cirrhosis   0.0           NCI-H292 none   17.7           NCI-H292 IL-4   16.6           NCI-H292 IL-9   14.6           NCI-H292 IL-13   31.0           NCI-H292 IFN gamma   30.4           HPAEC none   0.0           HPAEC TNF alpha + IL-1 beta   12.1           Lung fibroblast none   23.2           Lung fibroblast TNF alpha + IL-1 beta   0.0           Lung fibroblast IL-4   42.0           Lung fibroblast IL-9   47.3           Lung fibroblast IL-13   30.8           Lung fibroblast IFN gamma   36.3           Dermal fibroblast CCD1070 rest   27.7           Dermal fibroblast CCD1070 TNF alpha   28.1           Dermal fibroblast CCD1070 IL-1 beta   10.2           Dermal fibroblast IFN gamma   15.7           Dermal fibroblast IL-4   34.2           Dermal Fibroblasts rest   22.5           Neutrophils TNFa + LPS   0.0           Neutrophils rest   0.0           Colon   0.0           Lung   0.0           Thymus   0.0           Kidney   100.0                        
     [0813] General_screening_panel_v1.5 Summary: Ag4819 Expression of this gene is restricted to a few samples in this panel, with highest expression in a breast cancer cell line (CT=29). Low, but significant levels of expression are seen in cell lines derived from brain, renal and gastric cancers, as well as in normal testis. Thus, the expression of this gene could be used to distinguish the breast cancer cell line sample from other samples on this panel, and as a marker of breast cancer. In addition, therapeutic modulation of this gene or its protein product may be useful in the treatment of breast, gastric, renal and brain cancers.  
     [0814] Panel 4.1D Summary: Ag4819 This gene is only expressed at detectable levels in the kidney (CT=34.5). Thus, expression of this gene could be used to differentiate the kidney derived sample from other samples on this panel and as a marker of kidney tissue. In addition, therapeutic targeting of the expression or function of this gene may modulate kidney function and be important in the treatment of inflammatory or autoimmune diseases that affect the kidney, including lupus and glomerulonephritis.  
     [0815] R. NOV18a (CG132423-01): Pregnancy-specific Beta-1-glycoprotein 2 Precursor.  
     [0816] Expression of gene CG132423-01 was assessed using the primer-probe set Ag7021, described in Table RA.  
                   TABLE RA                          Probe Name Ag7021                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-aggtccctgatttggacaag-3′   20   848   274                   Probe   TET-5′-aagaacatccttcccctcggacactt-3′-   26   871   275           TAMRA               Reverse   5′-ctgcccaagtcatgattgaa-3′   20   910   276                  
 
     [0817] CNS_neurodegeneration_v1.0 Summary: Ag7021 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0818] General_screening_panel_v1.6 Summary: Ag7021 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0819] Panel 4.1D Summary: Ag7021 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0820] S. Nov19a and NOV19b (CG132541-01 and CG132541-02): Protocadherin 16 Precursor.  
     [0821] Expression of gene CG132541 -01 and CG132541-02 was assessed using the primer-probe sets Ag1076, Ag1311, Ag482, and Ag6709 described in Tables SA, SB, SC, and SD. Results of the RTQ-PCR runs are shown in Tables SE, SF, SG, SH, SI, SJ, SK and SL. Please note that probe and primer set Ag6709 is specific for CG132541-01 and probe Ag482 is specific for CG132541-02.  
                   TABLE SA                          Probe Name Ag1076                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-tgacagacactgtggtgcttag-3′   22   6228   277                   Probe   TET-5′-accatccactgcactcacagaaaagg-3′-   26   6187   278           TAMRA               Reverse   5′-agagaacagtgtcccagctaca-3′   22   6165   279                  
 
     [0822]                   TABLE SB                          Probe Name Ag1311                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-tccagtacctgagctggtagtt-3′   22   1016   280                   Probe   TET-5′-tggaccgagagaaccgctcacactat-3′-   26   1048   281           TAMRA               Reverse   5′-atcataggcctccagctgtag-3′   21   1077   282                    
     [0823]                   TABLE SC                          Probe Name Ag482                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-acagtgcttgtggaggatgtca-3′   22   7497   283                   Probe   TET-5′-aatgcacctgccttctcacagagcctc-3′-   27   7524   284           TAMRA               Reverse   5′-gctcaagcagcattacctggt-3′   21   7552   285                    
     [0824]                   TABLE SD                          Probe Name Ag6709                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-tcatcgacaccaatgacaatc-3′   21   6800   286                   Probe   TET-5′-ctgacactcggagctcccagggtt-3′-   24   6836   287           TAMRA               Reverse   5′-acacatggcttgccatctt-3′   19   6860   288                    
     [0825]               TABLE SE                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%)               Ag1311, Run           Tissue Name   273207795                                         AD 1 Hippo   27.0           AD 2 Hippo   44.4           AD 3 Hippo   15.7           AD 4 Hippo   21.3           AD 5 Hippo   75.8           AD 6 Hippo   100.0           Control 2 Hippo   41.2           Control 4 Hippo   33.9           Control (Path) 3 Hippo   20.7           AD 1 Temporal Ctx   31.2           AD 2 Temporal Ctx   48.3           AD 3 Temporal Ctx   16.3           AD 4 Temporal Ctx   35.4           AD 5 Inf Temporal Ctx   91.4           AD 5 Sup Temporal Ctx   50.3           AD 6 Inf Temporal Ctx   82.4           AD 6 Sup Temporal Ctx   88.9           Control 1 Temporal Ctx   36.3           Control 2 Temporal Ctx   64.6           Control 3 Temporal Ctx   33.2           Control 3 Temporal Ctx   28.9           Control (Path) 1 Temporal Ctx   72.2           Control (Path) 2 Temporal Ctx   45.7           Control (Path) 3 Temporal Ctx   24.7           Control (Path) 4 Temporal Ctx   47.3           AD 1 Occipital Ctx   27.2           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   24.1           AD 4 Occipital Ctx   22.5           AD 5 Occipital Ctx   52.1           AD 6 Occipital Ctx   21.5           Control 1 Occipital Ctx   30.1           Control 2 Occipital Ctx   61.1           Control 3 Occipital Ctx   39.0           Control 4 Occipital Ctx   25.3           Control (Path) 1 Occipital Ctx   90.1           Control (Path) 2 Occipital Ctx   16.7           Control (Path) 3 Occipital Ctx   18.6           Control (Path) 4 Occipital Ctx   20.7           Control 1 Parietal Ctx   31.6           Control 2 Parietal Ctx   59.0           Control 3 Parietal Ctx   31.0           Control (Path) 1 Parietal Ctx   77.4           Control (Path) 2 Parietal Ctx   38.7           Control (Path) 3 Parietal Ctx   24.5           Control (Path) 4 Parietal Ctx   55.9                        
     [0826]               TABLE SF                          General_screening_panel_v1.4                                 Rel. Exp. (%)               Ag1311, Run           Tissue Name   213323270                                         Adipose   7.6           Melanoma* Hs688(A).T   16.4           Melanoma* Hs688(B).T   1.0           Melanoma* M14   2.2           Melanoma* LOXIMVI   0.1           Melanoma* SK-MEL-5   0.3           Squamous cell carcinoma SCC-4   0.1           Testis Pool   0.8           Prostate ca.* (bone met) PC-3   0.1           Prostate Pool   6.0           Placenta   17.8           Uterus Pool   6.3           Ovarian ca. OVCAR-3   1.1           Ovarian ca. SK-OV-3   12.2           Ovarian ca. OVCAR-4   0.0           Ovarian ca. OVCAR-5   0.2           Ovarian ca. IGROV-1   2.9           Ovarian ca. OVCAR-8   0.2           Ovary   21.5           Breast ca. MCF-7   0.1           Breast ca. MDA-MB-231   0.3           Breast ca. BT 549   1.1           Breast ca. T47D   0.1           Breast ca. MDA-N   0.3           Breast Pool   45.7           Trachea   7.0           Lung   2.6           Fetal Lung   43.8           Lung ca. NCI-N417   0.1           Lung ca. LX-1   0.9           Lung ca. NCI-H146   10.2           Lung ca. SHP-77   0.0           Lung ca. A549   0.0           Lung ca. NCI-H526   4.4           Lung ca. NCI-H23   2.5           Lung ca. NCI-H460   0.6           Lung ca. HOP-62   0.4           Lung ca. NCI-H522   1.9           Liver   1.1           Fetal Liver   0.0           Liver ca. HepG2   0.0           Kidney Pool   67.8           Fetal Kidney   14.5           Renal ca. 786-0   0.2           Renal ca. A498   0.1           Renal ca. ACHN   0.6           Renal ca. UO-31   0.2           Renal ca. TK-10   0.0           Bladder   5.1           Gastric ca. (liver met.) NCI-N87   0.0           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.1           Colon ca. SW480   0.4           Colon ca.* (SW480 met) SW620   0.4           Colon ca. HT29   0.1           Colon ca. HCT-116   0.2           Colon ca. CaCo-2   0.9           Colon cancer tissue   10.1           Colon ca. SW1116   0.2           Colon ca. Colo-205   0.0           Colon ca. SW-48   0.1           Colon Pool   59.0           Small Intestine Pool   29.5           Stomach Pool   21.0           Bone Marrow Pool   17.2           Fetal Heart   23.0           Heart Pool   16.6           Lymph Node Pool   52.1           Fetal Skeletal Muscle   13.6           Skeletal Muscle Pool   2.8           Spleen Pool   8.4           Thymus Pool   19.3           CNS cancer (glio/astro) U87-MG   0.4           CNS cancer (glio/astro) U-118-MG   5.8           CNS cancer (neuro; met) SK-N-AS   46.0           CNS cancer (astro) SF-539   4.1           CNS cancer (astro) SNB-75   2.5           CNS cancer (glio) SNB-19   3.1           CNS cancer (glio) SF-295   33.2           Brain (Amygdala) Pool   3.3           Brain (cerebellum)   17.1           Brain (fetal)   100.0           Brain (Hippocampus) Pool   5.2           Cerebral Cortex Pool   5.6           Brain (Substantia nigra) Pool   5.9           Brain (Thalamus) Pool   4.5           Brain (whole)   14.1           Spinal Cord Pool   2.1           Adrenal Gland   4.4           Pituitary gland Pool   0.4           Salivary Gland   0.8           Thyroid (female)   2.5           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   27.4                        
     [0827]               TABLE SG                          HASS Panel v1.0                                 Rel. Exp. (%)           Tissue   Ag1311, Run           Name   268362648                                         MCF-7 C1   0.1           MCF-7 C2   0.0           MCF-7 C3   0.0           MCF-7 C4   0.1           MCF-7 C5   0.0           MCF-7 C6   0.1           MCF-7 C7   0.0           MCF-7 C9   0.0           MCF-7 C10   0.0           MCF-7 C11   0.0           MCF-7 C12   0.0           MCF-7 C13   0.0           MCF-7 C15   0.0           MCF-7 C16   0.0           MCF-7 C17   0.1           T24 D1   3.2           T24 D2   3.0           T24 D3   3.6           T24 D4   4.5           T24 D5   1.9           T24 D6   3.1           T24 D7   1.4           T24 D9   1.7           T24 D10   1.7           T24 D11   1.3           T24 D12   1.8           T24 D13   1.1           T24 D15   3.4           T24 D16   1.6           T24 D17   2.0           CAPaN B1   0.0           CAPaN B2   0.0           CAPaN B3   0.0           CAPaN B4   0.0           CAPaN B5   0.1           CAPaN B6   0.1           CAPaN B7   0.0           CAPaN B8   0.0           CAPaN B9   0.0           CAPaN B10   0.2           CAPaN B11   0.0           CAPaN B12   0.0           CAPaN B13   0.0           CAPaN B14   0.0           CAPaN B15   0.0           CAPaN B16   0.0           CAPaN B17   0.1           U87-MG F1 (B)   0.2           U87-MG F2   0.9           U87-MG F3   1.5           U87-MG F4   0.5           U87-MG F5   2.4           U87-MG F6   1.1           U87-MG F7   0.9           U87-MG F8   1.4           U87-MG F9   1.0           U87-MG F10   0.8           U87-MG F11   0.6           U87-MG F12   0.3           U87-MG F13   1.4           U87-MG F14   1.5           U87-MG F15   0.9           U87-MG F16   1.4           U87-MG F17   1.9           LnCAP A1   0.3           LnCAP A2   0.6           LnCAP A3   0.2           LnCAP A4   0.5           LnCAP A5   0.7           LnCAP A6   0.1           LnCAP A7   0.9           LnCAP A8   1.3           LnCAP A9   0.3           LnCAP A10   0.1           LnCAP A11   2.4           LnCAP A12   0.1           LnCAP A13   0.1           LnCAP A14   0.7           LnCAP A15   0.4           LnCAP A16   0.4           LnCAP A17   1.3           Primary Astrocytes   29.1           Primary Renal Proximal Tubule   0.1           Epithelial cell A2           Primary melanocytes A5   2.8           126443-341 medullo   2.3           126444-487 medullo   77.4           126445-425 medullo   3.4           126446-690 medullo   90.8           126447-54 adult glioma   0.2           126448-245 adult glioma   6.0           126449-317 adult glioma   38.4           126450-212 glioma   100.0           126451-456 glioma   27.4                        
     [0828]               TABLE SH                          Oncology_cell_line_screening_panel_v3.2                                 Rel. Exp. (%)               Ag1311, Run           Tissue Name   264977450                                         94905_Daoy_Medulloblastoma/   1.0           Cerebellum_sscDNA           94906_TE671_Medulloblastoma/   15.4           Cerebellum_sscDNA           94907_D283 Med_Medulloblastoma/   4.7           Cerebellum_sscDNA           94908_PFSK-1_Primitive Neuroectodermal/   1.1           Cerebellum_sscDNA           94909_XF-498_CNS_sscDNA   2.0           94910_SNB-78_CNS/glioma_sscDNA   0.0           94911_SF-268_CNS/glioblastoma_sscDNA   0.9           94912_T98G_Glioblastoma_sscDNA   0.6           96776_SK-N-SH_Neuroblastoma   16.2           (metastasis)_sscDNA           94913_SF-295_CNS/glioblastoma_sscDNA   10.2           132565_NT2 pool_sscDNA   4.2           94914_Cerebellum_sscDNA   5.7           96777_Cerebellum_sscDNA   8.9           94916_NCI-H292_Mucoepidermoid lung   0.5           carcinoma_sscDNA           94917_DMS-114_Small cell lung   7.7           cancer_sscDNA           94918_DMS-79_Small cell lung   100.0           cancer/neuroendocrine_sscDNA           94919_NCI-H146_Small cell lung   24.3           cancer/neuroendocrine_sscDNA           94920_NCI-H526_Small cell lung   11.4           cancer/neuroendocrine_sscDNA           94921_NCI-N417_Small cell lung   0.0           cancer/neuroendocrine_sscDNA           94923_NCI-H82_Small cell lung   28.5           cancer/neuroendocrine_sscDNA           94924_NCI-H157_Squamous cell   0.4           lung cancer (metastasis)_sscDNA           94925_NCI-H1155_Large cell lung   25.3           cancer/neuroendocrine_sscDNA           94926_NCI-H1299_Large cell lung   0.3           cancer/neuroendocrine_sscDNA           94927_NCI-H727_Lung carcinoid —     0.2           sscDNA           94928_NCI-UMC-11_Lung carcinoid —     0.8           sscDNA           94929_LX-1_Small cell lung   0.2           cancer_sscDNA           94930_Colo-205_Colon cancer_sscDNA   0.0           94931_KM12_Colon cancer_sscDNA   0.1           94932_KM20L2_Colon cancer_sscDNA   0.1           94933_NCI-H716_Colon cancer_sscDNA   0.5           94935_SW-48_Colon adenocarcinoma —     0.0           sscDNA           94936_SW1116_Colon   0.6           adenocarcinoma_sscDNA           94937_LS 174T_Colon   0.1           adenocarcinoma_sscDNA           94938_SW-948_Colon   0.0           adenocarcinoma_sscDNA           94939_SW-480_Colon   0.0           adenocarcinoma_sscDNA           94940_NCI-SNU-5_Gastric   0.1           carcinoma_sscDNA           112197_KATO III_Stomach_sscDNA   0.0           94943_NCI-SNU-16_Gastric   0.0           carcinoma_sscDNA           94944_NCI-SNU-1_Gastric   0.1           carcinoma_sscDNA           94946_RF-1_Gastric   0.3           adenocarcinoma_sscDNA           94947_RF-48_Gastric   0.4           adenocarcinoma_sscDNA           96778_MKN-45_Gastric   0.0           carcinoma_sscDNA           94949_NCI-N87_Gastric   0.0           carcinoma_sscDNA           94951_OVCAR-5_Ovarian   0.0           carcinoma_sscDNA           94952_RL95-2_Uterine   0.0           carcinoma_sscDNA           94953_HelaS3_Cervical   0.0           adenocarcinoma_sscDNA           94954_Ca Ski_Cervical   0.0           epidermoid carcinoma           (metastasis)_sscDNA           94955_ES-2_Ovarian clear   2.2           cell carcinoma_sscDNA           94957_Ramos/6 h stim_Stimulated   0.0           with PMA/ionomycin 6 h_sscDNA           94958_Ramos/14 h stim_Stimulated   0.2           with PMA/ionomycin 14 h_sscDNA           94962_MEG-01_Chronic myelogenous   0.3           leukemia (megokaryoblast)_sscDNA           94963_Raji_Burkitt&#39;s lymphoma —     0.0           sscDNA           94964_Daudi_Burkitt&#39;s lymphoma —     0.0           sscDNA           94965_U266_B-cell plasmacytoma/   0.1           myeloma_sscDNA           94968_CA46_Burkitt&#39;s lymphoma_sscDNA   0.0           94970_RL_non-Hodgkin&#39;s B-cell   0.0           lymphoma_sscDNA           94972_JM1_pre-B-cell lymphoma/   0.4           leukemia_sscDNA           94973_Jurkat_T cell leukemia_sscDNA   0.3           94974_TF-1_Erythroleukemia_sscDNA   0.0           94975_HUT 78_T-cell lymphoma_sscDNA   0.0           94977_U937_Histiocytic lymphoma —     0.2           sscDNA           94980_KU-812_Myelogenous   0.1           leukemia_sscDNA           94981_769-P_Clear cell renal   0.2           carcinoma_sscDNA           94983_Caki-2_Clear cell renal   0.1           carcinoma_sscDNA           94984_SW 839_Clear cell renal   0.0           carcinoma_sscDNA           94986_G401_Wilms&#39; tumor_sscDNA   0.2           126768_293 cells_sscDNA   1.6           94987_Hs766T_Pancreatic carcinoma   0.3           (LN metastasis)_sscDNA           94988_CAPAN-1_Pancreatic   0.0           adenocarcinoma (liver           metastasis)_sscDNA           94989_SU86.86_Pancreatic   1.0           carcinoma (liver           metastasis)_sscDNA           94990_BxPC-3_Pancreatic   0.4           adenocarcinoma_sscDNA           94991_HPAC_Pancreatic   0.0           adenocarcinoma_sscDNA           94992_MIA PaCa-2_Pancreatic   0.2           carcinoma_sscDNA           94993_CFPAC-1_Pancreatic ductal   0.1           adenocarcinoma_sscDNA           94994_PANC-1_Pancreatic   1.3           epithelioid ductal           carcinoma_sscDNA           94996_T24_Bladder carcinma   0.2           (transitional cell)_sscDNA           94997_5637_Bladder carcinoma —     0.0           sscDNA           94998_HT-1197_Bladder carcinoma —     0.1           sscDNA           94999_UM-UC-3_Bladder carcinma   0.0           (transitional cell)_sscDNA           95000_A204_Rhabdomyosarcoma_sscDNA   0.3           95001_HT-1080_Fibrosarcoma —     0.6           sscDNA           95002_MG-63_Osteosarcoma (bone) —     5.0           sscDNA           95003_SK-LMS-1_Leiomyosarcoma   3.5           (vulva)_sscDNA           95004_SJRH30_Rhabdomyosarcoma (met   6.4           to bone marrow)_sscDNA           95005_A431_Epidermoid carcinoma —     0.1           sscDNA           95007_WM266-4_Melanoma_sscDNA   0.1           112195_DU 145_Prostate_sscDNA   0.0           95012_MDA-MB-468_Breast   0.1           adenocarcinoma_sscDNA           112196_SSC-4_Tongue_sscDNA   0.0           112194_SSC-9_Tongue_sscDNA   0.1           112191_SSC-15_Tongue_sscDNA   0.1           95017_CAL 27_Squamous cell   0.0           carcinoma of tongue_sscDNA                        
     [0829]               TABLE SI                          Panel 1                                 Rel. Exp. (%)               Ag482, Run           Tissue Name   121039178                                         Endothelial cells   21.3           Endothelial cells (treated)   17.6           Pancreas   10.4           Pancreatic ca. CAPAN2   0.0           Adrenal gland   12.2           Thyroid   5.5           Salivary gland   6.6           Pituitary gland   35.4           Brain (fetal)   49.0           Brain (whole)   10.7           Brain (amygdala)   18.0           Brain (cerebellum)   11.2           Brain (hippocampus)   14.8           Brain (substantia nigra)   11.0           Brain (thalamus)   13.6           Brain (hypothalamus)   14.9           Spinal cord   8.1           glio/astro U87-MG   0.0           glio/astro U-118-MG   2.7           astrocytoma SW1783   3.8           neuro*; met SK-N-AS   61.6           astrocytoma SF-539   1.3           astrocytoma SNB-75   0.1           glioma SNB-19   17.2           glioma U251   0.6           glioma SF-295   23.7           Heart   38.2           Skeletal muscle   8.0           Bone marrow   3.6           Thymus   20.6           Spleen   18.2           Lymph node   9.9           Colon (ascending)   19.9           Stomach   11.3           Small intestine   20.4           Colon ca. SW480   2.1           Colon ca.* SW620 (SW480 met)   0.0           Colon ca. HT29   0.0           Colon ca. HCT-116   0.0           Colon ca. CaCo-2   4.5           Colon ca. HCT-15   0.0           Colon ca. HCC-2998   5.1           Gastric ca.* (liver met) NCI-N87   0.0           Bladder   15.3           Trachea   7.6           Kidney   21.6           Kidney (fetal)   33.4           Renal ca. 786-0   0.1           Renal ca. A498   0.0           Renal ca. RXF 393   0.0           Renal ca. ACHN   0.0           Renal ca. UO-31   0.0           Renal ca. TK-10   0.0           Liver   13.2           Liver (fetal)   14.2           Liver ca. (hepatoblast) HepG2   0.0           Lung   17.1           Lung (fetal)   10.2           Lung ca. (small cell) LX-1   2.6           Lung ca. (small cell) NCI-H69   1.6           Lung ca. (s. cell var.) SHP-77   0.0           Lung ca. (large cell)NCI-H460   3.0           Lung ca. (non-sm. cell) A549   0.0           Lung ca. (non-s. cell) NCI-H23   2.4           Lung ca. (non-s. cell) HOP-62   1.9           Lung ca. (non-s. cl) NCI-H522   5.4           Lung ca. (squam.) SW 900   0.0           Lung ca. (squam.) NCI-H596   1.5           Mammary gland   57.4           Breast ca.* (pl. ef) MCF-7   0.1           Breast ca.* (pl. ef) MDA-MB-231   0.1           Breast ca.* (pl. ef) T47D   0.0           Breast ca. BT-549   0.0           Breast ca. MDA-N   0.1           Ovary   100.0           Ovarian ca. OVCAR-3   4.4           Ovarian ca. OVCAR-4   0.0           ovarian ca. OVCAR-5   0.0           Ovarian ca. OVCAR-8   19.9           Ovarian ca. IGROV-1   3.3           Ovarian ca. (ascites) SK-OV-3   13.1           Uterus   17.6           Placenta   30.4           Prostate   17.2           Prostate ca.* (bone met) PC-3   0.0           Testis   22.7           Melanoma Hs688(A).T   11.7           Melanoma* (met) Hs688(B).T   3.8           Melanoma UACC-62   1.6           Melanoma M14   0.4           Melanoma LOX IMVI   0.0           Melanoma* (met) SK-MEL-5   0.0           Melanoma SK-MEL-28   0.0                        
     [0830]               TABLE SJ                          Panel 1.2                                 Rel. Exp. (%)               Ag1311, Run           Tissue Name   129674732                                         Endothelial cells   30.1           Heart (Fetal)   100.0           Pancreas   3.3           Pancreatic ca. CAPAN 2   0.0           Adrenal Gland   8.4           Thyroid   2.7           Salivary gland   4.8           Pituitary gland   4.8           Brain (fetal)   10.9           Brain (whole)   4.7           Brain (amygdala)   3.8           Brain (cerebellum)   4.5           Brain (hippocampus)   7.2           Brain (thalamus)   2.9           Cerebral Cortex   25.7           Spinal cord   4.2           glio/astro U87-MG   0.3           glio/astro U-118-MG   2.2           astrocytoma SW1783   1.0           neuro*; met SK-N-AS   22.5           astrocytoma SF-539   2.1           astrocytoma SNB-75   0.7           glioma SNB-19   4.6           glioma U251   0.2           glioma SF-295   0.2           Heart   36.9           Skeletal Muscle   5.8           Bone marrow   0.3           Thymus   2.2           Spleen   2.7           Lymph node   5.0           Colorectal Tissue   3.1           Stomach   9.4           Small intestine   9.3           Colon ca. SW480   0.0           Colon ca.* SW620 (SW480 met)   0.1           Colon ca. HT29   0.0           Colon ca. HCT-116   0.1           Colon ca. CaCo-2   0.4           Colon ca. Tissue (ODO3866)   4.1           Colon ca. HCC-2998   0.1           Gastric ca.* (liver met) NCI-N87   0.0           Bladder   9.3           Trachea   2.5           Kidney   7.6           Kidney (fetal)   26.8           Renal ca. 786-0   0.1           Renal ca. A498   0.1           Renal ca. RXF 393   0.0           Renal ca. ACHN   0.1           Renal ca. UO-31   0.1           Renal ca. TK-10   0.0           Liver   5.8           Liver (fetal)   3.3           Liver ca. (hepatoblast) HepG2   0.2           Lung   4.9           Lung (fetal)   7.0           Lung ca. (small cell) LX-1   0.2           Lung ca. (small cell) NCI-H69   0.9           Lung ca. (s. cell var.) SHP-77   0.0           Lung ca. (large cell) NCI-H460   1.1           Lung ca. (non-sm. cell) A549   0.1           Lung ca. (non-s. cell)NCI-H23   0.2           Lung ca. (non-s. cell) HOP-62   4.4           Lung ca. (non-s. cl) NCI-H522   1.3           Lung ca. (squam.) SW 900   0.2           Lung ca. (squam.) NCI-H596   0.6           Mammary gland   12.6           Breast ca.* (pl. ef) MCF-7   0.0           Breast ca.* (pl. ef) MDA-MB-231   0.1           Breast ca.* (pl. ef) T47D   0.0           Breast ca. BT-549   0.1           Breast ca. MDA-N   0.2           Ovary   41.5           Ovarian ca. OVCAR-3   0.3           Ovarian ca. OVCAR-4   0.1           Ovarian ca. OVCAR-5   0.1           Ovarian ca. OVCAR-8   1.0           Ovarian ca. IGROV-1   0.0           Ovarian ca. (ascites) SK-OV-3   4.0           Uterus   12.4           Placenta   19.6           Prostate   7.0           Prostate ca.* (bone met) PC-3   0.1           Testis   3.2           Melanoma Hs688(A).T   4.6           Melanoma* (met) Hs688(B).T   13.0           Melanoma UACC-62   0.3           Melanoma M14   0.1           Melanoma LOX IMVI   0.0           Melanoma* (met) SK-MEL-5   0.1                        
     [0831]               TABLE SK                          Panel 4D                                 Rel. Exp. (%)               Ag1311, Run           Tissue Name   138960982                                         Secondary Th1 act   0.4           Secondary Th2 act   2.0           Secondary Tr1 act   1.6           Secondary Th1 rest   0.2           Secondary Th2 rest   0.1           Secondary Tr1 rest   0.3           Primary Th1 act   0.7           Primary Th2 act   1.2           Primary Tr1 act   0.6           Primary Th1 rest   2.8           Primary Th2 rest   2.4           Primary Tr1 rest   0.7           CD45RA CD4 lymphocyte act   11.8           CD45RO CD4 lymphocyte act   2.2           CD8 lymphocyte act   1.4           Secondary CD8 lymphocyte rest   1.2           Secondary CD8 lymphocyte act   0.3           CD4 lymphocyte none   8.5           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.5           LAK cells rest   5.9           LAK cells IL-2   0.6           LAK cells IL-2 + IL-12   2.2           LAK cells IL-2 + IFN gamma   2.5           LAK cells IL-2 + IL-18   1.3           LAK cells PMA/ionomycin   8.5           NK Cells IL-2 rest   3.7           Two Way MLR 3 day   1.7           Two Way MLR 5 day   2.4           Two Way MLR 7 day   2.4           PBMC rest   1.4           PBMC PWM   1.2           PBMC PHA-L   1.7           Ramos (B cell) none   0.3           Ramos (B cell) ionomycin   1.4           B lymphocytes PWM   1.6           B lymphocytes CD40L and IL-4   1.0           EOL-1 dbcAMP   0.1           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   2.8           Dendritic cells LPS   0.6           Dendritic cells anti-CD40   0.9           Monocytes rest   1.0           Monocytes LPS   1.1           Macrophages rest   1.7           Macrophages LPS   1.4           HUVEC none   45.7           HUVEC starved   75.8           HUVEC IL-1beta   22.4           HUVEC IFN gamma   100.0           HUVEC TNF alpha + IFN gamma   11.7           HUVEC TNF alpha + IL4   24.5           HUVEC IL-11   38.2           Lung Microvascular EC none   54.3           Lung Microvascular EC TNFalpha + IL-   24.3           1beta           Microvascular Dermal EC none   79.0           Microsvasular Dermal EC TNFalpha +   51.4           IL-1beta           Bronchial epithelium TNFalpha +   0.0           IL1beta           Small airway epithelium none   0.0           Small airway epithelium TNFalpha +   1.2           IL-1beta           Coronery artery SMC rest   2.1           Coronery artery SMC TNFalpha + IL-   3.5           1beta           Astrocytes rest   19.3           Astrocytes TNFalpha + IL-1beta   8.2           KU-812 (Basophil) rest   0.3           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   0.7           CCD1106 (Keratinocytes) TNFalpha +   0.6           IL-1beta           Liver cirrhosis   3.3           Lupus kidney   1.4           NCI-H292 none   1.6           NCI-H292 IL-4   1.4           NCI-H292 IL-9   0.7           NCI-H292 IL-13   1.7           NCI-H292 IFN gamma   2.1           HPAEC none   56.6           HPAEC TNF alpha + IL-1 beta   41.8           Lung fibroblast none   22.4           Lung fibroblast TNF alpha + IL-1 beta   14.8           Lung fibroblast IL-4   33.4           Lung fibroblast IL-9   23.2           Lung Fibroblast IL-13   50.7           Lung fibroblast IFN gamma   52.1           Dermal fibroblast CCD1070 rest   23.5           Dermal fibroblast CCD1070 TNF alpha   19.3           Dermal fibroblast CCD1070 IL-1 beta   19.9           Dermal fibroblast IFN gamma   29.7           Dermal fibroblast IL-4   62.0           IBD Colitis 2   2.1           IBD Crohn&#39;s   2.6           Colon   20.0           Lung   75.3           Thymus   29.7           Kidney   32.5                        
     [0832]               TABLE SL                          general oncology screening panel_v_2.4                                 Rel. Exp. (%)               Ag1311, Run           Tissue Name   259733190                                         Colon cancer 1   10.6           Colon cancer NAT 1   7.6           Colon cancer 2   6.6           Colon cancer NAT 2   3.1           Colon cancer 3   9.4           Colon cancer NAT 3   12.9           Colon malignant cancer 4   8.2           Colon normal adjacent tissue 4   2.0           Lung cancer 1   4.3           Lung NAT 1   2.1           Lung cancer 2   50.3           Lung NAT 2   2.9           Squamous cell carcinoma 3   9.9           Lung NAT 3   0.6           metastatic melanoma 1   24.5           Melanoma 2   2.7           Melanoma 3   0.7           metastatic melanoma 4   100.0           metastatic melanoma 5   87.7           Bladder cancer 1   1.5           Bladder cancer NAT 1   0.0           Bladder cancer 2   2.8           Bladder cancer NAT 2   0.5           Bladder cancer NAT 3   0.4           Bladder cancer NAT 4   6.5           Prostate adenocarcinoma 1   43.2           Prostate adenocarcinoma 2   3.5           Prostate adenocarcinoma 3   2.7           Prostate adenocarcinoma 4   7.6           Prostate cancer NAT 5   2.9           Prostate adenocarcinoma 6   2.1           Prostate adenocarcinoma 7   5.6           Prostate adenocarcinoma 8   1.8           Prostate adenocarcinoma 9   28.7           Prostate cancer NAT 10   1.4           Kidney cancer 1   17.6           Kidney NAT 1   2.6           Kidney cancer 2   20.2           Kidney NAT 2   5.2           Kidney cancer 3   8.7           Kidney NAT 3   3.0           Kidney cancer 4   11.2           Kidney NAT 4   2.4                        
     [0833] CNS_neurodegeneration_v1.0 Summary: Ag1311 This panel confirms the expression of this gene at moderate levels in the brain in an independent group of individuals. This gene appears to be slightly down-regulated in the temporal cortex of Alzheimer&#39;s disease patients. Therefore, up-regulation of this gene or its protein product, or treatment with specific agonists for this receptor may be of use in reversing the dementia, memory loss, and neuronal death associated with this disease. Ag6709 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0834] General_screening_panel_v1.4 Summary: Ag1311 Highest expression of this gene is seen in the fetal brain (CT=25). Thus, expression of this gene could be used to differentiate between fetal and adult brain tissue. Moderate levels of expression are seen in all regions of the CNS examined. This gene has homology to cadherin, transmembrane glycoproteins that are involved in many biological processes such as cell adhesion, cytoskeletal organization and morphogenesis. Cadherins can act as axon guidance and cell adhesion proteins, specifically during development and in the response to injury (Ranscht B. Int. J. Dev. Neurosci. 18: 643-651). Therefore, manipulation of levels of this protein may be of use in inducing a compensatory synaptogenic response to neuronal death in Alzheimer&#39;s disease, Parkinson&#39;s disease, Huntington&#39;s disease, spinocerebellar ataxia, progressive supranuclear palsy, ALS, head trauma, stroke, or any other disease/condition associated with neuronal loss.  
     [0835] As in Panel 1.2, this gene is expressed at high to moderate levels in metabolic tissues, including pancreas, pituitary, adipose, adrenal gland, pancreas, thyroid, liver and adult and fetal skeletal muscle, and heart. Please see Panel 1.2 for discussion of utility of this gene in metabolic disease.  
     [0836] Moderate levels of expression are also seen in cancer cell lines derived from melanoma, ovarian, lung, colon and brain cancers.  
     [0837] General_screening_panel_v1.6 Summary: Ag6709 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0838] HASS Panel v1.0 Summary: Ag1311 Highest expression of this gene is detected in glioma cells (CT=27.3). This gene is expressed at a low to moderate level in samples of brain cancer as well as primary astrocytes in culture. Expression is also slightly increased in LnCAP and U87 cells that are subjected to cell stresses such as reduced oxygen, low serum or an acidotic environment which are some of the conditions seen in tumors.  
     [0839] Oncology_cell_line_screening_panel_v3.2 Summary: Ag1311 Highest expression of this gene is seen in a lung cancer cell line (CT=27.5). Moderate levels of expression of this gene are also seen in a cluster of samples derived from lung cancer cell lines, bone cancer cell lines and brain cancer cell lines. Please see Panels 1.2 and 2.4 for discussion of utility of this gene in cancer.  
     [0840] Panel 1 Summary: Ag482 Highest expression is seen in ovary (CT=24.3), with high levels of expression in many samples on this panel including melanoma, ovarian, and brain cancer cell lines and normal lung, liver, heart, muscle, brain, pancreas, adrenal, and endothelial cells. This expression is in agreement with results of panels run with Ag1311. Please see those experiments for discussion of utility of this gene in metabolic and autoimmune disorders and cancer.  
     [0841] Panel 1.2 Summary: Ag1311 The protein encoded by this gene is homologous to cadherin, a cell-adhesion protein and is highly expressed in a number of samples on panel 1.2. Specifically, the highest expression is detected in fetal heart (CT value=22.6), although it is also highly expressed in adult heart. This may suggest a potential role for this gene in cardiovascular diseases such as cardiomyopathy, atherosclerosis, hypertension congenital heart defects, aortic stenosis, atrial septal defect (asd), atrioventricular (a-v) canal defect, ductus arteriosus, pulmonary stenosis, subaortic stenosis, ventricular septal defect (vsd), and valve diseases. Overall, gene expression in this panel is associated with normal tissues rather than cancel cell lines. Loss of function of the related E-cadherin protein has been described in many tumors, along with an increased invasiveness and a decreased prognosis of many carcinomas, including tumors of endocrine glands and their target systems (ref 1). Thus, this gene product might similarly be useful as a protein therapeutic to treat a variety of tumors, since it is found in normal cells but missing from cancer cells.  
     [0842] In addition, this gene is highly expressed in pituitary gland, adrenal gland, thyroid, pancreas, skeletal muscle, and liver, reflecting the widespread role of cadherins in cell-cell adhesion. This observation may suggest that the gene plays a role in normal metabolic and neuroendocrine function and that disregulated expression of this gene may contribute to metabolic diseases (such as obesity and diabetes) or neuroendocrine disorders.  
     [0843] Expression of this gene is also high in many regions of the brain, including the amygdala, thalamus, cerebellum, and cerebral cortex, with highest expression in the hippocampus. Expression is also detected in the spinal cord. Cadherins can act as axon guidance and cell adhesion proteins, specifically during development and in the response to injury (ref 2). Manipulation of levels of this protein may be of use in inducing a compensatory synaptogenic response to neuronal death in Alzheimer&#39;s disease, Parkinson&#39;s disease, Huntington&#39;s disease, spinocerebellar ataxia, progressive supranuclear palsy, ALS, head trauma, stroke, or any other disease/condition associated with neuronal loss.  
     [0844] Reference:  
     [0845] 1. Potter E., Bergwitz C., Brabant G. (1999) The cadherin-catenin system: implications for growth and differentiation of endocrine tissues. Endocr. Rev. 20: 207-239.  
     [0846] 2. Ranscht B. (2000) Cadherins: molecular codes for axon guidance and synapse formation. Int. J. Dev. Neurosci. 18: 643-651.  
     [0847] Panel 4D Summary: Ag1311 Expression of this gene is primarily in endothelial cells and in fibroblasts. However, this gene is also expressed in the kidney, thymus, lung and colon. The expression of this gene is high in normal tissue and untreated cells and is not affected by most treatments with the exception of IL-1 alpha and TNFbeta, which reduce expression of this gene by half in treated HUVECs and reduce expression 10-fold in gamma interferon treated HUVECs. Therefore, the protein encoded for by this gene may be important in normal function of endothelium and fibroblasts. Protein therapeutics designed with the protein encoded for by this transcript could reduce or block inflammation in diseases such as asthma, emphysema, allergy, arthritis, IBD and psoriasis.  
     [0848] Panel 4.1D Summary: Ag6709 Expression of this gene is low/undetectable in all samples on this panel (CTs&gt;35).  
     [0849] general oncology screening panel_v — 2.4 Summary: Ag1311 Highest expression of this gene is seen in a sample from metastatic melanoma (CT=27). Moderate to high levels of expression are also seen samples from colon, kidney, bladder, and prostate cancers. In addition, higher levels of expression are seen in prostate, lung, and kidney cancers when compared to expression in normal adjacent tissue. This gene encodes a putative cadherin, similar to VE cadherin that shows specific expression in mesenchymal cells, fibroblasts and endothelial cells. On Panel 4 this gene shows expression in fibroblasts and endothelial cells and is induced by starvation in Huvec. Activated fibroblasts have shown to be involved in supporting tumor cells (Okada, Lab Invest 2000 November;80(11): 1617-28). Corada et al (Blood Mar 15, 2001;97(6):1679-84) has shown that there are epitopes in VE Cadherin that are only exposed upon activation of the endothelial cells, probably due to changes in cell-cell adhesions. mAbs against those epitopes have antitumor activities without inducing bleeding. Therefore, based on the expression of this gene in fibroblasts and tumors, and the homology of the protein product to cadherin, targeting of this gene product with a human monoclonal antibody that results in an inhibition of the activity of this protein, preferably as it relates to endothelial and fibroblast activation by tumor cells, may have therapeutic effect on all solid tumors that depend on angiogenesis, and specifically on colon, lung, kidney, melanoma, prostate and bladder. Results from a second experiment with the same probe and primer set, run 263102793, are not included because the amp plot indicates there were experimental difficulties with this run.  
     [0850] T. NOV20a (CG132888-02): M130 Antigen.  
     [0851] Expression of gene CG132888-02 was assessed using the primer-probe set Ag4955, described in Table TA. Results of the RTQ-PCR runs are shown in Tables TB, TC and TD.  
                   TABLE TA                          Probe Name Ag4955                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gaggagacctggatcacatgt-3′   21   2841   289                   Probe   TET-5′-aagacttcaggaaggacccacttcct-3′-   26   2873   290           TAMRA               Reverse   5′-agatctccacacgtccagaac-3′   21   2899   291                  
 
     [0852]               TABLE TB                          General_screening_panel_v1.5                                 Rel. Exp. (%)               Ag4955, Run           Tissue Name   228886961                                         Adipose   27.7           Melanoma* Hs688(A).T   0.2           Melanoma* Hs688(B).T   0.0           Melanoma* M14   0.0           Melanoma* LOXIMVI   0.1           Melanoma* SK-MEL-5   0.0           Squamous cell carcinoma SCC-4   0.2           Testis Pool   6.5           Prostate ca.* (bone met) PC-3   0.0           Prostate Pool   2.4           Placenta   8.2           Uterus Pool   6.8           Ovarian ca. OVCAR-3   0.0           Ovarian ca. SK-OV-3   0.0           Ovarian ca. OVCAR-4   0.0           Ovarian ca. OVCAR-5   0.0           Ovarian ca. IGROV-1   0.0           Ovarian ca. OVCAR-8   0.0           Ovary   11.2           Breast ca. MCF-7   0.0           Breast ca. MDA-MB-231   0.0           Breast ca. BT 549   0.4           Breast ca. T47D   0.0           Breast ca. MDA-N   0.0           Breast Pool   5.6           Trachea   5.1           Lung   1.0           Fetal Lung   5.0           Lung ca. NCI-N417   0.0           Lung ca. LX-1   0.0           Lung ca. NCI-H146   0.0           Lung ca. SHP-77   0.0           Lung ca. A549   0.0           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   0.0           Lung ca. NCI-H460   0.0           Lung ca. HOP-62   0.0           Lung ca. NCI-H522   0.0           Liver   9.0           Fetal Liver   29.5           Liver ca. HepG2   0.0           Kidney Pool   15.8           Fetal Kidney   2.1           Renal ca. 786-0   0.0           Renal ca. A498   0.0           Renal ca. ACHN   0.0           Renal ca. UO-31   0.0           Renal ca. TK-10   0.0           Bladder   100.0           Gastric ca. (liver met.) NCI-N87   1.8           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.0           Colon ca. SW480   0.0           Colon ca.* (SW480 met) SW620   0.0           Colon ca. HT29   0.0           Colon ca. HCT-116   0.0           Colon ca. CaCo-2   0.1           Colon cancer tissue   38.4           Colon ca. SW1116   0.0           Colon ca. Colo-205   0.0           Colon ca. SW-48   0.0           Colon Pool   10.0           Small Intestine Pool   5.3           Stomach Pool   18.3           Bone Marrow Pool   4.1           Fetal Heart   0.9           Heart Pool   3.3           Lymph Node Pool   5.1           Fetal Skeletal Muscle   2.3           Skeletal Muscle Pool   11.7           Spleen Pool   28.1           Thymus Pool   14.2           CNS cancer (glio/astro) U87-MG   0.1           CNS cancer (glio/astro) U-118-MG   0.1           CNS cancer (neuro; met) SK-N-AS   0.0           CNS cancer (astro) SF-539   0.0           CNS cancer (astro) SNB-75   0.0           CNS cancer (glio) SNB-19   0.0           CNS cancer (glio) SF-295   0.1           Brain (Amygdala) Pool   0.5           Brain (cerebellum)   1.2           Brain (fetal)   2.4           Brain (Hippocampus) Pool   1.3           Cerebral Cortex Pool   1.2           Brain (Substantia nigra) Pool   0.3           Brain (Thalamus) Pool   0.6           Brain (whole)   4.6           Spinal Cord Pool   4.4           Adrenal Gland   41.2           Pituitary gland Pool   0.7           Salivary Gland   1.0           Thyroid (female)   3.0           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   10.4                        
     [0853]               TABLE TC                          Panel 4.1D                                 Rel. Exp. (%)               Ag4955, Run           Tissue Name   223629644                                         Secondary Th1 act   0.0           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.0           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.1           Primary Th1 rest   0.0           Primary Th2 rest   0.0           Primary Tr1 rest   0.0           CD45RA CD4 lymphocyte act   0.0           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.3           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   0.2           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0           LAK cells rest   12.2           LAK cells IL-2   0.1           LAK cells IL-2 + IL-12   0.2           LAK cells 1L-2 + IFN gamma   0.1           LAK cells IL-2 + IL-18   0.3           LAK cells PMA/ionomycin   14.6           NK Cells IL-2 rest   0.0           Two Way MLR 3 day   10.6           Two Way MLR 5 day   4.6           Two Way MLR 7 day   0.6           PBMC rest   10.0           PBMC PWM   0.8           PBMC-PHA-L   7.8           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   0.0           EOL-1 dbcAMP   0.2           EOL-1 dbcAMP PMA/ionomycin   1.5           Dendritic cells none   36.3           Dendritic cells LPS   1.9           Dendritic cells anti-CD40   20.3           Monocytes rest   60.7           Monocytes LPS   100.0           Macrophages rest   59.5           Macrophages LPS   10.2           HUVEC none   0.0           HUVEC starved   0.0           HUVEC IL-1beta   0.0           HUVEC IFN gamma   0.0           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.2           Lung Microvascular EC none   0.0           Lung Microvascular EC TNFalpha +   0.0           IL-1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   0.0           IL1beta           Small airway epithelium none   0.0           Small airway epithelium TNFalpha +   0.0           IL-1beta           Coronery artery SMC rest   0.0           Coronery artery SMC TNFalpha + IL-   0.0           1beta           Astrocytes rest   0.0           Astrocytes TNFalpha + IL-1beta   0.0           KU-812 (Basophil) rest   0.1           KU-812 (Basophil) PMA/ionomycin   0.1           CCD1106 (Keratinocytes) none   0.1           CCD1106 (Keratinocytes) TNFalpha +   0.0           IL-1beta           Liver cirrhosis   12.5           NCI-H292 none   0.0           NCI-H292 IL-4   0.0           NCI-H292 IL-9   0.0           NCI-H292 IL-13   0.0           NCI-H292 IFN gamma   0.0           HPAEC none   0.0           HPAEC TNF alpha + IL-1 beta   0.0           Lung fibroblast none   0.0           Lung fibroblast TNF alpha + IL-1   0.2           beta           Lung fibroblast IL-4   0.0           Lung fibroblast IL-9   0.0           Lung fibroblast IL-13   0.5           Lung fibroblast IFN gamma   0.1           Dermal fibroblast CCD1070 rest   0.0           Dermal fibroblast CCD1070 TNF alpha   0.0           Dermal fibroblast CCD1070 IL-1 beta   0.1           Dermal fibroblast IFN gamma   0.2           Dermal fibroblast IL-4   0.2           Dermal Fibroblasts rest   0.5           Neutrophils TNFa + LPS   0.4           Neutrophils rest   0.2           Colon   3.7           Lung   55.1           Thymus   11.3           Kidney   2.6                        
     [0854]               TABLE TD                          Panel 5 Islet                                 Rel. Exp. (%)               Ag4955, Run           Tissue Name   263594804                                         97457_Patient-02go_adipose   1.1           97476_Patient-07sk_skeletal muscle   4.8           97477_Patient-07ut_uterus   9.3           97478_Patient-07pl_placenta   42.6           99167_Bayer Patient 1   0.0           97482_Patient-08ut_uterus   63.7           97483_Patient-08pl_placenta   2.3           97486_Patient-09sk_skeletal muscle   0.7           97487_Patient-09ut_uterus   7.1           97488_Patient-09pl_placenta   33.7           97492_Patient-10ut_uterus   29.3           97493_Patient-10pl_placenta   100.0           97495_Patient-11go_adipose   0.1           97496_Patient-11sk_skeletal muscle   1.1           97497_Patient-11ut_uterus   12.2           97498_Patient-11pl_placenta   12.1           97500_Patient-12go_adipose   84.1           97501_Patient-12sk_skeletal muscle   24.1           97502_Patient-12ut_uterus   1.0           97503_Patient-12pl_placenta   1.8           94721_Donor 2 U - A_Mesenchymal Stem   0.0           Cells           94722_Donor 2 U - B Mesenchymal Stem   0.0           Cells           94723_Donor 2 U - C_Mesenchymal Stem   0.1           Cells           94709_Donor 2 AM - A_adipose   0.9           94710_Donor 2 AM - B_adipose   0.0           94711_Donor 2 AM - C_adipose   0.0           94712_Donor 2 AD - A_adipose   0.0           94713_Donor 2 AD - B_adipose   0.0           94714_Donor 2 AD - C_adipose   0.3           94742_Donor 3 U - A_Mesenchymal   0.0           Stem Cells           94743_Donor 3 U - B_Mesenchymal   0.0           Stem Cells           94730_Donor 3 AM - A_adipose   0.0           94731_Donor 3 AM - B_adipose   0.0           94732_Donor 3 AM - C_adipose   0.0           94733_Donor 3 AD - A_adipose   0.0           94734_Donor 3 AD - B_adipose   0.0           94735_Donor 3 AD - C_adipose   1.0           77138_Liver_HepG2untreated   0.0           73556_Heart Cardiac stromal cells   0.0           (primary)           81735_Small Intestine   24.5           72409_Kidney_Proximal Convoluted   0.0           Tubule           82685_Small intestine_Duodenum   51.1           90650_Adrenal_Adrenocortical   3.8           adenoma           72410_Kidney_HRCE   0.0           72411_Kidney_HRE   0.0           73139_Uterus_Uterine smooth   0.0           muscle cells                        
     [0855] General_screening_panel_v1.5 Summary: Ag4955 Highest expression of this gene is detected in bladder (CT=26.8). Therefore, expression of this gene may be useful in distinguishing bladder from other samples used in this panel. In addition, therapeutic modulation of this gene may be useful in the treatment of bladder related diseases. Among tissues with metabolic or endocrine function, this gene is expressed at high to moderate levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0856] In addition, this gene is expressed at moderate to low levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0857] Panel 4.1D Summary: Ag4955 Highest expression of this gene is detected in LPS treated monocytes (CT=28.3). In addition, moderate to low levels of expression of this gene is also seen in LAK cells, two way MLRs, PBMC, dendritic cells, activated eosinophils and normal tissues represented by colon, lung, thymus and kidney. This gene encodes splice variant of M130 antigen (CD163) precursor. CD163 is a macrophage-associated antigen belonging to the scavenger receptor cysteine rich (SRCR) domain family and it scavenges haemoglobin by mediating endocytosis of haptoglobin-haemoglobin complexes (Kristiansen, 2001, Nature 409(6817):198-201, PMID: 11196644). CD163 is expressed exclusively on human monocytes and macrophages and it is significantly upregulated by glucocorticoids and IL-10. The highly purified CD163 protein is shown to inhibit phorbol ester-induced human T-lymphocyte activation, thus attenuating the immune response to the inflammatory mediator (Hogger P, Sorg C., 2001, Biochem Biophys Res Commun Nov. 9, 2001;288(4):841-3, PMID: 11688984). Furthermore, macrophages expressing the scavenger receptor CD163 are shown to be increased in synovium and in colonic mucosa in patients with spondyloarthropathy (SpA). Therefore, therapeutic modulation of the CD163 encoded by this gene may be useful in the treatment of asthma, emphysema, inflammatory bowel disease, arthritis, psoriasis and SpA.  
     [0858] Moderate levels of expression of this gene is also seen in liver cirrhosis sample. Therefore, therapeutic modulation of this gene may be beneficial in the treatment of liver cirrhosis.  
     [0859] Panel 5 Islet Summary: Ag4955 Highest expression of this gene is detected in placenta (CT=30.2). In addition, moderate to low levels of expression of this gene is also seen in uterus, skeletal muscle, adipose and small intestine. Please see panel 1.5 for the discussion on utility of this gene.  
     [0860] U. NOV22a (CGI33508-01): Synaptotagmin VI.  
     [0861] Expression of gene CG133508-01 was assessed using the primer-probe set Ag4837, described in Table UA. Results of the RTQ-PCR runs are shown in Tables UB, UC and UD.  
                   TABLE UA                          Probe Name Ag4837                                                         SEQ ID           Primers   Sequences   Length   Start Position   No                                             Forward   5′-ggagagatcatgttctcccttt-3′   22   1147   292                   Probe   TET-5′-caggcaggctcaccctcacagtg-3′-   23   1184   293           TAMRA               Reverse   5′-ccttgaggttccgacacttaat-3′   22   1207   294                  
 
     [0862]               TABLE UB                          CNS_neurodegeneration_v1.0                                 Rel. Exp. (%)               Ag4837, Run           Tissue Name   249271251                                         AD 1 Hippo   4.4           AD 2 Hippo   10.1           AD 3 Hippo   1.8           AD 4 Hippo   4.7           AD 5 Hippo   100.0           AD 6 Hippo   17.8           Control 2 Hippo   9.2           Control 4 Hippo   3.8           Control (Path) 3 Hippo   1.4           AD 1 Temporal Ctx   7.0           AD 2 Temporal Ctx   5.8           AD 3 Temporal Ctx   2.7           AD 4 Temporal Ctx   3.6           AD 5 Inf Temporal Ctx   17.3           AD 5 Sup Temporal Ctx   17.7           AD 6 Inf Temporal Ctx   7.0           AD 6 Sup Temporal Ctx   9.3           Control 1 Temporal Ctx   0.6           Control 2 Temporal Ctx   7.4           Control 3 Temporal Ctx   3.1           Control 3 Temporal Ctx   1.1           Control (Path) 1 Temporal Ctx   8.4           Control (Path) 2 Temporal Ctx   4.5           Control (Path) 3 Temporal Ctx   0.8           Control (Path) 4 Temporal Ctx   2.6           AD 1 Occipital Ctx   16.6           AD 2 Occipital Ctx (Missing)   0.0           AD 3 Occipital Ctx   0.7           AD 4 Occipital Ctx   2.6           AD 5 Occipital Ctx   26.1           AD 6 Occipital Ctx   26.6           Control 1 Occipital Ctx   1.3           Control 2 Occipital Ctx   82.4           Control 3 Occipital Ctx   19.1           Control 4 Occipital Ctx   0.9           Control (Path) 1 Occipital Ctx   34.9           Control (Path) 2 Occipital Ctx   6.0           Control (Path) 3 Occipital Ctx   0.5           Control (Path) 4 Occipital Ctx   28.9           Control 1 Parietal Ctx   1.0           Control 2 Parietal Ctx   6.2           Control 3 Parietal Ctx   5.1           Control (Path) 1 Parietal Ctx   11.9           Control (Path) 2 Parietal Ctx   4.5           Control (Path) 3 Parietal Ctx   0.8           Control (Path) 4 Parietal Ctx   10.9                        
     [0863]               TABLE UC                          General_screening_panel_v1.5                                 Rel. Exp. (%)               Ag4837, Run           Tissue Name   228787809                                         Adipose   0.2           Melanoma* Hs688(A).T   0.0           Melanoma* Hs688(B).T   0.0           Melanoma* M14   0.8           Melanoma* LOXIMVI   0.0           Melanoma* SK-MEL-5   0.1           Squamous cell carcinoma SCC-4   0.0           Testis Pool   2.9           Prostate ca.* (bone met) PC-3   0.0           Prostate Pool   1.5           Placenta   0.6           Uterus Pool   0.0           Ovarian ca. OVCAR-3   0.0           Ovarian ca. SK-OV-3   0.0           Ovarian ca. OVCAR-4   0.0           Ovarian ca. OVCAR-5   0.0           Ovarian ca. IGROV-1   0.0           Ovarian ca. OVCAR-8   0.4           Ovary   9.0           Breast ca. MCF-7   0.0           Breast ca. MDA-MB-231   0.0           Breast ca. BT 549   0.0           Breast ca. T47D   0.0           Breast ca. MDA-N   0.0           Breast Pool   0.5           Trachea   0.8           Lung   2.9           Fetal Lung   5.5           Lung ca. NCI-N417   2.4           Lung ca. LX-1   0.0           Lung ca. NCI-H146   0.0           Lung ca. SHP-77   0.0           Lung ca. A549   1.4           Lung ca. NCI-H526   51.1           Lung ca. NCI-H23   0.3           Lung ca. NCI-H460   0.0           Lung ca. HOP-62   0.0           Lung ca. NCI-H522   0.0           Liver   0.0           Fetal Liver   0.6           Liver ca. HepG2   0.0           Kidney Pool   0.4           Fetal Kidney   5.6           Renal ca. 786-0   0.0           Renal ca. A498   0.0           Renal ca. ACHN   0.0           Renal ca. UO-31   0.0           Renal ca. TK-10   0.0           Bladder   5.1           Gastric ca. (liver met.) NCI-N87   0.0           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.0           Colon ca. SW480   0.4           Colon ca.* (SW480 met) SW620   0.0           Colon ca. HT29   0.0           Colon ca. HCT-116   0.0           Colon ca. CaCo-2   1.0           Colon cancer tissue   0.1           Colon ca. SW1116   0.0           Colon ca. Colo-205   0.0           Colon ca. SW-48   0.0           Colon Pool   0.4           Small Intestine Pool   0.3           Stomach Pool   0.7           Bone Marrow Pool   0.3           Fetal Heart   0.1           Heart Pool   0.0           Lymph Node Pool   0.2           Fetal Skeletal Muscle   3.3           Skeletal Muscle Pool   3.6           Spleen Pool   0.4           Thymus Pool   0.5           CNS cancer (glio/astro) U87-MG   0.4           CNS cancer (glio/astro) U-118-MG   0.0           CNS cancer (neuro; met) SK-N-AS   0.0           CNS cancer (astro) SF-539   0.0           CNS cancer (astro) SNB-75   0.0           CNS cancer (glio) SNB-19   0.0           CNS cancer (glio) SF-295   0.0           Brain (Amygdala) Pool   10.2           Brain (cerebellum)   6.2           Brain (fetal)   100.0           Brain (Hippocampus) Pool   12.6           Cerebral Cortex Pool   12.1           Brain (Substantia nigra) Pool   14.2           Brain (Thalamus) Pool   15.0           Brain (whole)   22.5           Spinal Cord Pool   13.0           Adrenal Gland   0.8           Pituitary gland Pool   0.4           Salivary Gland   0.4           Thyroid (female)   0.0           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   1.2                        
     [0864]               TABLE UD                          Panel 4.1D                                 Rel. Exp. (%)               Ag4837, Run           Tissue Name   223335536                                         Secondary Th1 act   0.0           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.6           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.0           Primary Th1 rest   0.0           Primary Th2 rest   0.0           Primary Tr1 rest   1.1           CD45RA CD4 lymphocyte act   0.0           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.5           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   0.0           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.4           LAK cells rest   0.0           LAK cells IL-2   0.0           LAK cells IL-2 + IL-12   0.5           LAK cells IL-2 + IFN gamma   0.0           LAK cells IL-2 + IL-18   0.0           LAK cells PMA/ionomycin   8.2           NK Cells IL-2 rest   0.0           Two Way MLR 3 day   0.0           Two Way MLR 5 day   0.8           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   0.0           PBMC PHA-L   0.0           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.0           B lymphocytes CD40L and IL-4   0.0           EOL-1 dbcAMP   0.0           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   3.0           Dendritic cells LPS   0.0           Dendritic cells anti-CD40   0.7           Monocytes rest   0.0           Monocytes LPS   0.0           Macrophages rest   0.4           Macrophages LPS   0.0           HUVEC none   0.0           HUVEC starved   0.0           HUVEC IL-1beta   0.0           HUVEC IFN gamma   0.0           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.0           Lung Microvascular EC none   0.0           Lung Microvascular EC TNFalpha +   0.0           IL-1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   0.0           IL1beta           Small airway epithelium none   0.0           Small airway epithelium TNFalpha +   0.0           IL-1beta           Coronery artery SMC rest   0.0           Coronery artery SMC TNFalpha + IL-   0.0           1beta           Astrocytes rest   1.6           Astrocytes TNFalpha + IL-1beta   0.0           KU-812 (Basophil) rest   0.0           KU-812 (Basophil) PMA/ionomycin   0.0           CCD1106 (Keratinocytes) none   1.6           CCD1106 (Keratinocytes) TNFalpha +   0.0           IL-1beta           Liver cirrhosis   0.0           NCI-H292 none   0.0           NCI-H292 IL-4   0.0           NCI-H292 IL-9   0.0           NCI-H292 IL-13   0.0           NCI-H292 IFN gamma   0.0           HPAEC none   0.0           HPAEC TNF alpha + IL-1 beta   0.0           Lung fibroblast none   0.0           Lung fibroblast TNF alpha + IL-1   0.0           beta           Lung fibroblast IL-4   0.0           Lung fibroblast IL-9   0.0           Lung fibroblast IL-13   0.5           Lung fibroblast IFN gamma   0.0           Dermal fibroblast CCD1070 rest   0.0           Dermal fibroblast CCD1070 TNF alpha   0.0           Dermal fibroblast CCD1070 IL-1 beta   0.0           Dermal fibroblast IFN gamma   0.4           Dermal fibroblast IL-4   0.0           Dermal Fibroblasts rest   1.9           Neutrophils TNFa + LPS   0.0           Neutrophils rest   1.1           Colon   6.0           Lung   4.3           Thymus   14.1           Kidney   100.0                        
     [0865] CNS_neurodegeneration_v1.0 Summary: Ag4837 Expression of this gene is ubiquitous throughout the samples in this panel, with highest expression in the hippocampus of a patient with Alzheimer&#39;s disease (CT=28). While no association between the expression of this gene and the presence of Alzheimer&#39;s disease is detected in this panel, these results confirm the expression of this gene in areas that degenerate in Alzheimer&#39;s disease, including the cortex, hippocampus, amygdala and thalamus. Synaptotagmin expression is altered in the brain of Alzheimer&#39;s patients, possibly explaining impaired synaptogenesis and/or synaptosomal loss secondary to neuronal loss observed in the neurodegenerative disorder. It may also represent, reflect or account for the impaired neuronal transmission in Alzheimer&#39;s disease (AD), caused by deterioration of the exocytic machinery. Since this gene is a homolog of synaptotagmin, agents that potentiate the expression or function of the protein encoded by this gene may be useful in the treatment of Alzheimer&#39;s disease.  
     [0866] References:  
     [0867] Sze C I, Bi H, Kleinschmidt-DeMasters B K, Filley C M, Martin L J. (2000) J Neurol Sci. 175:81-90.  
     [0868] Masliah F, Mallory M, Alford M, DeTeresa R, Hansen L A, McKeel D W Jr, Morris J C. (2001)Neurology 56:127-9.  
     [0869] Yoo B C, Cairns N, Fountoulakis M, Lubec G. (2001) Dement Geriatr Cogn Disord. 12:219-25.  
     [0870] General_screening_panel_v1.5 Summary: Ag4837 This gene encodes a homolog of synaptotagmin which appears to be almost exclusively expressed in the brain. This experiment shows moderate to high expression across all brain regions with highest expression in the fetal brain (CT=28.3). Synaptotagmin is a presynaptic protein involved in synaptic vesicle release, making this an ideal drug target for diseases such as epilepsy, in which reduction of neurotransmission is beneficial. Selective inhibition of this gene or its protein product may therefore be useful in the treatment of seizure disorders. Furthermore, selective inhibition of neural transmission through antagonism of the protein encoded by this gene may show therapeutic benefit in psychiatric diseases where it is believed that inappropriate neural connections have been established, such as schizophrenia and bipolar disorder. In addition, antibodies against synaptotagmin may cause Lambert-Eaton myasthenic syndrome. Therefore, peptide fragments of the protein encoded by this gene may serve to block the action of these antibodies and treat Lambert-Eaton myasthenic syndrome.  
     [0871] References:  
     [0872] Takamori M, Komai K, Iwasa K. (2000) Am J Med Sci. 319:204-8.  
     [0873] Sokolov B P, Tcherepanov A A, Haroutunian V, Davis K L. (2000) Biol Psychiatry. 48:184-96.  
     [0874] Panel 4.1D Summary: Ag4837 This gene is expressed at detectable levels in the kidney (CT=29.8). Thus, expression of this gene could be used to differentiate the kidney derived sample from other samples on this panel and as a marker of kidney tissue. In addition, therapeutic targeting of the expression or function of this gene may modulate kidney function and be important in the treatment of inflammatory or autoimmune diseases that affect the kidney, including lupus and glomerulonephritis.  
     [0875] V. NOV23a and NOV23b (CG133548-01 and CG133548-02): 1300003P13RIK Protein Homolog (TmMP)  
     [0876] Expression of gene CG133548-01 and CG133548-02 was assessed using the primer-probe set Ag4839, described in Table VA. Results of the RTQ-PCR runs are shown in Tables VB and VC.  
                   TABLE VA                          Probe Name Ag4839                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-ttccaatgttctttggttttgt-3′   22   1216   295                   Probe   TET-5′-tctgctgctcttatggccaggtttct-3′-   26   1250   296           TAMRA               Reverse   5′-gaaactcgaagtcctcaaatcc-3′   22   1293   297                  
 
     [0877]               TABLE VB                          General_screening_panel_v1.5                                 Rel. Exp. (%)               Ag4839, Run           Tissue Name   228787839                                         Adipose   3.3           Melanoma* Hs688(A).T   21.8           Melanoma* Hs688(B).T   26.2           Melanoma* M14   13.9           Melanoma* LOXIMVI   9.0           Melanoma* SK-MEL-5   44.4           Squamous cell carcinoma SCC-4   6.8           Testis Pool   5.6           Prostate ca.* (bone met) PC-3   8.1           Prostate Pool   8.8           Placenta   3.0           Uterus Pool   4.5           Ovarian ca. OVCAR-3   100.0           Ovarian ca. SK-OV-3   34.2           Ovarian ca. OVCAR-4   14.3           Ovarian ca. OVCAR-5   46.7           Ovarian ca. IGROV-1   14.6           Ovarian ca. OVCAR-8   9.2           Ovary   8.6           Breast ca. MCF-7   21.5           Breast ca. MDA-MB-231   25.2           Breast ca. BT 549   10.5           Breast ca. T47D   4.7           Breast ca. MDA-N   16.3           Breast Pool   7.6           Trachea   10.5           Lung   4.4           Fetal Lung   18.7           Lung ca. NCI-N417   1.9           Lung ca. LX-1   20.3           Lung ca. NCI-H146   4.5           Lung ca. SHP-77   14.8           Lung ca. A549   27.4           Lung ca. NCI-H526   2.6           Lung ca. NCI-H23   33.2           Lung ca. NCI-H460   19.2           Lung ca. HOP-62   12.0           Lung ca. NCI-H522   18.3           Liver   0.8           Fetal Liver   16.3           Liver ca. HepG2   29.1           Kidney Pool   0.0           Fetal Kidney   12.6           Renal ca. 786-0   27.0           Renal ca. A498   5.6           Renal ca. ACHN   49.7           Renal ca. UO-31   33.9           Renal ca. TK-10   32.3           Bladder   20.6           Gastric ca. (liver met.) NCI-N87   33.7           Gastric ca. KATO III   17.6           Colon ca. SW-948   5.1           Colon ca. SW480   39.2           Colon ca.* (SW480 met) SW620   14.9           Colon ca. HT29   6.5           Colon ca. HCT-116   5.5           Colon ca. CaCo-2   39.2           Colon cancer tissue   20.0           Colon ca. SW1116   1.4           Colon ca. Colo-205   2.5           Colon ca. SW-48   4.9           Colon Pool   5.5           Small Intestine Pool   8.3           Stomach Pool   7.5           Bone Marrow Pool   3.5           Fetal Heart   4.7           Heart Pool   3.8           Lymph Node Pool   10.0           Fetal Skeletal Muscle   3.6           Skeletal Muscle Pool   16.4           Spleen Pool   7.2           Thymus Pool   5.6           CNS cancer (glio/astro) U87-MG   21.6           CNS cancer (glio/astro) U-118-MG   25.2           CNS cancer (neuro; met) SK-N-AS   12.2           CNS cancer (astro) SF-539   8.5           CNS cancer (astro) SNB-75   17.6           CNS cancer (glio) SNB-19   15.4           CNS cancer (glio) SF-295   37.4           Brain (Amygdala) Pool   3.4           Brain (cerebellum)   13.5           Brain (fetal)   7.9           Brain (Hippocampus) Pool   3.7           Cerebral Cortex Pool   3.4           Brain (Substantia nigra) Pool   2.6           Brain (Thalamus) Pool   5.1           Brain (whole)   2.7           Spinal Cord Pool   3.4           Adrenal Gland   21.8           Pituitary gland Pool   2.1           Salivary Gland   5.7           Thyroid (female)   5.9           Pancreatic ca. CAPAN2   17.7           Pancreas Pool   12.2                        
     [0878]               TABLE VC                          Panel 4.1D                                 Rel. Exp. (%)               Ag4839, Run           Tissue Name   223335453                                         Secondary Th1 act   54.0           Secondary Th2 act   56.6           Secondary Tr1 act   23.0           Secondary Th1 rest   11.7           Secondary Th2 rest   12.9           Secondary Tr1 rest   18.4           Primary Th1 act   32.3           Primary Th2 act   37.1           Primary Tr1 act   40.9           Primary Th1 rest   13.3           Primary Th2 rest   13.5           Primary Tr1 rest   24.8           CD45RA CD4 lymphocyte act   54.7           CD45RO CD4 lymphocyte act   34.9           CD8 lymphocyte act   34.2           Secondary CD8 lymphocyte rest   26.8           Secondary CD8 lymphocyte act   20.4           CD4 lymphocyte none   8.1           2ry Th1/Th2/Tr1_anti-CD95 CH11   26.1           LAK cells rest   48.3           LAK cells IL-2   27.2           LAK cells IL-2 + IL-12   30.8           LAK cells IL-2 + IFN gamma   27.4           LAK cells IL-2 + IL-18   42.6           LAK cells PMA/ionomycin   43.8           NK Cells IL-2 rest   36.6           Two Way MLR 3 day   36.6           Two Way MLR 5 day   29.7           Two Way MLR 7 day   31.0           PBMC rest   7.3           PBMC PWM   27.4           PBMC PHA-L   29.1           Ramos (B cell) none   50.3           Ramos (B cell) ionomycin   53.2           B lymphocytes PWM   27.5           B lymphocytes CD40L and IL-4   33.0           EOL-1 dbcAMP   33.7           EOL-1 dbcAMP PMA/ionomycin   50.3           Dendritic cells none   64.6           Dendritic cells LPS   55.1           Dendritic cells anti-CD40   49.0           Monocytes rest   29.7           Monocytes LPS   76.8           Macrophages rest   60.3           Macrophages LPS   44.8           HUVEC none   30.1           HUVEC starved   47.6           HUVEC IL-1beta   55.1           HUVEC IFN gamma   45.7           HUVEC TNF alpha + IFN gamma   33.4           HUVEC TNF alpha + IL4   44.4           HUVEC IL-11   22.1           Lung Microvascular EC none   100.0           Lung Microvascular EC TNFalpha +   85.9           IL-1beta           Microvascular Dermal EC none   53.6           Microsvasular Dermal EC   41.2           TNFalpha + IL-1beta           Bronchial epithelium TNFalpha +   59.0           IL1beta           Small airway epithelium none   32.8           Small airway epithelium   60.7           TNFalpha + IL-1beta           Coronery artery SMC rest   37.1           Coronery artery SMC TNFalpha +   25.5           IL-1beta           Astrocytes rest   51.4           Astrocytes TNFalpha + IL-1beta   61.1           KU-8l2 (Basophil) rest   12.2           KU-812 (Basophil) PMA/ionomycin   33.2           CCD1106 (Keratinocytes) none   53.2           CCD1106 (Keratinocytes)   37.4           TNFalpha + IL-1beta           Liver cirrhosis   14.6           NCI-H292 none   40.6           NCI-H292 IL-4   69.3           NCI-H292 IL-9   75.8           NCI-H292 IL-13   56.3           NCI-H292 IFN gamma   55.1           HPAEC none   28.3           HPAEC TNF alpha + IL-1 beta   61.1           Lung fibroblast none   62.0           Lung fibroblast TNF alpha +   56.6           IL-1 beta           Lung fibroblast IL-4   82.4           Lung fibroblast IL-9   95.9           Lung fibroblast IL-13   62.9           Lung fibroblast IFN gamma   0.0           Dermal fibroblast CCD1070 rest   80.7           Dermal fibroblast CCD1070 TNF   81.8           alpha           Dermal fibroblast CCD 1070 IL-1   42.6           beta           Dermal fibroblast IFN gamma   51.8           Dermal fibroblast IL-4   96.6           Dermal Fibroblasts rest   58.2           Neutrophils TNFa + LPS   8.1           Neutrophils rest   16.8           Colon   32.1           Lung   22.5           Thymus   55.1           Kidney   64.6                        
     [0879] General_screening_panel_v1.5 Summary: Ag4839 Highest expression of the CG133548-01 gene is detected in ovarian cancer OVCAR-3 cell line (CT=24.8). High to moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.  
     [0880] Among tissues with metabolic or endocrine function, this gene is expressed at high to moderate levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0881] In addition, this gene is expressed at high to moderate levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0882] Interestingly, this gene is expressed at much higher levels in fetal (CT=27.8) when compared to adult kidney (CT=40). This observation suggests that expression of this gene can be used to distinguish fetal from adult kidney. In addition, the relative overexpression of this gene in fetal kidney suggests that the protein product may enhance kidney growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of kidney related diseases.  
     [0883] Panel 4.1D Summary: Ag4839 Highest expression of the CG133548-01 gene is detected in lung microvascular EC (CT=27.4). This gene is expressed at high to moderate levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This pattern is in agreement with the expression profile in General_screening_panel_v1.5 and also suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.  
     [0884] W. NOV24a and NOV24b (CG133569-01 and CG133569-02): Type I Membrane Protein with SH3 Domain  
     [0885] Expression of gene CG133569-01 and CG133569-02 was assessed using the primer-probe set Ag4843, described in Table WA. Results of the RTQ-PCR runs are shown in Tables WB and WC.  
                   TABLE WA                          Probe Name Ag4843                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-gagcaatggaagagatgcaa-3′   20   3170   298                   Probe   TET-5′-ccactgcatgaagataatttctcacga-3′-   27   3190   299           TAMRA               Reverse   5′-cttcaggaacctgcacattaag-3′   22   3232   300                  
 
     [0886]               TABLE WB                          General_screening_panel_v1.5                                 Rel. Exp. (%)               Ag4843, Run           Tissue Name   228796268                                         Adipose   18.7           Melanoma* Hs688(A).T   36.9           Melanoma* Hs688(B).T   42.0           Melanoma* M14   17.2           Melanoma* LOXIMVI   10.5           Melanoma* SK-MEL-5   25.0           Squamous cell carcinoma SCC-4   16.4           Testis Pool   22.7           Prostate ca.* (bone met) PC-3   80.7           Prostate Pool   44.1           Placenta   2.8           Uterus Pool   29.5           Ovarian ca. OVCAR-3   18.4           Ovarian ca. SK-OV-3   16.5           Ovarian ca. OVCAR-4   2.1           Ovarian ca. OVCAR-5   27.9           Ovarian ca. IGROV-1   17.0           Ovarian ca. OVCAR-8   10.4           Ovary   12.3           Breast ca. MCF-7   25.0           Breast ca. MDA-MB-231   35.1           Breast ca. BT 549   63.3           Breast ca. T47D   14.8           Breast ca. MDA-N   6.0           Breast Pool   27.7           Trachea   18.8           Lung   7.6           Fetal Lung   32.1           Lung ca. NCI-N417   4.5           Lung ca. LX-1   21.3           Lung ca. NCI-H146   8.8           Lung ca. SHP-77   46.0           Lung ca. A549   21.3           Lung ca. NCI-H526   1.9           Lung ca. NCI-H23   25.3           Lung ca. NCI-H460   31.9           Lung ca. HOP-62   15.8           Lung ca. NCI-H522   31.6           Liver   2.9           Fetal Liver   25.9           Liver ca. HepG2   13.7           Kidney Pool   41.2           Fetal Kidney   17.4           Renal ca. 786-0   23.8           Renal ca. A498   11.7           Renal ca. ACHN   11.7           Renal ca. UO-31   12.5           Renal ca. TK-10   34.2           Bladder   32.8           Gastric ca. (liver met.) NCI-N87   28.5           Gastric ca. KATO III   45.7           Colon ca. SW-948   5.9           Colon ca. SW480   14.8           Colon ca.* (SW480 met) SW620   18.0           Colon ca. HT29   18.8           Colon ca. HCT-116   21.6           Colon ca. CaCo-2   23.3           Colon cancer tissue   11.2           Colon ca. SW1116   3.1           Colon ca. Colo-205   2.9           Colon ca. SW-48   2.5           Colon Pool   26.8           Small Intestine Pool   19.9           Stomach Pool   15.3           Bone Marrow Pool   11.8           Fetal Heart   15.6           Heart Pool   9.5           Lymph Node Pool   29.5           Fetal Skeletal Muscle   5.6           Skeletal Muscle Pool   24.3           Spleen Pool   11.3           Thymus Pool   18.8           CNS cancer (glio/astro) U87-MG   37.1           CNS cancer (glio/astro) U-118-MG   47.6           CNS cancer (neuro; met) SK-N-AS   47.3           CNS cancer (astro) SF-539   19.1           CNS cancer (astro) SNB-75   100.0           CNS cancer (glio) SNB-19   15.3           CNS cancer (glio) SF-295   92.7           Brain (Amygdala) Pool   l3.4           Brain (cerebellum)   30.8           Brain (fetal)   19.1           Brain (Hippocampus) Pool   16.5           Cerebral Cortex Pool   21.6           Brain (Substantia nigra) Pool   10.8           Brain (Thalamus) Pool   22.2           Brain (whole)   9.2           Spinal Cord Pool   7.7           Adrenal Gland   8.5           Pituitary gland Pool   8.3           Salivary Gland   5.6           Thyroid (female)   5.1           Pancreatic ca. CAPAN2   6.9           Pancreas Pool   26.1                        
     [0887]               TABLE WC                          Panel 4.1D                                 Rel. Exp. (%)               Ag4843, Run           Tissue Name   223335454                                         Secondary Th1 act   31.6           Secondary Th2 act   30.8           Secondary Tr1 act   27.5           Secondary Th1 rest   15.8           Secondary Th2 rest   22.2           Secondary Tr1 rest   23.3           Primary Th1 act   23.2           Primary Th2 act   35.4           Primary Tr1 act   28.9           Primary Th1 rest   14.4           Primary Th2 rest   19.6           Primary Tr1 rest   38.4           CD45RA CD4 lymphocyte act   47.0           CD45RO CD4 lymphocyte act   41.8           CD8 lymphocyte act   49.0           Secondary CD8 lymphocyte rest   27.7           Secondary CD8 lymphocyte act   19.5           CD4 lymphocyte none   32.3           2ry Th1/Th2/Tr1_anti-CD95 CH11   24.8           LAK cells rest   36.1           LAK cells IL-2   35.6           LAK cells IL-2 + IL-12   23.0           LAK cells IL-2 + IFN gamma   40.6           LAK cells IL-2 + IL-18   44.8           LAK cells PMA/ionomycin   20.3           NK Cells IL-2 rest   42.3           Two Way MLR 3 day   54.0           Two Way MLR 5 day   25.5           Two Way MLR 7 day   24.5           PBMC rest   25.7           PBMC PWM   23.8           PBMC PHA-L   26.8           Ramos (B cell) none   59.0           Ramos (B cell) ionomycin   52.9           B lymphocytes PWM   37.1           B lymphocytes CD40L and IL-4   32.8           EOL-1 dbcAMP   34.6           EOL-1 dbcAMP PMA/ionomycin   17.4           Dendritic cells none   28.3           Dendritic cells LPS   20.6           Dendritic cells anti-CD40   37.4           Monocytes rest   48.3           Monocytes LPS   44.8           Macrophages rest   24.5           Macrophages LPS   10.7           HUVEC none   35.1           HUVEC starved   38.2           HUVEC IL-1beta   50.3           HUVEC IFN gamma   49.3           HUVEC TNF alpha + IFN gamma   31.0           HUVEC TNF alpha + IL4   46.7           HUVEC IL-11   36.9           Lung Microvascular EC none   66.0           Lung Microvascular EC TNFalpha +   56.6           IL-1beta           Microvascular Dermal EC none   54.7           Microsvasular Dermal EC TNFalpha +   37.4           IL-1beta           Bronchial epithelium TNFalpha +   48.6           IL1beta           Small airway epithelium none   11.6           Small airway epithelium TNFalpha +   20.0           IL-1beta           Coronery artery SMC rest   42.9           Coronery artery SMC TNFalpha + IL-   46.0           1beta           Astrocytes rest   28.5           Astrocytes TNFalpha + IL-1beta   13.5           KU-812 (Basophil) rest   49.7           KU-812 (Basophil) PMA/ionomycin   100.0           CCD1106 (Keratinocytes) none   20.7           CCD1106 (Keratinocytes) TNFalpha +   22.2           IL-1beta           Liver cirrhosis   28.9           NCI-H292 none   25.7           NCI-H292 IL-4   39.0           NCI-H292 IL-9   44.8           NCI-H292 IL-13   41.5           NCI-H292 IFN gamma   38.4           HPAEC none   40.6           HPAEC TNF alpha + IL-1 beta   72.2           Lung fibroblast none   88.3           Lung fibroblast TNF alpha + IL-1   88.3           beta           Lung fibroblast IL-4   50.7           Lung fibroblast IL-9   84.1           Lung fibroblast IL-13   47.0           Lung fibroblast IFN gamma   37.9           Dermal fibroblast CCD1070 rest   51.8           Dermal fibroblast CCD1070 TNF alpha   69.7           Dermal fibroblast CCD1070 IL-1 beta   59.9           Dermal fibroblast IFN gamma   42.9           Dermal fibroblast IL-4   75.8           Dermal Fibroblasts rest   66.9           Neutrophils TNFa + LPS   8.1           Neutrophils rest   23.8           Colon   22.7           Lung   38.2           Thymus   41.8           Kidney   35.8                        
     [0888] General_screening_panel_v1.5 Summary: Ag4843 Highest expression of the CG133569-01 gene is detected in CNS cancer SNB-75 cell line (CT=26). High levels of expression of this gene is also seen in cluster of cancer cell lines derived from pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of pancreatic, gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.  
     [0889] Among tissues with metabolic or endocrine function, this gene is expressed at moderate to high levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0890] In addition, this gene is expressed at high levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0891] Panel 4.1D Summary: Ag4843 Highest expression of the CG133569-01 gene is detected in PMA/ionomycin treated basophils (CT=29). This gene is expressed at high to moderate levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This pattern is in agreement with the expression profile in General_screening_panel v1.5 and also suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.  
     [0892] X. NOV26a and NOV26b (CG134100-01 and CG134100-02): Amidase — 2 Domain Protein  
     [0893] Expression of gene CG134100-01 and CG134100-02 was assessed using the primer-probe sets Ag44387, Ag4893 and Ag4894, described in Tables XA, XB and XC. Results of the RTQ-PCR runs are shown in Tables XD, XE, XF and XG.  
                   TABLE XA                          Probe Name Ag4387                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-tgtatccacagactgccagact-3′   22   753   301                   Probe   TET-5′-tcgtccgaaacatacagtcctttcaca-3′-   27   776   302           TAMRA               Reverse   5′-atgtcacaaaagttccgtgtgt-3′   22   806   303                  
 
     [0894]                   TABLE XB                          Probe Name Ag4893                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-aacatcatcaaacgatctgctt-3′   22   646   304                   Probe   TET-5′-cacactgccctaaaatgaacctccca-3′-   26   683   305           TAMRA               Reverse   5′-tggatgatgatgacatatttgg-3′   22   710   306                    
     [0895]                   TABLE XC                          Probe Name Ag4894                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-aacatcatcaaacgatctgctt-3′   22   646   307                   Probe   TET-5′-cacactgccctaaaatgaacctccca-3′-   26   683   308           TAMRA               Reverse   5′-tggatgatgatgacatatttgg-3′   22   710   309                    
     [0896]               TABLE XD                          General_screening_panel_v1.4                                 Rel. Exp. (%)               Ag4387, Run           Tissue Name   222567011                                         Adipose   0.5           Melanoma* Hs688(A).T   0.0           Melanoma* Hs688(B).T   0.0           Melanoma* M14   0.0           Melanoma* LOXIMVI   0.0           Melanoma* SK-MEL-5   0.0           Squamous cell carcinoma SCC-4   4.4           Testis Pool   1.8           Prostate ca.* (bone met) PC-3   0.0           Prostate Pool   0.0           Placenta   0.0           Uterus Pool   15.9           Ovarian ca. OVCAR-3   2.8           Ovarian ca. SK-OV-3   0.0           Ovarian ca. OVCAR-4   0.0           Ovarian ca. OVCAR-5   0.4           Ovarian ca. IGROV-1   0.0           Ovarian ca. OVCAR-8   0.0           Ovary   0.0           Breast ca. MCF-7   1.1           Breast ca. MDA-MB-231   0.0           Breast ca. BT 549   0.0           Breast ca. T47D   0.7           Breast ca. MDA-N   0.0           Breast Pool   0.0           Trachea   10.1           Lung   0.0           Fetal Lung   0.4           Lung ca. NCI-N417   0.0           Lung ca. LX-1   0.0           Lung ca. NCI-H146   0.0           Lung ca. SHP-77   0.0           Lung ca. A549   1.7           Lung ca. NCI-H526   0.0           Lung ca. NCI-H23   1.5           Lung ca. NCI-H460   0.0           Lung ca. HOP-62   0.0           Lung ca. NCI-H522   0.0           Liver   0.0           Fetal Liver   0.0           Liver ca. HepG2   0.0           Kidney Pool   0.7           Fetal Kidney   0.0           Renal ca. 786-0   0.5           Renal ca. A498   0.0           Renal ca. ACHN   0.0           Renal ca. UO-31   0.0           Renal ca. TK-10   0.0           Bladder   7.8           Gastric ca. (liver met.) NCI-N87   4.6           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.0           Colon ca. SW480   0.0           Colon ca* (SW480 met) SW620   0.0           Colon ca. HT29   0.0           Colon ca. HCT-116   1.2           Colon ca. CaCo-2   0.0           Colon cancer tissue   0.0           Colon ca. SW1116   0.0           Colon ca. Colo-205   0.0           Colon ca. SW-48   0.0           Colon Pool   0.0           Small Intestine Pool   0.0           Stomach Pool   0.0           Bone Marrow Pool   100.0           Fetal Heart   0.0           Heart Pool   0.0           Lymph Node Pool   0.0           Fetal Skeletal Muscle   0.0           Skeletal Muscle Pool   0.0           Spleen Pool   0.0           Thymus Pool   1.3           CNS cancer (glio/astro) U87-MG   0.0           CNS cancer (glio/astro) U-118-MG   0.6           CNS cancer (neuro; met) SK-N-AS   0.0           CNS cancer (astro) SF-539   0.0           CNS cancer (astro) SNB-75   0.0           CNS cancer (glio) SNB-19   0.0           CNS cancer (glio) SF-295   0.0           Brain (Amygdala) Pool   0.5           Brain (cerebellum)   0.0           Brain (fetal)   0.0           Brain (Hippocampus) Pool   0.0           Cerebral Cortex Pool   0.0           Brain (Substantia nigra) Pool   0.0           Brain (Thalamus) Pool   0.0           Brain (whole)   0.0           Spinal Cord Pool   0.0           Adrenal Gland   0.0           Pituitary gland Pool   0.0           Salivary Gland   2.4           Thyroid (female)   0.0           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   0.0                        
     [0897]               TABLE XE                          General_screening_panel_v1.5                             Rel. Exp. (%)   Rel. Exp. (%)           Ag4893, Run   Ag4894, Run       Tissue Name   228829406   228829491                                 Adipose   0.0   1.0       Melanoma* Hs688(A).T   0.0   0.0       Melanoma* Hs688(B).T   0.0   0.0       Melanoma* M14   0.0   0.0       Melanoma* LOXIMVI   0.0   0.0       Melanoma* SK-MEL-5   0.0   0.0       Squamous cell carcinoma SCC-4   7.6   11.4       Testis Pool   0.0   2.5       Prostate ca.* (bone met) PC-3   0.0   0.0       Prostate Pool   0.0   0.0       Placenta   0.0   1.9       Uterus Pool   43.2   48.6       Ovarian ca. OVCAR-3   3.7   2.8       Ovarian ca. SK-OV-3   0.0   0.0       Ovarian ca. OVCAR-4   0.0   0.0       Ovarian ca. OVCAR-5   0.0   0.8       Ovarian ca. IGROV-1   0.0   0.0       Ovarian ca. OVCAR-8   0.0   0.0       Ovary   0.0   0.5       Breast ca. MCF-7   0.0   0.0       Breast ca. MDA-MB-231   0.0   0.0       Breast ca. BT 549   0.0   0.0       Breast ca. T47D   0.0   0.0       Breast ca. MDA-N   0.0   0.0       Breast Pool   0.0   0.5       Trachea   15.4   14.6       Lung   0.0   0.0       Fetal Lung   3.6   1.1       Lung ca. NCI-N417   0.0   0.0       Lung ca. LX-1   0.0   0.0       Lung ca. NCI-H146   0.0   0.0       Lung ca. SHP-77   0.0   0.0       Lung ca. A549   0.0   0.0       Lung ca. NCI-H526   0.0   0.0       Lung ca. NCI-H23   0.0   0.0       Lung ca. NCI-H460   0.0   0.0       Lung ca. HOP-62   0.0   0.0       Lung ca. NCI-H522   0.0   0.0       Liver   0.0   0.0       Fetal Liver   0.0   0.0       Liver ca. HepG2   0.0   0.0       Kidney Pool   0.0   0.8       Fetal Kidney   0.0   0.0       Renal ca. 786-0   0.0   0.0       Renal ca. A498   0.0   0.0       Renal ca. ACHN   0.0   0.0       Renal ca. UO-31   0.0   0.0       Renal ca. TK-10   0.0   0.0       Bladder   9.2   5.7       Gastric ca. (liver-met.) NCI-N87   7.9   8.0       Gastric ca. KATO III   0.0   0.0       Colon ca. SW-948   0.0   1.7       Colon ca. SW480   0.0   0.0       Colon ca.* (SW480 met) SW620   0.0   0.0       Colon ca. HT29   0.0   0.0       Colon ca. HCT-116   0.0   0.0       Colon ca. CaCo-2   0.0   0.0       Colon cancer tissue   0.0   0.0       Colon ca. SW1116   0.0   0.0       Colon ca. Colo-205   0.0   0.0       Colon ca. SW-48   0.0   0.7       Colon Pool   0.0   0.0       Small Intestine Pool   0.0   0.0       Stomach Pool   0.0   0.0       Bone Marrow Pool   100.0   100.0       Fetal Heart   0.0   0.0       Heart Pool   0.0   0.9       Lymph Node Pool   0.0   0.0       Fetal Skeletal Muscle   0.0   0.0       Skeletal Muscle Pool   0.0   0.0       Spleen Pool   0.0   0.0       Thymus Pool   2.0   1.7       CNS cancer (glio/astro) U87-MG   0.0   0.0       CNS cancer (glio/astro) U-118-MG   0.0   0.0       CNS cancer (neuro; met) SK-N-AS   0.0   0.0       CNS cancer (astro) SF-539   0.0   0.0       CNS cancer (astro) SNB-75   0.0   0.0       CNS cancer (glio) SNB-19   0.0   0.0       CNS cancer (glio) SF-295   0.0   0.0       Brain (Amygdala) Pool   0.0   0.0       Brain (cerebellum)   0.0   0.7       Brain (fetal)   0.0   1.7       Brain (Hippocampus) Pool   0.0   0.0       Cerebral Cortex Pool   0.0   0.0       Brain (Substantia nigra) Pool   0.0   0.0       Brain (Thalamus) Pool   0.0   0.0       Brain (whole)   0.0   0.0       Spinal Cord Pool   0.0   0.6       Adrenal Gland   0.0   0.0       Pituitary gland Pool   0.0   0.0       Salivary Gland   3.0   1.7       Thyroid (female)   0.0   0.0       Pancreatic ca. CAPAN2   0.0   0.0       Pancreas Pool   0.0   0.0                    
     [0898]               TABLE XF                          Oncology_cell_line_screening_panel_v3.1                         Rel. Exp. (%)           Ag4893, Run       Tissue Name   225052585                             Daoy Medulloblastoma/Cerebellum   0.0       TE671 Medulloblastom/Cerebellum   0.0       D283 Med Medulloblastoma/Cerebellum   0.0       PFSK-1 Primitive Neuroectodermal/Cerebellum   0.0       XF-498_CNS   0.0       SNB-78_CNS/glioma   0.6       SF-268_CNS/glioblastoma   0.0       T98G_Glioblastoma   0.0       SK-N-SH_Neuroblastoma (metastasis)   0.0       SF-295_CNS/glioblastoma   0.0       Cerebellum   0.0       Cerebellum   0.0       NCI-H292_Mucoepidermoid lung ca.   0.5       DMS-114_Small cell lung cancer   0.0       DMS-79_Small cell lung cancer/neuroendocrine   0.0       NCI-H146_Small cell lung cancer/   0.0       neuroendocrine       NCI-H526_Small cell lung cancer/   0.0       neuroendocrine       NCI-N417_Small cell lung cancer/   0.0       neuroendocrine       NCI-H82_Small cell lung cancer/   0.0       neuroendocrine       NCI-H157_Squamous cell lung cancer   0.0       (metastasis)       NCI-H1155_Large cell lung cancer/   0.0       neuroendocrine       NCI-H1299_Large cell lung cancer/   0.0       neuroendocrine       NCI-H727_Lung carcinoid   0.0       NCI-UMC-11_Lung carcinoid   0.0       LX-1_Small cell lung cancer   0.0       Colo-205_Colon cancer   0.0       KM12_Colon cancer   0.0       KM20L2_Colon cancer   0.0       NCI-H716 Colon cancer   0.0       SW-48_Colon adenocarcinoma   0.0       SW1116_Colon adenocarcinoma   0.0       LS 174T_Colon adenocarcinoma   0.0       SW-948_Colon adenocarcinoma   0.0       SW-480_Colon adenocarcinoma   0.0       NCI-SNU-5_Gastric ca   0.0       KATO III_Stomach   0.0       NCI-SNU-16_Gastric ca.   0.0       NCI-SNU-1_Gastric ca.   0.0       RF-1_Gastric adenocarcinoma   0.0       RF-48_Gastric adenocarcinoma   1.1       MKN-45_Gastric ca   2.0       NCI-N87_Gastric ca.   20.3       OVCAR-5_Ovarian ca.   0.0       RL95-2_Uterine carcinoma   6.3       HelaS3_Cervical adenocarcinoma   0.0       Ca Ski_Cervical epidermoid carcinoma   0.0       (metastasis)       ES-2_Ovarian clear cell carcinoma   0.0       Ramos/6 h stim_Stimulated with PMA/   0.0       ionomycin 6 h       Ramos/14 h stim_Stimulated with PMA/   0.0       ionomycin 14 h       MEG-01_Chronic myelogenous leukemia   0.0       (megokaryoblast)       Raji_Burkitt&#39;s lymphoma   0.0       Daudi_Burkitt&#39;s lymphoma   0.0       U266_B-cell plasmacytoma/myeloma   0.0       CA46_Burkitt&#39;s lymphoma   0.0       RL_non-Hodgkin&#39;s B-cell lymphoma   0.0       JM1_pre-B-cell lymphoma/leukemia   0.0       Jurkat_T cell leukemia   0.0       TF-1_Erythroleukemia   0.0       HUT 78_T-cell lymphoma   100.0       U937_Histiocytic lymphoma   0.0       KU-812 Myelogenous leukemia   19.6       769-P_Clear cell renal ca.   0.0       Caki-2_Clear cell renal ca.   0.0       SW 839_Clear cell renal ca.   0.0       G401_Wilms&#39; tumor   0.0       Hs766T_Pancreatic ca. (LN metastasis)   0.0       CAPAN-1_Pancreatic adenocarcinoma (liver   0.0       metastasis)       SU86.86_Pancreatic carcinoma (liver   2.1       metastasis)       BxPC-3_Pancreatic adenocarcinoma   1.2       HPAC_Pancreatic adenocarcinoma   0.0       MIA PaCa-2_Pancreatic ca.   0.0       CFPAC-1_Pancreatic ductal adenocarcinoma   10.4       PANC-1_Pancreatic epithelioid ductal ca.   0.0       T24_Bladder ca. (transitional cell)   0.0       5637_Bladder ca.   0.6       HT-1197_Bladder ca.   3.7       UM-UC-3_Bladder ca. (transitional cell)   0.0       A204_Rhabdomyosarcoma   0.0       HT-1080_Fibrosarcoma   0.0       MG-63_Osteosarcoma (bone)   0.0       SK-LMS-1_Leiomyosarcoma (vulva)   0.0       SJRH30_Rhabdomyosarcoma (met to bone   0.0       marrow)       A431_Epidermoid ca.   69.7       WM266-4_Melanoma   0.0       DU 145_Prostate   0.0       MDA-MB-468_Breast adenocarcinoma   1.5       SSC-4_Tongue   1.7       SSC-9_Tongue   2.7       SSC-15_Tongue   24.0       CAL 27_Squamous cell ca. of tongue   14.5                    
     [0899]               TABLE XG                          Panel 4.1D                                 Rel. Exp. (%)               Ag4387, Run           Tissue Name   186501500                                         Secondary Th1 act   0.0           Secondary Th2 act   0.0           Secondary Tr1 act   0.0           Secondary Th1 rest   0.0           Secondary Th2 rest   0.0           Secondary Tr1 rest   0.0           Primary Th1 act   0.0           Primary Th2 act   0.0           Primary Tr1 act   0.0           Primary Th1 rest   0.3           Primary Th2 rest   0.0           Primary Tr1 rest   0.0           CD45RA CD4 lymphocyte act   0.0           CD45RO CD4 lymphocyte act   0.0           CD8 lymphocyte act   0.0           Secondary CD8 lymphocyte rest   0.0           Secondary CD8 lymphocyte act   0.0           CD4 lymphocyte none   0.0           2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0           LAK cells rest   0.6           LAK cells IL-2   1.0           LAK cells IL-2 + IL-12   0.9           LAK cells IL-2 + IFN gamma   0.0           LAK cells IL-2 + IL-18   0.9           LAK cells PMA/ionomycin   0.6           NK Cells IL-2 rest   0.0           Two Way MLR 3 day   0.0           Two Way MLR 5 day   0.0           Two Way MLR 7 day   0.0           PBMC rest   0.0           PBMC PWM   0.9           PBMC PHA-L   0.0           Ramos (B cell) none   0.0           Ramos (B cell) ionomycin   0.0           B lymphocytes PWM   0.5           B lymphocytes CD40L and IL-4   0.0           EOL-1 dbcAMP   0.0           EOL-1 dbcAMP PMA/ionomycin   0.0           Dendritic cells none   0.0           Dendritic cells LPS   0.0           Dendritic cells anti-CD40   0.0           Monocytes rest   0.0           Monocytes LPS   0.0           Macrophages rest   0.0           Macrophages LPS   0.0           HUVEC none   0.0           HUVEC starved   0.0           HUVEC IL-1beta   0.0           HUVEC IFN gamma   0.0           HUVEC TNF alpha + IFN gamma   0.0           HUVEC TNF alpha + IL4   0.0           HUVEC IL-11   0.9           Lung Microvascular EC none   0.0           Lung Microvascular EC TNFalpha +   0.0           IL-1beta           Microvascular Dermal EC none   0.0           Microsvasular Dermal EC TNFalpha +   0.0           IL-1beta           Bronchial epithelium TNFalpha +   4.6           IL1beta           Small airway epithelium none   20.0           Small airway epithelium TNFalpha +   22.4           IL-1beta           Coronery artery SMC rest   0.0           Coronery artery SMC TNFalpha + IL-   0.0           1beta           Astrocytes rest   0.0           Astrocytes TNFalpha + IL-1beta   0.0           KU-812 (Basophil) rest   6.7           KU-812 (Basophil) PMA/ionomycin   16.3           CCD1106 (Keratinocytes) none   0.4           CCD1106 (Keratinocytes) TNFalpha +   2.5           IL-1beta           Liver cirrhosis   0.0           NCI-H292 none   0.4           NCI-H292 IL-4   0.9           NCI-H292 IL-9   0.0           NCI-H292 IL-13   0.0           NCI-H292 IFN gamma   0.0           HPAEC none   0.0           HPAEC TNF alpha + IL-1 beta   0.0           Lung fibroblast none   1.0           Lung fibroblast TNF alpha + IL-1   0.4           beta           Lung fibroblast IL-4   0.0           Lung fibroblast IL-9   0.0           Lung fibroblast IL-13   0.8           Lung fibroblast IFN gamma   0.0           Dermal fibroblast CCD1070 rest   0.0           Dermal fibroblast CCD1070 TNF   0.0           alpha           Dermal fibroblast CCD1070 IL-1   0.0           beta           Dermal fibroblast IFN gamma   0.0           Dermal fibroblast IL-4   0.0           Dermal Fibroblasts rest   0.0           Neutrophils TNFa + LPS   0.0           Neutrophils rest   1.8           Colon   2.0           Lung   2.1           Thymus   18.4           Kidney   100.0                        
     [0900] CNS_neurodegeneration_v1.0 Summary: Ag4387 Expression of the CG134100-01 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0901] General_screening_panel v1.4 Summary: Ag4387 Highest expression of the CG134100-01 gene is detected in bone marrow (CT=30.6). Therefore, expression of this gene may be used to distinguish this sample from other samples used in this panel. In addition, therapeutic modulation of this gene product may be useful in the bone marrow related diseases such as leukemia.  
     [0902] Low levels of expression of this gene is also seen in uterus, trachea and bladder. Therefore, therapeutic modulation of this gene may be useful in the treatment of diseases that affect these tissues.  
     [0903] General_screening_panel_v1.5 Summary: Ag4893/Ag4894 Two experiments with same probe and primer sets are in excellent agreement. Highest expression of the CG134100-01 gene is detected in bone marrow (CT=30-34). Therefore, expression of this gene may be used to distinguish this sample from other samples used in this panel. In addition, therapeutic modulation of this gene product may be useful in the bone marrow related diseases such as leukemia.  
     [0904] Oncology_cell_line_screening_panel_v3.1 Summary: Ag4893 Highest expression of the CG134100-01 gene is detected in T cell lymphoma (CT=29.6). In addition, high to moderate levels of expression of this gene is also seen number of cancer samples derived from tongue squamous cell carcinoma, epidermoid carcinoma, bladder carcinoma, pancreatic ductal adenocarcinoma, myelogenous leukemia, uterine and gastric carcinoma. Therefore, expression of this gene may be useful as marker to detect the presence of these cancers.  
     [0905] Ag4894 Results from one experiment with this gene are not included. The amp plot indicates that there were experimental difficulties with this run.  
     [0906] Panel 4.1D Summary: Ag4387 Highest expression of the CG134100-01 gene is detected in kidney (CT=30.9). Therefore, expression of this gene may be used to distinguish kidney from other samples used in this panel. In addition, therapeutic modulation of this gene may be beneficial in the treatment of autoimmune of inflammatory disease that affect kidney including lupus and glomerulonephritis.  
     [0907] Moderate to low levels of expression of this gene is also seen in thymus, basophils, and small airway epithelium. Therefore, therapeutic modulation of this gene product may be beneficial in the treatment of asthma, allergies, COPD, and emphysema, inflammatory bowel disease, and autoimmune diseases.  
     [0908] Y. NOV27a (CG134403-01): 2510042P03RIK Homolog (TmSP)  
     [0909] Expression of gene CG134403-01 was assessed using the primer-probe set Ag4871, described in Table YA. Results of the RTQ-PCR runs are shown in Tables YB and YC. Table YA. Probe Name Ag4871  
                   TABLE YA                          Probe Name Ag4871                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-cctaacagatttcttgcgacaa-3′   22   7   310                   Probe   TET-5′-agtcttccgcttccggttgctctgtt-3′-   26   39   311           TAMRA               Reverse   5′-tgttatgggtgcggttactatg-3′   22   67   312                  
 
     [0910]               TABLE YB                          General_screening_panel_v1.5                                 Rel. Exp. (%)               Ag4871, Run           Tissue Name   228903633                                         Adipose   2.2           Melanoma* Hs688(A).T   8.3           Melanoma* Hs688(B).T   5.7           Melanoma* M14   25.5           Melanoma* LOXIMVI   9.6           Melanoma* SK-MEL-5   10.3           Squamous cell carcinoma SCC-4   6.0           Testis Pool   26.8           Prostate ca.* (bone met) PC-3   13.0           Prostate Pool   3.2           Placenta   1.4           Uterus Pool   2.7           Ovarian ca. OVCAR-3   28.5           Ovarian ca. SK-OV-3   29.7           Ovarian ca. OVCAR-4   3.0           Ovarian ca. OVCAR-5   15.3           Ovarian ca. IGROV-1   7.7           Ovarian ca OVCAR-8   6.2           Ovary   4.3           Breast ca. MCF-7   9.5           Breast ca. MDA-MB-231   15.5           Breast ca. BT 549   8.1           Breast ca. T47D   6.0           Breast ca. MDA-N   14.1           Breast Pool   13.4           Trachea   3.9           Lung   0.5           Fetal Lung   4.6           Lung ca. NCI-N417   6.5           Lung ca. LX-1   13.4           Lung ca. NCI-H146   18.3           Lung ca. SHP-77   11.0           Lung ca. A549   14.7           Lung ca. NCI-H526   5.8           Lung ca. NCI-H23   10.1           Lung ca. NCI-H460   6.0           Lung ca. HOP-62   4.3           Lung ca. NCI-H522   11.3           Liver   0.7           Fetal Liver   7.5           Liver ca. HepG2   9.2           Kidney Pool   8.5           Fetal Kidney   19.2           Renal ca. 786-0   17.2           Renal ca. A498   5.4           Renal ca. ACHN   8.4           Renal ca. UO-31   8.1           Renal ca. TK-10   12.4           Bladder   3.0           Gastric ca. (liver met.) NCI-N87   31.9           Gastric ca. KATO III   8.0           Colon ca. SW-948   1.8           Colon ca. SW480   30.1           Colon ca.* (SW480 met) SW620   9.5           Colon ca. HT29   9.3           Colon ca. HCT-116   9.7           Colon ca. CaCo-2   15.9           Colon cancer tissue   2.6           Colon ca. SW1116   5.0           Colon ca. Colo-205   4.1           Colon ca. SW-48   2.1           Colon Pool   9.7           Small Intestine Pool   3.0           Stomach Pool   2.1           Bone Marrow Pool   1.3           Fetal Heart   5.6           Heart Pool   1.5           Lymph Node Pool   8.3           Fetal Skeletal Muscle   4.7           Skeletal Muscle Pool   4.8           Spleen Pool   2.7           Thymus Pool   4.3           CNS cancer (glio/astro) U87-MG   20.3           CNS cancer (glio/astro) U-118-MG   27.0           CNS cancer (neuro; met) SK-N-AS   100.0           CNS cancer (astro) SF-539   8.9           CNS cancer (astro) SNB-75   13.2           CNS cancer (glio) SNB-19   12.8           CNS cancer (glio) SF-295   22.4           Brain (Amygdala) Pool   4.5           Brain (cerebellum)   5.4           Brain (fetal)   8.3           Brain (Hippocampus) Pool   3.7           Cerebral Cortex Pool   5.9           Brain (Substantia nigra) Pool   4.3           Brain (Thalamus) Pool   6.3           Brain (whole)   6.4           Spinal Cord Pool   9.6           Adrenal Gland   4.1           Pituitary gland Pool   3.0           Salivary Gland   2.9           Thyroid (female)   3.4           Pancreatic ca. CAPAN2   8.8           Pancreas Pool   8.0                        
     [0911]               TABLE YC                          Panel 4.1D                                 Rel. Exp. (%)               Ag4871, Run           Tissue Name   223458798                                         Secondary Th1 act   21.9           Secondary Th2 act   25.0           Secondary Tr1 act   23.8           Secondary Th1 rest   11.5           Secondary Th2 rest   4.2           Secondary Tr1 rest   0.0           Primary Th1 act   1.5           Primary Th2 act   34.6           Primary Tr1 act   40.1           Primary Th1 rest   0.0           Primary Th2 rest   8.4           Primary Tr1 rest   17.6           CD45RA CD4 lymphocyte act   29.7           CD45RO CD4 lymphocyte act   34.9           CD8 lymphocyte act   27.4           Secondary CD8 lymphocyte rest   5.3           Secondary CD8 lymphocyte act   24.7           CD4 lymphocyte none   26.2           2ry Th1/Th2/Tr1_anti-CD95 CH11   24.8           LAK cells rest   9.8           LAK cells IL-2   26.4           LAK cells IL-2 + IL-12   20.4           LAK cells IL-2 + IFN gamma   35.8           LAK cells IL-2 + IL-18   21.3           LAK cells PMA/ionomycin   21.9           NK Cells IL-2 rest   14.7           Two Way MLR 3 day   7.2           Two Way MLR 5 day   12.7           Two Way MLR 7 day   12.4           PBMC rest   18.6           PBMC PWM   39.8           PBMC PHA-L   10.4           Ramos (B cell) none   4.3           Ramos (B cell) ionomycin   25.9           B lymphocytes PWM   2.4           B lymphocytes CD40L and IL-4   31.6           EOL-1 dbcAMP   9.7           EOL-1 dbcAMP PMA/ionomycin   5.0           Dendritic cells none   17.2           Dendritic cells LPS   9.4           Dendritic cells anti-CD40   1.0           Monocytes rest   11.5           Monocytcs LPS   20.3           Macrophages rest   21.2           Macrophages LPS   15.2           HUVEC none   18.7           HUVEC starved   50.7           HUVEC IL-1beta   60.7           HUVEC IFN gamma   100.0           HUVEC TNF alpha + IFN gamma   70.2           HUVEC TNF alpha + IL4   28.3           HUVEC IL-11   28.7           Lung Microvascular EC none   90.1           Lung Microvascular EC TNFalpha +   39.8           IL-1beta           Microvascular Dermal EC none   49.0           Microsvasular Dermal EC TNFalpha +   10.9           IL-1beta           Bronchial epithelium TNFalpha +   27.2           IL1beta           Small airway epithelium none   11.0           Small airway epithelium TNFalpha +   21.5           IL-1beta           Coronery artery SMC rest   22.7           Coronery artery SMC TNFalpha + IL-   71.7           1beta           Astrocytes rest   8.7           Astrocytes TNFalpha + IL-1beta   9.3           KU-812 (Basophil) rest   30.4           KU-812 (Basophil) PMA/ionomycin   25.7           CCD1106 (Keratinocytes) none   37.9           CCD1106 (Keratinocytes) TNFalpha +   47.6           IL-1beta           Liver cirrhosis   9.7           NCI-H292 none   39.8           NCI-H292 IL-4   47.6           NCI-H292 IL-9   79.6           NCI-H292 IL-13   59.0           NCI-H292 IFN gamma   45.1           HPAEC none   43.2           HPAEC TNF alpha + IL-1 beta   40.3           Lung fibroblast none   46.0           Lung fibroblast TNF alpha + IL-1   46.7           beta           Lung fibroblast IL-4   18.9           Lung fibroblast IL-9   42.6           Lung fibroblast IL-13   17.2           Lung fibroblast IFN gamma   26.8           Dermal fibroblast CCD1070 rest   25.3           Dermal fibroblast CCD1070 TNF alpha   57.8           Dermal fibroblast CCD1070 IL-1 beta   20.6           Dermal fibroblast IFN gamma   38.4           Dermal fibroblast IL-4   25.2           Dermal Fibroblasts rest   12.7           Neutrophils TNFa + LPS   0.7           Neutrophils rest   13.8           Colon   3.4           Lung   23.5           Thymus   36.3           Kidney   32.3                        
     [0912] General_screening_panel_v1.5 Summary: Ag4871 Highest expression of this gene is detected in CNS cancer SK-N-AS cell line (CT=28.5). Moderate levels of expression of this gene is also seen in cluster of cancer cell lines derived from gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers. Thus, expression of this gene could be used as a marker to detect the presence of these cancers. Furthermore, therapeutic modulation of the expression or function of this gene may be effective in the treatment of gastric, colon, lung, renal, breast, ovarian, prostate, squamous cell carcinoma, melanoma and brain cancers.  
     [0913] Among tissues with metabolic or endocrine function, this gene is expressed at moderate to low levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0914] Interestingly, this gene is expressed at much higher levels in fetal (CTs=32.2-32.9) when compared to adult liver and lung, respectively (CTs=36). This observation suggests that expression of this gene can be used to distinguish fetal from adult liver and lung, respectively. In addition, the relative overexpression of this gene in fetal tissues suggests that the protein product may enhance growth or development of liver and lung in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the protein encoded by this gene could be useful in treatment of liver and lung related diseases.  
     [0915] In addition, this gene is expressed at moderate levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0916] Panel 4.1D Summary: Ag4871 Highest expression of this gene is detected in IFN gamma treated HUVEC cells (CT=31.9). This gene is expressed at low to moderate levels in a wide range of cell types of significance in the immune response in health and disease. These cells include members of the T-cell, B-cell, endothelial cell, macrophage/monocyte, and peripheral blood mononuclear cell family, as well as epithelial and fibroblast cell types from lung and skin, and normal tissues represented by colon, lung, thymus and kidney. This ubiquitous pattern of expression suggests that this gene product may be involved in homeostatic processes for these and other cell types and tissues. This pattern is in agreement with the expression profile in General_screening_panel_v1.5 and also suggests a role for the gene product in cell survival and proliferation. Therefore, modulation of the gene product with a functional therapeutic may lead to the alteration of functions associated with these cell types and lead to improvement of the symptoms of patients suffering from autoimmune and inflammatory diseases such as asthma, allergies, inflammatory bowel disease, lupus erythematosus, psoriasis, rheumatoid arthritis, and osteoarthritis.  
     [0917] Z. NOV32a (CG56711-01): Kallistatin Precursor.  
     [0918] Expression of gene CG56711-01 was assessed using the primer-probe set Ag1689, described in Table ZA. Results of the RTQ-PCR runs are shown in Tables ZB, ZC and ZD. Please note that CG56711-01 represents a full-length physical clone  
                   TABLE ZA                          Probe Name Ag1689                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-aatgaggtggaacaacttgttg-3′   22   894   313                   Probe   TET-5′-caagaagctagagttgcatcttccca-3′-   26   933   314           TAMRA               Reverse   5′-ataggagccagaaatggagaac-3′   22   960   315                  
 
     [0919]               TABLE ZB                          Panel 1.3D                             Rel. Exp. (%)   Rel. Exp. (%)           Ag1689, Run   Ag1689, Run       Tissue Name   159350722   165534829                                 Liver adenocarcinoma   0.0   0.0       Pancreas   12.7   18.4       Pancreatic ca. CAPAN 2   0.0   0.0       Adrenal gland   0.0   0.0       Thyroid   0.0   0.0       Salivary gland   0.0   0.0       Pituitary gland   0.0   0.0       Brain (fetal)   0.0   0.0       Brain (whole)   0.0   0.0       Brain (amygdala)   0.0   0.0       Brain (cerebellum)   0.0   0.0       Brain (hippocampus)   0.0   0.0       Brain (substantia nigra)   0.0   0.0       Brain (thalamus)   0.0   0.0       Cerebral Cortex   0.0   0.0       Spinal cord   0.0   0.1       glio/astro U87-MG   0.0   0.0       glio/astro U-118-MG   0.0   0.0       astrocytoma SW1783   0.0   0.0       neuro*; met SK-N-AS   0.0   0.0       astrocytoma SF-539   0.0   0.0       astrocytoma SNB-75   0.0   0.0       glioma SNB-19   0.0   0.0       glioma U251   0.0   0.0       glioma SF-295   0.0   0.0       Heart (fetal)   0.0   0.0       Heart   0.0   0.0       Skeletal muscle (fetal)   0.0   0.0       Skeletal muscle   0.0   0.0       Bone marrow   0.0   0.0       Thymus   0.0   0.0       Spleen   0.0   0.8       Lymph node   0.0   0.0       Colorectal   0.0   0.0       Stomach   8.7   10.5       Small intestine   0.0   0.0       Colon ca. SW480   0.0   0.0       Colon ca.* SW620 (SW480 met)   0.0   0.0       Colon ca. HT29   0.5   0.3       Colon ca. HCT-116   0.0   0.0       Colon ca. CaCo-2   2.5   3.0       Colon ca. tissue (ODO3866)   1.9   0.4       Colon ca. HCC-2998   0.0   0.0       Gastric ca.* (liver met) NCI-N87   0.0   0.0       Bladder   7.2   12.4       Trachea   0.0   0.0       Kidney   2.0   0.1       Kidney (fetal)   10.9   8.4       Renal ca. 786-0   0.0   0.0       Renal ca. A498   0.0   0.0       Renal ca. RXF 393   0.0   0.0       Renal ca. ACHN   0.0   0.0       Renal ca. UO-31   0.0   0.0       Renal ca. TK-10   0.0   0.0       Liver   91.4   100.0       Liver (fetal)   100.0   93.3       Liver ca. (hepatoblast) HepG2   14.0   25.9       Lung   0.0   0.0       Lung (fetal)   0.0   0.0       Lung ca. (small cell) LX-1   0.0   0.1       Lung ca. (small cell) NCI-H69   0.0   0.0       Lung ca. (s. cell var.) SHP-77   0.0   0.0       Lung ca. (large cell) NCI-H460   0.0   0.0       Lung ca. (non-sm. cell) A549   0.0   0.1       Lung ca. (non-s. cell) NCI-H23   0.0   0.0       Lung ca. (non-s. cell) HOP-62   0.0   0.0       Lung ca. (non-s. cl) NCI-H522   0.0   0.0       Lung ca. (squam.) SW 900   0.0   0.0       Lung ca. (squam.) NCI-H596   0.0   0.0       Mammary gland   0.1   0.2       Breast ca.* (pl. ef) MCF-7   0.0   0.1       Breast ca.* (pl. ef) MDA-MB-231   0.0   0.0       Breast ca.* (pl. ef) T47D   0.0   0.1       Breast ca. BT-549   0.0   0.0       Breast ca. MDA-N   0.0   0.0       Ovary   0.0   0.0       Ovarian ca. OVCAR-3   0.0   0.0       Ovarian ca. OVCAR-4   0.0   0.1       Ovarian ca. OVCAR-5   0.0   0.0       Ovarian ca. OVCAR-8   0.0   0.0       Ovarian ca. IGROV-1   0.0   0.0       Ovarian ca.* (ascites) SK-OV-3   0.0   0.0       Uterus   0.0   0.0       Placenta   0.0   0.0       Prostate   0.1   0.4       Prostate ca.* (bone met) PC-3   0.0   0.0       Testis   0.3   0.2       Melanoma Hs688(A).T   0.0   0.0       Melanoma* (met) Hs688(B).T   0.0   0.0       Melanoma UACC-62   0.0   0.0       Melanoma M14   0.0   0.0       Melanoma LOX IMVI   0.0   0.0       Melanoma* (met) SK-MEL-5   0.0   0.0       Adipose   0.0   0.0                    
     [0920]               TABLE ZC                          Panel 2D                                 Rel. Exp. (%)               Ag1689, Run           Tissue Name   159352635                                         Normal Colon   0.8           CC Well to Mod Diff (ODO3866)   0.9           CC Margin (ODO3866)   0.0           CC Gr.2 rectosigmoid (ODO3868)   0.1           CC Margin (ODO3868)   0.0           CC Mod Diff (ODO3920)   0.3           CC Margin (ODO3920)   0.0           CC Gr.2 ascend colon (ODO3921)   0.1           CC Margin (ODO3921)   0.0           CC From Partial Hepatectomy (ODO4309)   9.9           Mets           Liver Margin (ODO4309)   100.0           Colon mets to lung (OD04451-01)   0.1           Lung Margin (OD04451-02)   0.0           Normal Prostate 6546-1   0.1           Prostate Cancer (OD04410)   0.0           Prostate Margin (OD04410)   0.1           Prostate Cancer (OD04720-01)   0.0           Prostate Margin (OD04720-02)   0.0           Normal Lung 061010   0.5           Lung Met to Muscle (ODO4286)   0.0           Muscle Margin (ODO4286)   0.0           Lung Malignant Cancer (OD03126)   0.1           Lung Margin (OD03126)   0.0           Lung Cancer (OD04404)   0.0           Lung Margin (OD04404)   0.0           Lung Cancer (OD04565)   0.0           Lung Margin (OD04565)   0.0           Lung Cancer (OD04237-01)   0.0           Lung Margin (OD04237-02)   0.0           Ocular Mel Met to Liver (ODO4310)   0.0           Liver Margin (ODO4310)   69.7           Melanoma Mets to Lung (OD04321)   0.0           Lung Margin (OD04321)   3.6           Normal Kidney   3.9           Kidney Ca, Nuclear grade 2 (OD04338)   0.3           Kidney Margin (OD04338)   3.1           Kidney Ca Nuclear grade 1/2 (OD04339)   0.2           Kidney Margin (OD04339)   4.8           Kidney Ca, Clear cell type (OD04340)   0.0           Kidney Margin (OD04340)   1.1           Kidney Ca, Nuclear grade 3 (OD04348)   0.0           Kidney Margin (OD04348)   1.2           Kidney Cancer (OD04622-01)   0.0           Kidney Margin (OD04622-03)   0.5           Kidney Cancer (OD04450-01)   0.0           Kidney Margin (OD04450-03)   1.3           Kidney Cancer 8120607   0.0           Kidney Margin 8120608   1.3           Kidney Cancer 8120613   0.0           Kidney Margin 8120614   2.7           Kidney Cancer 9010320   0.1           Kidney Margin 9010321   1.4           Normal Uterus   0.0           Uterus Cancer 064011   2.7           Normal Thyroid   0.0           Thyroid Cancer 064010   0.6           Thyroid Cancer A302152   0.0           Thyroid Margin A302153   0.0           Normal Breast   0.0           Breast Cancer (OD04566)   0.0           Breast Cancer (OD04590-01)   0.0           Breast Cancer Mets (OD04590-03)   0.0           Breast Cancer Metastasis (OD04655-05)   0.0           Breast Cancer 064006   1.0           Breast Cancer 1024   0.0           Breast Cancer 9100266   0.1           Breast Margin 9100265   0.0           Breast Cancer A209073   0.0           Breast Margin A209073   0.0           Normal Liver   72.7           Liver Cancer 064003   21.0           Liver Cancer 1025   73.7           Liver Cancer 1026   63.3           Liver Cancer 6004-T   84.7           Liver Tissue 6004-N   5.5           Liver Cancer 6005-T   40.1           Liver Tissue 6005-N   48.3           Normal Bladder   33.7           Bladder Cancer 1023   0.1           Bladder Cancer A302173   0.2           Bladder Cancer (OD04718-01)   0.8           Bladder Normal Adjacent (OD04718-03)   0.0           Normal Ovary   0.0           Ovarian Cancer 064008   0.0           Ovarian Cancer (OD04768-07)   0.8           Ovary Margin (OD04768-08)   0.0           Normal Stomach   3.7           Gastric Cancer 9060358   0.7           Stomach Margin 9060359   9.9           Gastric Cancer 9060395   0.1           Stomach Margin 9060394   4.9           Gastric Cancer 9060397   8.6           Stomach Margin 9060396   2.2           Gastric Cancer 064005   0.2                        
     [0921]               TABLE ZD                          Panel 4D                             Rel. Exp. (%)   Rel. Exp. (%)           Ag1689, Run   Ag1689, Run       Tissue Name   159350723   165725926                                 Secondary Th1 act   0.0   0.0       Secondary Th2 act   0.0   0.0       Secondary Tr1 act   0.0   0.0       Secondary Th1 rest   0.0   0.0       Secondary Th2 rest   0.0   0.0       Secondary Tr1 rest   0.0   0.0       Primary Th1 act   0.0   0.0       Primary Th2 act   0.0   0.0       Primary Tr1 act   0.0   0.0       Primary Th1 rest   0.0   0.0       Primary Th2 rest   0.0   0.0       Primary Tr1 rest   0.0   0.0       CD45RA CD4 lymphocyte act   0.0   0.0       CD45RO CD4 lymphocyte act   0.0   0.0       CD8 lymphocyte act   0.0   0.0       Secondary CD8 lymphocyte rest   0.0   0.0       Secondary CD8 lymphocyte act   0.0   0.0       CD4 lymphocyte none   0.0   0.0       2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0   0.0       LAK cells rest   0.0   0.0       LAK cells IL-2   0.0   0.0       LAK cells IL-2 + IL-12   0.0   0.0       LAK cells IL-2 + IFN gamma   0.0   0.0       LAK cells IL-2 + IL-18   0.0   0.0       LAK cells PMA/ionomycin   0.0   0.0       NK Cells IL-2 rest   0.0   0.0       Two Way MLR 3 day   0.0   0.0       Two Way MLR 5 day   0.0   0.0       Two Way MLR 7 day   0.0   0.0       PBMC rest   0.0   0.0       PBMC PWM   0.0   0.0       PBMC PHA-L   0.0   0.0       Ramos (B cell) none   0.0   0.0       Ramos (B cell) ionomycin   0.0   0.0       B lymphocytes PWM   0.0   0.0       B lymphocytes CD40L and IL-4   0.0   0.0       EOL-1 dbcAMP   0.0   0.0       EOL-1 dbcAMP PMA/ionomycin   0.0   0.0       Dendritic cells none   0.0   0.0       Dendritic cells LPS   0.0   0.0       Dendritic cells anti-CD40   0.0   0.0       Monocytes rest   0.0   0.0       Monocytes LPS   0.0   0.0       Macrophages rest   0.0   0.0       Macrophages LPS   0.0   0.0       HUVEC none   0.0   0.0       HUVEC starved   0.0   0.0       HUVEC IL-1beta   0.0   0.0       HUVEC IFN gamma   0.0   0.0       HUVEC TNF alpha + IFN gamma   0.0   0.0       HUVEC TNF alpha + IL4   0.0   0.0       HUVEC IL-11   0.0   0.0       Lung Microvascular EC none   0.3   0.0       Lung Microvascular EC TNF alpha +   0.0   0.0       IL-1beta       Microvascular Dermal EC none   0.0   0.0       Microsvasular Dermal EC TNF   0.0   0.0       alpha + IL-1beta       Bronchial epithelium TNF alpha +   0.0   0.0       IL1beta       Small airway epithelium none   0.0   0.0       Small airway epithelium   0.0   0.0       TNFalpha + IL-1beta       Coronery artery SMC rest   0.0   0.0       Coronery artery SMC TNFalpha +   0.0   0.0       IL-1beta       Astrocytes rest   0.0   0.0       Astrocytes TNF alpha + IL-1beta   0.0   0.0       KU-812 (Basophil) rest   0.0   0.0       KU-812 (Basophil) PMA/ionomycin   0.0   0.0       CCD1106 (Keratinocytes) none   0.0   0.0       CCD1106 (Keratinocytes) TNF   0.0   0.0       alpha + IL-1beta       Liver cirrhosis   100.0   100.0       Lupus kidney   5.7   4.6       NCI-H292 none   0.0   0.0       NCI-H292 IL-4   0.0   0.0       NCI-H292 IL-9   0.0   0.0       NCI-H292 IL-13   0.0   0.0       NCI-H292 IFN gamma   0.0   0.0       HPAEC none   0.0   0.0       HPAEC TNF alpha + IL-1 beta   0.0   0.0       Lung fibroblast none   0.0   0.0       Lung fibroblast TNF alpha + IL-1   0.0   0.0       beta       Lung fibroblast IL-4   0.0   0.0       Lung fibroblast IL-9   0.0   0.0       Lung fibroblast IL-13   0.0   0.0       Lung fibroblast IFN gamma   0.0   0.0       Dermal fibroblast CCD1070 rest   0.0   0.0       Dermal fibroblast CCD1070 TNF   0.0   0.0       alpha       Dermal fibroblast CCD1070 IL-1 beta   0.0   0.0       Dermal fibroblast IFN gamma   0.0   0.0       Dermal fibroblast IL-4   0.0   0.0       IBD Colitis 2   0.0   0.0       IBD Crohn&#39;s   0.0   0.2       Colon   0.7   0.4       Lung   0.5   0.1       Thymus   45.1   17.9       Kidney   0.0   0.1                    
     [0922] CNS_neurodegeneration_v1.0 Summary: Ag1689 Expression of this gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0923] Panel 1.3D Summary: Ag1689 Two experiment with same probe and primer sets arc in excellent agreement with highest expression of the CG56711-01 gene in adult and fetal liver (CTs=27-29). Therefore, expression of this gene may be used to distinguish these samples from other samples in this panel. Moderate to low expression of this gene is also seen in liver cancer and colon cancer cell line. Therefore, therapeutic modulation of this gene may be useful in the treatment of liver related diseases, liver and colon cancers.  
     [0924] Moderate levels of expression of this gene is also seen in pancreas and stomach. This gene codes for a kallistatin precursor, a serine proteinase inhibitor (serpin) with Phe-Phe residues at the P2 and P1 positions. Kallistatin inhibits the proliferation, migration and adhesion of endothelial cells in vitro and angiogenesis in the rat model of hindlimb ischemia. It induces vasorelaxation of isolated aortic rings and reduces renal perfusion pressure in isolated rat kidneys. It also inhibits the proliferation, migration and adhesion of endothelial cells in vitro and angiogenesis in the rat model of hindlimb ischemia (Chao et al., 2001, Biol Chem 382(1):15-21, PMID: 11258665). Furthermore, kallistatin expression is lower in the eye of patients suffering from diabetes and thus may be involved in diabetic retinopathy (Ma et al., 1996, Curr Eye Res 1996 November;15(11):1117-23, PMID: 8950506). Thus, therapeutic modulation of the activity of the kallistatin precursor encoded by this gene, through the use of protein therapeutics or antibodies, may be useful in the treatment of diabetes, diabetic retinopathy, blood pressure regulation and vascular remodeling.  
     [0925] Panel 2D Summary: Ag1689 Highest expression of the CG56711-01 gene is detected in liver (ODO4309)(CT=25.8). Interestingly, expression of this gene is much lower in the samples derived hepatectomy (ODO4309) metastasis and occular cancer metastasis to liver (ODO4310) (CT=29-40) as compared to corresponding adjacent control samples (CTs=25-26). High levels of expression of this gene is also seen in normal and liver cancer samples. Therefore, therapeutic modulation of expression of this gene or use of the protein encoded by this gene in the form of protein therapeutics may be useful in the treatment of these cancers and their metastasis.  
     [0926] Moderate to low levels of expression of this gene is also seen in gastric and kidney normal tissue samples compared with the adjacent tumor sample. It is also expressed in a sample of uterine and breast cancer. It may thus be used as a marker for these cancers and modulation of the activity of this gene or its protein product, through the use of protein therapeutics or antibodies, might be beneficial in the treatment of these cancers.  
     [0927] Panel 4D Summary: Ag1689 Two experiment with same probe and primer sets are in excellent agreement with highest expression of the CG56711-01 gene in liver cirrhosis (CTs=27-3 1). Therefore, expression of this gene may be useful distinguishing this sample from other samples in this panel and also as a marker for the diagnosis of liver cirrhosis. Furthermore, therapeutic modulation of this gene or its product may be beneficial in the treatment of liver cirrhosis.  
     [0928] In addition, moderate levels of expression of this gene is also seen in thymus. Thus, drugs that inhibit the function of this protein may regulate T cell development in the thymus and reduce or eliminate the symptoms of T cell mediated autoimmune or inflammatory diseases, including asthma, allergies, inflammatory bowel disease, lupus erythematosus, or rheumatoid arthritis. Additionally, small molecule or antibody therapeutics designed against this putative protein may disrupt T cell development in the thymus and function as an immunosuppresant for tissue transplant.  
     [0929] AA. NOV40a and NOV21a (CG95205-02 and CG133159-01): TEM-1 Splice Variant.  
     [0930] Expression of gene CG95205-02 and CG133159-01 was assessed using the primer-probe sets Ag389, Ag4808 and Ag4834, described in Tables AAA, AAB and AAC. Results of the RTQ-PCR runs are shown in Tables AAD, AAE, AAF, AAG, AAH, AAI and AAJ. Please note that the probes and primer sets Ag4808 and Ag4834 are specific for CG95205-02.  
                   TABLE AAA                          Probe Name Ag389                                                     Start   SEQ ID           Primers   Sequences   Length   Position   No                                             Forward   5′-catgtccctcgctacaataacact-3′   24   1006   316                   Probe   TET-5′-agccaccaacgtagttgacacacatctgc-3′-   29   974   317           TAMRA               Reverse   5′-gccagattgccggtgtg-3′   17   952   318                  
 
     [0931]                   TABLE AAB                          Probe Name Ag4808                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-gggtcctctctcaaccactaga-3′   22   1346   319                   Probe   TET-5′-cttggctctcaggaactctgcttcct-3′-   26   1368   320           TAMRA               Reverse   5′-aggtcttaagggctttggtgta-3′   22   1417   321                    
     [0932]                   TABLE AAC                          Probe Name Ag4834                                     Primers   Sequences   Length   Start Position   SEQ ID No                                             Forward   5′-ggagcccacctggcca-3′   16   1280   322                   Probe   TET-5′-gctgcccagctggacagat-3′-TAMRA   19   1301   323               Reverse   5′-cctggggagcaggaagc-3′   17   1321   324                    
     [0933]               TABLE AAD                          General_screening_panel_v1.4                                 Rel. Exp. (%)               Ag4808, Run           Tissue Name   223204451                                         Adipose   17.8           Melanoma* Hs688(A).T   71.7           Melanoma* Hs688(B).T   100.0           Melanoma* M14   0.0           Melanoma* LOXIMVI   0.0           Melanoma* SK-MEL-5   0.0           Squamous cell carcinoma SCC-4   0.5           Testis Pool   4.5           Prostate ca.* (bone met) PC-3   0.1           Prostate Pool   3.1           Placenta   20.0           Uterus Pool   3.1           Ovarian ca. OVCAR-3   0.2           Ovarian ca. SK-OV-3   0.1           Ovarian ca. OVCAR-4   0.3           Ovarian ca. OVCAR-5   0.1           Ovarian ca. IGROV-1   0.0           Ovarian ca. OVCAR-8   0.0           Ovary   6.3           Breast ca. MCF-7   0.0           Breast ca. MDA-MB-231   0.1           Breast ca. BT 549   1.1           Breast ca. T47D   0.3           Breast ca. MDA-N   0.0           Breast Pool   8.1           Trachea   6.6           Lung   5.2           Fetal Lung   24.1           Lung ca. NCI-N417   5.0           Lung ca. LX-1   0.0           Lung ca. NCI-H146   0.0           Lung ca. SHP-77   3.2           Lung ca. A549   0.1           Lung ca. NCI-H526   0.1           Lung ca. NCI-H23   0.5           Lung ca. NCI-H460   0.0           Lung ca. HOP-62   0.1           Lung ca. NCI-H522   0.8           Liver   0.0           Fetal Liver   4.2           Liver ca. HepG2   0.8           Kidney Pool   16.2           Fetal Kidney   6.8           Renal ca. 786-0   0.0           Renal ca. A498   0.1           Renal ca. ACHN   0.0           Renal ca. UO-31   0.1           Renal ca. TK-10   0.1           Bladder   12.9           Gastric ca. (liver met.) NCI-N87   0.2           Gastric ca. KATO III   0.0           Colon ca. SW-948   0.0           Colon ca. SW480   0.1           Colon ca.* (SW480 met) SW620   0.2           Colon ca. HT29   0.0           Colon ca. HCT-116   0.3           Colon ca. CaCo-2   0.6           Colon cancer tissue   29.1           Colon ca. SW1116   0.0           Colon ca. Colo-205   0.0           Colon ca. SW-48   0.0           Colon Pool   7.2           Small Intestine Pool   9.4           Stomach Pool   8.5           Bone Marrow Pool   2.9           Fetal Heart   2.7           Heart Pool   4.0           Lymph Node Pool   7.7           Fetal Skeletal Muscle   4.4           Skeletal Muscle Pool   8.3           Spleen Pool   2.7           Thymus Pool   13.6           CNS cancer (glio/astro) U87-MG   0.5           CNS cancer (glio/astro) U-118-MG   0.9           CNS cancer (neuro; met) SK-N-AS   58.2           CNS cancer (astro) SF-539   0.3           CNS cancer (astro) SNB-75   1.4           CNS cancer (glio) SNB-19   0.0           CNS cancer (glio) SF-295   0.0           Brain (Amygdala) Pool   0.6           Brain (cerebellum)   1.4           Brain (fetal)   2.3           Brain (Hippocampus) Pool   1.1           Cerebral Cortex Pool   0.9           Brain (Substantia nigra) Pool   1.4           Brain (Thalamus) Pool   0.4           Brain (whole)   0.6           Spinal Cord Pool   0.6           Adrenal Gland   3.9           Pituitary gland Pool   0.3           Salivary Gland   0.9           Thyroid (female)   2.9           Pancreatic ca. CAPAN2   0.0           Pancreas Pool   17.0                        
     [0934]               TABLE AAE                          HASS Panel v1.0                                 Rel. Exp. (%)               Ag389, Run           Tissue Name   268362650                                         MCF-7 C1   0.3           MCF-7 C2   0.5           MCF-7 C3   1.1           MCF-7 C4   0.1           MCF-7 C5   0.2           MCF-7 C6   0.6           MCF-7 C7   0.1           MCF-7 C9   0.8           MCF-7 C10   0.2           MCF-7 C11   0.2           MCF-7 C12   0.3           MCF-7 C13   0.4           MCF-7 C15   0.3           MCF-7 C16   0.5           MCF-7 C17   0.8           T24 D1   0.1           T24 D2   0.1           T24 D3   0.5           T24 D4   0.2           T24 D5   0.2           T24 D6   0.0           T24 D7   0.2           T24 D9   0.0           T24 D10   0.0           T24 D11   0.3           T24 D12   0.1           T24 D13   0.3           T24 D15   0.1           T24 D16   0.1           T24 D17   0.0           CAPaN B1   0.0           CAPaN B2   0.0           CAPaN B3   0.1           CAPaN B4   0.0           CAPaN B5   0.0           CAPaN B6   0.2           CAPaN B7   0.0           CAPaN B8   0.0           CAPaN B9   0.0           CAPaN B10   0.0           CAPaN B11   0.0           CAPaN B12   0.0           CAPaN B13   0.0           CAPaN B14   0.0           CAPaN B15   0.0           CAPaN B16   0.0           CAPaN B17   0.0           U87-MG F1 (B)   0.2           U87-MG F2   0.1           U87-MG F3   1.2           U87-MG F4   0.0           U87-MG F5   0.5           U87-MG F6   0.9           U87-MG F7   0.4           U87-MG F8   0.1           U87-MG F9   0.1           U87-MG F10   0.9           U87-MG F11   2.0           U87-MG F12   0.2           U87-MG F13   0.3           U87-MG F14   0.5           U87-MG F15   0.4           U87-MG F16   0.3           U87-MG F17   0.4           LnCAP A1   0.0           LnCAP A2   0.0           LnCAP A3   0.0           LnCAP A4   0.6           LnCAP A5   0.2           LnCAP A6   0.7           LnCAP A7   0.2           LnCAP A8   0.3           LnCAP A9   0.2           LnCAP A10   0.0           LnCAP A11   1.3           LnCAP A12   0.0           LnCAP A13   0.0           LnCAP A14   0.0           LnCAP A15   0.1           LnCAP A16   0.0           LnCAP A17   0.2           Primary Astrocytes   52.5           Primary Renal Proximal Tubule   0.0           Epithelial cell A2           Primary melanocytes A5   100.0           126443 - 341 medullo   0.7           126444 - 487 medullo   61.1           126445 - 425 medullo   0.0           126446 - 690 medullo   0.7           126447 - 54 adult glioma   0.5           126448 - 245 adult glioma   0.1           126449 - 317 adult glioma   3.0           126450 - 212 glioma   0.9           126451 - 456 glioma   1.1                        
     [0935]               TABLE AAF                          Panel 1.1                             Rel. Exp. (%)   Rel. Exp. (%)           Ag389, Run   Ag389, Run       Tissue Name   109668399   129785554                                 Adrenal gland   8.7   8.0       Bladder   15.8   13.8       Brain (amygdala)   0.4   0.5       Brain (cerebellum)   2.9   2.4       Brain (hippocampus)   1.4   2.2       Brain (substantia nigra)   6.6   3.8       Brain (thalamus)   1.7   1.3       Cerebral Cortex   3.1   1.9       Brain (fetal)   3.0   3.0       Brain (whole)   2.1   1.5       glio/astro U-118-MG   0.1   0.2       astrocytoma SF-539   0.0   0.1       astrocytoma SNB-75   0.0   0.0       astrocytoma SW1783   1.7   1.2       glioma U251   0.0   0.0       glioma SF-295   0.0   0.0       glioma SNB-19   0.0   0.0       glio/astro U87-MG   0.0   0.1       neuro*; met SK-N-AS   95.3   100.0       Mammary gland   85.3   80.7       Breast ca. BT-549   5.6   5.1       Breast ca. MDA-N   0.0   0.0       Breast ca.* (pl. ef) T47D   0.1   0.1       Breast ca.* (pl. ef) MCF-7   0.0   0.0       Breast ca.* (pl. ef) MDA-MB-231   0.0   0.0       Small intestine   51.4   37.6       Colorectal   0.8   0.8       Colon ca. HT29   0.1   0.1       Colon ca. CaCo-2   0.5   0.3       Colon ca HCT-15   0.1   0.1       Colon ca. HCT-116   0.0   0.0       Colon ca. HCC-2998   0.3   0.2       Colon ca. SW480   0.0   0.0       Colon ca.* SW620 (SW480 met)   0.1   0.1       Stomach   8.8   20.4       Gastric ca. (liver met) NCI-N87   0.0   0.1       Heart   45.7   41.2       Skeletal muscle (Fetal)   24.0   27.4       Skeletal muscle   44.1   31.6       Endothelial cells   0.0   0.0       Heart (Fetal)   20.3   18.6       Kidney   13.5   11.0       Kidney (fetal)   27.2   16.2       Renal ca. 786-0   0.0   0.0       Renal ca. A498   0.0   0.1       Renal ca. ACHN   0.0   0.0       Renal ca TK-10   0.0   0.0       Renal ca. UO-31   0.1   0.0       Renal ca. RXF 393   0.0   0.0       Liver   5.3   3.5       Liver (fetal)   4.8   3.2       Liver ca. (hepatoblast) HepG2   0.0   0.0       Lung   4.8   4.9       Lung (fetal)   17.8   17.4       Lung ca. (non-s. cell) HOP-62   0.8   0.4       Lung ca. (large cell) NCI-H460   0.1   0.0       Lung ca. (non-s. cell) NCI-H23   0.2   0.2       Lung ca. (non-s. cl) NCI-H522   1.7   0.7       Lung ca. (non-sm. cell) A549   0.0   0.1       Lung ca. (s. cell var.) SHP-77   1.9   1.4       Lung ca. (small cell) LX-1   0.1   0.2       Lung ca. (small cell) NCI-H69   1.0   0.7       Lung ca. (squam.) SW 900   0.1   0.0       Lung ca. (squam.) NCI-H596   2.8   2.7       Lymph node   9.3   10.6       Spleen   3.2   3.3       Thymus   7.1   3.5       Ovary   23.0   22.1       Ovarian ca. IGROV-1   0.0   0.0       Ovarian ca. OVCAR-3   0.0   0.0       Ovarian ca. OVCAR-4   0.3   0.2       Ovarian ca. OVCAR-5   0.7   0.2       Ovarian ca. OVCAR-8   0.1   0.1       Ovarian ca.* (ascites) SK-OV-3   0.1   0.0       Pancreas   12.7   9.5       Pancreatic ca. CAPAN 2   0.0   0.0       Pituitary gland   4.5   1.8       Placenta   87.1   89.5       Prostate   11.1   5.1       Prostate ca.* (bone met) PC-3   0.2   0.2       Salivary gland   10.9   13.5       Trachea   17.1   8.9       Spinal cord   5.5   3.7       Testis   3.7   2.9       Thyroid   24.1   15.8       Uterus   19.6   9.4       Melanoma M14   0.0   0.0       Melanoma LOX IMVI   0.0   0.0       Melanoma UACC-62   0.0   0.0       Melanoma SK-MEL-28   0.0   0.0       Melanoma* (met) SK-MEL-5   0.0   0.0       Melanoma Hs688(A).T   69.7   66.0       Melanoma* (met) Hs688(B).T   100.0   95.9                    
     [0936]               TABLE AAG                          Panel 1.2                             Rel. Exp. (%)   Rel. Exp. (%)           Ag389, Run   Ag389, Run       Tissue Name   139735024   142359249                                 Endothelial cells   0.0   0.0       Heart (Fetal)   77.9   74.2       Pancreas   0.3   2.4       Pancreatic ca. CAPAN 2   0.0   0.0       Adrenal Gland   25.0   22.1       Thyroid   1.2   1.8       Salivary gland   12.2   20.0       Pituitary gland   1.1   2.5       Brain (fetal)   0.3   0.4       Brain (whole)   0.1   0.8       Brain (amygdala)   1.2   0.8       Brain (cerebellum)   0.2   0.9       Brain (hippocampus)   2.8   2.0       Brain (thalamus)   2.2   1.6       Cerebral Cortex   7.1   6.5       Spinal cord   0.8   1.0       glio/astro U87-MG   0.0   0.1       glio/astro U-118-MG   0.1   0.2       astrocytoma SW1783   1.6   1.6       neuro*; met SK-N-AS   63.3   62.4       astrocytoma SF-539   0.0   0.0       astrocytoma SNB-75   0.0   0.0       glioma SNB-19   0.0   0.0       glioma U251   0.0   0.0       glioma SF-295   0.0   0.0       Heart   85.3   82.9       Skeletal Muscle   33.0   40.6       Bone marrow   0.9   1.2       Thymus   1.5   1.1       Spleen   3.0   3.0       Lymph node   1.1   1.3       Colorectal Tissue   3.6   1.8       Stomach   3.1   5.7       Small intestine   45.1   44.1       Colon ca. SW480   0.0   0.0       Colon ca.* SW620 (SW480 met)   0.0   0.0       Colon ca. HT29   0.0   0.0       Colon ca. HCT-116   0.0   0.0       Colon ca. CaCo-2   0.1   0.2       Colon ca. Tissue (ODO3866)   6.8   5.2       Colon ca. HCC-2998   0.1   0.3       Gastric ca.* (liver met) NCI-N87   0.8   0.0       Bladder   37.4   29.5       Trachea   0.9   1.6       Kidney   19.8   20.2       Kidney (fetal)   13.3   22.1       Renal ca. 786-0   0.0   0.0       Renal ca. A498   0.0   0.0       Renal ca. RXF 393   0.0   0.0       Renal ca. ACHN   0.0   0.0       Renal ca. UO-31   0.0   0.1       Renal ca. TK-10   0.0   0.0       Liver   5.9   5.2       Liver (fetal)   5.4   4.2       Liver ca. (hepatoblast) HepG2   1.1   1.6       Lung   0.8   0.9       Lung (fetal)   3.3   2.7       Lung ca. (small cell) LX-1   0.1   0.1       Lung ca. (small cell) NCI-H69   0.8   0.8       Lung ca. (s. cell var.) SHP-77   1.3   1.1       Lung ca. (large cell) NCI-H460   0.0   0.0       Lung ca. (non-sm. cell) A549   0.0   0.0       Lung ca. (non-s. cell) NCI-H23   0.1   0.3       Lung ca. (non-s. cell) HOP-62   0.1   0.2       Lung ca. (non-s. cl) NCI-H522   1.2   1.7       Lung ca. (squam.) SW 900   0.0   0.0       Lung ca. (squam.) NCI-H596   3.0   2.8       Mammary gland   20.0   44.8       Breast ca.* (pl. ef) MCF-7   0.0   0.0       Breast ca.* (pl. ef) MDA-MB-231   0.0   0.0       Breast ca.* (pl. ef) T47D   0.0   0.1       Breast ca. BT-549   4.6   4.1       Breast ca. MDA-N   0.0   0.1       Ovary   48.3   42.3       Ovarian ca. OVCAR-3   0.0   0.0       Ovarian ca. OVCAR-4   0.4   0.4       Ovarian ca. OVCAR-5   0.3   0.7       Ovarian ca. OVCAR-8   0.0   0.1       Ovarian ca. IGROV-1   0.0   0.1       Ovarian ca. (ascites) SK-OV-3   0.0   0.0       Uterus   9.9   10.0       Placenta   8.0   24.7       Prostate   7.7   9.8       Prostate ca.* (bone met) PC-3   0.1   0.1       Testis   0.5   0.5       Melanoma Hs688(A).T   87.1   83.5       Melanoma* (met) Hs688(B).T   100.0   100.0       Melanoma UACC-62   0.0   0.0       Melanoma M14   0.0   0.0       Melanoma LOX IMVI   0.0   0.0       Melanoma* (met) SK-MEL-5   0.0   0.0                    
     [0937]               TABLE AAH                          Panel 2D                             Rel. Exp. (%)               Ag389, Run       Tissue Name   145188404                                 Normal Colon   26.2           CC Well to Mod Diff (ODO3866)   21.6       CC Margin (ODO3866)   15.6       CC Gr.2 rectosigmoid (ODO3868)   10.4       CC Margin (ODO3868)   3.3       CC Mod Diff (ODO3920)   2.8       CC Margin (ODO3920)   4.5       CC Gr.2 ascend colon (ODO3921)   13.0       CC Margin (ODO3921)   10.2       CC from Partial Hepatectomy (ODO4309) Mets   5.9       Liver Margin (ODO4309)   1.5       Colon mets to lung (OD04451-01)   8.5       Lung Margin (OD04451-02)   5.8       Normal Prostate 6546-1   9.5       Prostate Cancer (OD04410)   8.0       Prostate Margin (OD04410)   11.7       Prostate Cancer (OD04720-01)   5.5       Prostate Margin (OD04720-02)   12.6       Normal Lung 061010   12.7       Lung Met to Muscle (ODO4286)   2.6       Muscle Margin (ODO4286)   54.0       Lung Malignant Cancer (OD03126)   31.6       Lung Margin (OD03126)   7.3       Lung Cancer (OD04404)   10.4       Lung Margin (OD04404)   47.6       Lung Cancer (OD04565)   9.0       Lung Margin (OD04565)   5.0       Lung Cancer (OD04237-01)   7.3       Lung Margin (OD04237-02)   17.4       Ocular Mel Met to Liver (ODO4310)   0.6       Liver Margin (ODO4310)   0.7       Melanoma Mets to Lung (OD04321)   1.3       Lung Margin (OD04321)   12.5       Normal Kidney   14.4       Kidney Ca, Nuclear grade 2 (OD04338)   2.7       Kidney Margin (OD04338)   6.9       Kidney Ca Nuclear grade 1/2 (OD04339)   1.1       Kidney Margin (OD04339)   11.0       Kidney Ca, Clear cell type (OD04340)   19.9       Kidney Margin (OD04340)   11.8       Kidney Ca, Nuclear grade 3 (OD04348)   23.5       Kidney Margin (OD04348)   13.7       Kidney Cancer (OD04622-01)   24.0       Kidney Margin (OD04622-03)   2.6       Kidney Cancer (OD04450-01)   0.4       Kidney Margin (OD04450-03)   10.2       Kidney Cancer 8120607   7.1       Kidney Margin 8120608   13.6       Kidney Cancer 8120613   1.8       Kidney Margin 8120614   9.2       Kidney Cancer 9010320   64.2       Kidney Margin 9010321   16.6       Normal Uterus   16.2       Uterus Cancer 064011   17.9       Normal Thyroid   22.7       Thyroid Cancer 064010   6.6       Thyroid Cancer A302152   5.3       Thyroid Margin A302153   5.4       Normal Breast   32.1       Breast Cancer (OD04566)   6.0       Breast Cancer (OD04590-01)   26.6       Breast Cancer Mets (OD04590-03)   37.4       Breast Cancer Metastasis (OD04655-05)   8.4       Breast Cancer 064006   15.1       Breast Cancer 1024   26.6       Breast Cancer 9100266   16.8       Breast Margin 9100265   16.4       Breast Cancer A209073   32.1       Breast Margin A209073   27.7       Normal Liver   1.0       Liver Cancer 064003   0.5       Liver Cancer 1025   1.5       Liver Cancer 1026   13.0       Liver Cancer 6004-T   2.3       Liver Tissue 6004-N   3.5       Liver Cancer 6005-T   12.8       Liver Tissue 6005-N   1.5       Normal Bladder   14.2       Bladder Cancer 1023   6.9       Bladder Cancer A302173   4.8       Bladder Cancer (OD04718-01)   11.7       Bladder Normal Adjacent (OD04718-03)   100.0       Normal Ovary   19.6       Ovarian Cancer 064008   15.5       Ovarian Cancer (OD04768-07)   5.0       Ovary Margin (OD04768-08)   40.6       Normal Stomach   18.3       Gastric Cancer 9060358   9.9       Stomach Margin 9060359   7.9       Gastric Cancer 9060395   13.1       Stomach Margin 9060394   9.2       Gastric Cancer 9060397   13.3       Stomach Margin 9060396   3.6       Gastric Cancer 064005   9.7                    
     [0938]               TABLE AAI                          Panel 4D                             Rel. Exp. (%)   Rel. Exp. (%)           Ag389, Run   Ag389, Run       Tissue Name   139853806   140196439                                 Secondary Th1 act   0.0   0.0       Secondary Th2 act   0.0   0.0       Secondary Tr1 act   0.0   0.0       Secondary Th1 rest   0.0   0.0       Secondary Th2 rest   0.0   0.1       Secondary Tr1 rest   0.0   0.0       Primary Th1 act   0.0   0.0       Primary Th2 act   0.0   0.0       Primary Tr1 act   0.1   0.0       Primary Th1 rest   0.2   0.5       Primary Th2 rest   0.1   0.2       Primary Tr1 rest   0.6   0.5       CD45RA CD4 lymphocyte act   11.0   11.2       CD45RO CD4 lymphocyte act   0.1   0.1       CD8 lymphocyte act   0.8   0.7       Secondary CD8 lymphocyte rest   0.0   0.0       Secondary CD8 lymphocyte act   0.0   0.1       CD4 lymphocyte none   0.1   0.1       2ry Th1/Th2/Tr1_anti-CD95 CH11   0.0   0.1       LAK cells rest   0.1   0.1       LAK cells IL-2   0.1   0.2       LAK cells IL-2 + IL-12   0.1   0.3       LAK cells IL-2 + IFN gamma   0.2   0.2       LAK cells IL-2 + IL-18   0.1   0.4       LAK cells PMA/ionomycin   0.0   0.0       NK Cells IL-2 rest   0.1   0.1       Two Way MLR 3 day   0.2   0.3       Two Way MLR 5 day   0.1   0.2       Two Way MLR 7 day   0.1   0.1       PBMC rest   0.1   0.2       PBMC PWM   0.1   0.3       PBMC PHA-L   0.7   1.2       Ramos (B cell) none   0.0   0.0       Ramos (B cell) ionomycin   0.0   0.0       B lymphocytes PWM   0.1   0.2       B lymphocytes CD40L and IL-4   0.2   0.1       EOL-1 dbcAMP   0.1   0.0       EOL-1 dbcAMP PMA/ionomycin   0.1   0.0       Dendritic cells none   0.0   0.1       Dendritic cells LPS   0.0   0.0       Dendritic cells anti-CD40   0.0   0.0       Monocytes rest   0.0   0.0       Monocytes LPS   0.0   0.0       Macrophages rest   0.0   0.0       Macrophages LPS   0.0   0.0       HUVEC none   0.0   0.0       HUVEC starved   0.0   0.0       HUVEC IL-1beta   0.0   0.0       HUVEC IFN gamma   0.0   0.0       HUVEC TNF alpha + IFN gamma   0.0   0.0       HUVEC TNF alpha + IL4   0.0   0.0       HUVEC IL-11   0.0   0.0       Lung Microvascular EC none   0.0   0.0       Lung Microvascular EC TNFalpha +   0.0   0.0       IL-1beta       Microvascular Dermal EC none   0.0   0.0       Microsvasular Dermal EC TNF   0.0   0.0       alpha + IL-1beta       Bronchial epithelium TNFalpha +   0.0   0.0       IL1beta       Small airway epithelium none   0.2   0.5       Small airway epithelium TNF   0.0   0.0       alpha + IL-1beta       Coronery artery SMC rest   6.2   6.7       Coronery artery SMC TNF alpha +   6.0   4.4       IL-1beta       Astrocytes rest   0.3   0.4       Astrocytes TNFalpha + IL-1beta   1.1   1.5       KU-812 (Basophil) rest   0.0   0.0       KU-812 (Basophil) PMA/ionomycin   0.0   0.0       CCD1106 (Keratinocytes) none   0.0   0.0       CCD1106 (Keratinocytes)   0.0   0.0       TNFalpha + IL-1beta       Liver cirrhosis   0.8   0.7       Lupus kidney   0.7   1.0       NCI-H292 none   0.0   0.0       NCI-H292 IL-4   0.0   0.0       NCI-H292 IL-9   0.0   0.0       NCI-H292 IL-13   0.0   0.0       NCI-H292 IFN gamma   0.0   0.0       HPAEC none   0.0   0.0       HPAEC TNF alpha + IL-1 beta   0.0   0.0       Lung fibroblast none   24.3   25.7       Lung fibroblast TNF alpha + IL-1   3.8   5.4       beta       Lung fibroblast IL-4   22.5   31.2       Lung fibroblast IL-19   20.6   24.7       Lung fibroblast IL-13   41.2   59.0       Lung fibroblast IFN gamma   24.1   29.9       Dermal fibroblast CCD1070 rest   61.6   69.3       Dermal fibroblast CCD1070 TNF alpha   25.9   28.9       Dermal fibroblast CCD1070 IL-1 beta   55.1   42.6       Dermal fibroblast IFN gamma   51.1   42.3       Dermal fibroblast IL-4   100.0   100.0       IBD Colitis 2   0.0   0.1       IBD Crohn&#39;s   0.6   0.6       Colon   1.6   2.1       Lung   9.8   13.2       Thymus   1.0   1.4       Kidney   1.5   1.4                    
     [0939]               TABLE AAJ                          Panel 5 Islet                         Rel. Exp. (%)           Ag4808, Run       Tissue Name   259154757                             97457_Patient-02go_adipose   80.7       97476_Patient-07sk_skeletal muscle   22.4       97477_Patient-07ut_uterus   35.8       97478_Patient-07pl_placenta   12.9       99167_Bayer Patient 1   1.8       97482_Patient-08ut_uterus   32.8       97483_Patient-08pl_placenta   6.1       97486_Patient-09sk_skeletal muscle   3.3       97487_Patient-09ut_uterus   11.9       97488_Patient-09pl_placenta   8.3       97492_Patient-10ut_uterus   23.2       97493_Patient-10pl_placenta   15.0       97495_Patient-11go_adipose   6.9       97496_Patient-11sk_skeletal muscle   5.0       97497_Patient-11ut_uterus   27.4       97498_Patient-11pl_placenta   12.8       97500_Patient-12go_adipose   72.7       97501_Patient-12sk_skeletal muscle   22.2       97502_Patient-12ut_uterus   54.7       97503_Patient-12pl_placenta   3.5       94721_Donor 2 U - A_Mesenchymal Stem Cells   49.0       94722_Donor 2 U - B_Mesenchymal Stem Cells   46.7       94723_Donor 2 U - C_Mesenchymal Stem Cells   57.0       94709_Donor 2 AM - A adipose   46.0       94710_Donor 2 AM - B_adipose   46.0       94711_Donor 2 AM - C_adipose   41.5       94712_Donor 2 AD - A_adipose   30.6       94713_Donor 2 AD - B_adipose   53.6       94714_Donor 2 AD - C_adipose   49.0       94742_Donor 3 U - A_Mesenchymal Stem Cells   69.3       94743_Donor 3 U - B_Mesenchymal Stem Cells   82.4       94730_Donor 3 AM - A_adipose   100.0       94731_Donor 3 AM - B_adipose   67.8       94732_Donor 3 AM - C_adipose   80.1       94733_Donor 3 AD - A_adipose   85.9       94734_Donor 3 AD - B_adipose   69.7       94735_Donor 3 AD - C_adipose   62.4       77138_Liver_HepG2untreated   4.8       73556_Heart_Cardiac stromal cells (primary)   0.0       81735_Small Intestine   9.4       72409_Kidney_Proximal Convoluted Tubule   0.0       82685_Small intestine_Duodenum   0.9       90650_Adrenal_Adrenocortical adenoma   3.9       72410_Kidney_HRCE   0.0       72411_Kidney_HRE   0.1       73139_Uterus_Uterine smooth muscle cells   28.1                    
     [0940] AI_comprehensive panel_v1.0 Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0941] General_screening_panel_v1.4 Summary: Ag4808 Highest expression of this gene is detected in melanoma Hs688(B).T cell line (CT=26.7). In addition, high to moderate expression of this is also seen in colon cancer, melanoma melanoma Hs688(A).T cell line, and cell lines derived from brain, liver, lung and breast cancers. This gene codes for endosialin (TEM1) protein, a cell surface glycoprotein identified with monoclonal antibody FB5. It is a highly expressed by tumor blood vessel endothelium in a broad range of human cancers but not detected in blood vessels or other cell types in many normal tissues (Carson-Walter et al., 2001, Cancer Res 61(18):6649-55, PMID: 11559528; Christian et al., 2001, J Biol Chem 276(10):7408-14, PMID: 11084048). Therefore, therapeutic modulation of the protein encoded by this gene through the use of antibody or small molecule drug, may be beneficial in the treatment of these cancers.  
     [0942] Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adipose, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, fetal liver and the gastrointestinal tract. Therefore, therapeutic modulation of the activity of this gene may prove useful in the treatment of endocrine/metabolically related diseases, such as obesity and diabetes.  
     [0943] Interestingly, this gene is expressed at much higher levels in fetal (CT=31.2) when compared to adult liver (CT=37.9). This observation suggests that expression of this gene can be used to distinguish fetal from adult liver. In addition, the relative overexpression of this gene in fetal skeletal muscle suggests that the protein product may enhance liver growth or development in the fetus and thus may also act in a regenerative capacity in the adult. Therefore, therapeutic modulation of the TEM1 encoded by this gene could be useful in treatment of liver related diseases.  
     [0944] In addition, this gene is expressed at moderate to low levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Therefore, therapeutic modulation of this gene product may be useful in the treatment of central nervous system disorders such as Alzheimer&#39;s disease, Parkinson&#39;s disease, epilepsy, multiple sclerosis, schizophrenia and depression.  
     [0945] General_screening_panel_v1.5 Summary: Ag4834 Expression of the CG95205-02 gene (Runs 228726951 and 228783170) is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0946] HASS Panel v1.0 Summary: Ag389 Highest expression of this gene is detected in primary melanocytes A5 (CT=29.5). Moderate levels of expression of this gene is detected in a sample of brain cancer, as well as, in cultured primary melanocytes and astrocytes.  
     [0947] Oncology_cell_line_screening_panel_v3.1 Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0948] Panel 1.1 Summary: Ag4808 Two experiment with same probe and primer sets are in excellent agreement. Highest expression of this gene is detected in melanoma Hs688(B).T and neuronial metastatic SK-N-AS cell lines (CTs=22-24). In addition, high to moderate expression of this is also seen in colon cancer, melanoma melanoma Hs688(A).T cell line, and cell lines derived from brain, liver, lung and breast cancers. Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, fetal liver and the gastrointestinal tract. In addition, this gene is expressed at moderate to low levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Please see panel 1.4 for discussion on utility of this gene.  
     [0949] Panel 1.2 Summary: Ag389 Two experiment with same probe and primer sets are in excellent agreement. Highest expression of this gene is detected in melanoma Hs688(B).T (CTs=25). In addition, high to moderate expression of this is also seen in colon cancer, melanoma melanoma Hs688(A).T cell line, and cell lines derived from brain, liver, lung and breast cancers Among tissues with metabolic or endocrine function, this gene is expressed at moderate levels in pancreas, adrenal gland, thyroid, pituitary gland, skeletal muscle, heart, fetal liver and the gastrointestinal tract. In addition, this gene is expressed at moderate to low levels in all regions of the central nervous system examined, including amygdala, hippocampus, substantia nigra, thalamus, cerebellum, cerebral cortex, and spinal cord. Please see panel 1.4 for discussion on utility of this gene.  
     [0950] Results from two experiments (Runs 138522289 and 138564094) with this gene are not included. The amp plot indicates that there were experimental difficulties with this run.  
     [0951] Panel 2D Summary: Ag389 Highest expression of this gene is detected in normal bladder (CT=30). Moderate to low expression of this gene is seen in both normal and cancer samples derived from colon, stomach, ovary, bladder, liver, thyroid, uterus, kidney, lung, and prostate. Therefore, therapeutic modulation of the protein encoded by this gene through the use of antibody or small molecule drug, may be beneficial in the treatment of these cancers. Please see panel 1.4 for more discussion.  
     [0952] Panel 4.1D Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     [0953] Panel 4D Summary: Ag389 Two experiment with same probe and primer sets are in excellent agreement. Highest expression of this gene is detected in IL-4 treated dermal fibroblast (CTs=27.4). In addition, high to moderate expression of this gene is seen in lung and dermal fibroblasts, coronary artery SMC, PHA-L activated PBMC cells, and normal tissues represented by colon, lung, thymus and kidney. Moderate expression of this gene is also detected in CD45RA CD4 lymphocytes, which represents activated naive T cells. Interestingly, the expression of this gene is strongly down regulated in activated memory T cells (CD45RO CD4 lymphocyte) or CD4 Th1 or Th2 cells, resting CD4 cells (CTs&gt;35), suggesting a role for this putative protein in differentiation or activation of naive T cells. Therefore, modulation of the expression and/or activity of this putative protein encoded by this gene might be beneficial for the control of autoimmune diseases and T cell mediated diseases such as arthritis, IBD, asthma, COPD and skin disorders such as psoriasis and emphysema.  
     [0954] Panel 5 Islet Summary: Ag4808 Highest expression of this gene is detected in midway differentiated adipose (CT=28.3). Moderate to low expression of this gene is also seen in differentiated adipocytes and undifferentiated mesenchymal cells, skeletal muscle, islet cells, small intestine, placenta and uterus. Please see panel 1.4 for further discussion on the utility of this gene.  
     [0955] General oncology screening panel_v — 2.4 Summary: Ag4834 Expression of the CG95205-02 gene is low/undetectable (CTs&gt;35) across all of the samples on this panel.  
     Example D  
     [0956] Identification of Single Nucleotide Polymorphisms in NOVX Nucleic Acid Sequences  
     [0957] Variant sequences are also included in this application. A variant sequence can include a single nucleotide polymorphism (SNP). A SNP can, in some instances, be referred to as a “CSNP” to denote that the nucleotide sequence containing the SNP originates as a cDNA. A SNP can arise in several ways. For example, a SNP may be due to a substitution of one nucleotide for another at the polymorphic site. Such a substitution can be either a transition or a transversion. A SNP can also arise from a deletion of a nucleotide or an insertion of a nucleotide, relative to a reference allele. In this case, the polymorphic site is a site at which one allele bears a gap with respect to a particular nucleotide in another allele. SNPs occurring within genes may result in an alteration of the amino acid encoded by the gene at the position of the SNP. Intragenic SNPs may also be silent, when a codon including a SNP encodes the same amino acid as a result of the redundancy of the genetic code. SNPs occurring outside the region of a gene, or in an intron within a gene, do not result in changes in any amino acid sequence of a protein but may result in altered regulation of the expression pattern. Examples include alteration in temporal expression, physiological response regulation, cell type expression regulation, intensity of expression, and stability of transcribed message.  
     [0958] SeqCalling assemblies produced by the exon linking process were selected and extended using the following criteria. Genomic clones having regions with 98% identity to all or part of the initial or extended sequence were identified by BLASTN searches using the relevant sequence to query human genomic databases. The genomic clones that resulted were selected for further analysis because this identity indicates that these clones contain the genomic locus for these SeqCalling assemblies. These sequences were analyzed for putative coding regions as well as for similarity to the known DNA and protein sequences. Programs used for these analyses include Grail, Genscan, BLAST, HMMER, FASTA, Hybrid and other relevant programs.  
     [0959] Some additional genomic regions may have also been identified because selected SeqCalling assemblies map to those regions. Such SeqCalling sequences may have overlapped with regions defined by homology or exon prediction. They may also be included because the location of the fragment was in the vicinity of genomic regions identified by similarity or exon prediction that had been included in the original predicted sequence. The sequence so identified was manually assembled and then may have been extended using one or more additional sequences taken from CuraGen Corporation&#39;s human SeqCalling database. SeqCalling fragments suitable for inclusion were identified by the CuraTools™ program SeqExtend or by identifying SeqCalling fragments mapping to the appropriate regions of the genomic clones analyzed.  
     [0960] The regions defined by the procedures described above were then manually integrated and corrected for apparent inconsistencies that may have arisen, for example, from miscalled bases in the original fragments or from discrepancies between predicted exon junctions, EST locations and regions of sequence similarity, to derive the final sequence disclosed herein. When necessary, the process to identify and analyze SeqCalling assemblies and genomic clones was reiterated to derive the full length sequence (Alderborn et al., Determination of Single Nucleotide Polymorphisms by Real-time Pyrophosphate DNA Sequencing. Genome Research. 10 (8) 1249-1265, 2000).  
     [0961] Variants are reported individually but any combination of all or a select subset of variants are also included as contemplated NOVX embodiments of the invention. Ps NOV1a SNP Data:  
     [0962] Four ploymorphic variants of NOV1a have been identified and are shown in Table D1.  
                           TABLE D1                                      Nucleotides   Amino Acids                                             Base           Base                   Position   Wild-       Position   Wild-       Variant   of SNP   type   Variant   of SNP   type   Variant                                                 13379739   743   C   G   215   Arg   Gly       13379740   910   C   T   270   Ala   Ala       13379741   975   G   A   292   Gly   Asp       13379738   1500   T   C   467   Val   Ala                  
 
     [0963] NOV4a SNP Data:  
     [0964] Two polymorphic variants of NOV4a have been identified and are shown in Table D2.  
                           TABLE D2                                      Nucleotides   Amino Acids                                             Base           Base                   Position   Wild-       Position   Wild-       Variant   of SNP   type   Variant   of SNP   type   Variant                                                 13379812   153   G   C   32   Gly   Ala       13379809   954   C   T   0                  
 
     [0965] NOV5a SNP Data:  
     [0966] Two polymorphic variants of NOV5a have been identified and are shown in Table D3.  
                           TABLE D3                                      Nucleotides   Amino Acids                                             Base           Base                   Position   Wild-       Position   Wild-       Variant   of SNP   type   Variant   of SNP   type   Variant                                                 13379756   409   C   T   60   His   His       13379755   966   G   T   246   Gly   Val                  
 
     [0967] NOV6a SNP Data:  
     [0968] One polymorphic variant of NOV6a has been identified and is shown in Table D4.  
                           TABLE D4                                      Nucleotides   Amino Acids                                             Base           Base                   Position   Wild-       Position   Wild-       Variant   of SNP   type   Variant   of SNP   type   Variant               13378086   216   G   A   52   Ala   Thr                  
 
     [0969] NOV7a SNP Data:  
     [0970] Two polymorphic variants of NOV7a were identified and are shown in Table D5.  
                           TABLE D5                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379781   534   A   G   173   Gly   Gly       13379782   715   G   A   234   Ala   Thr                  
 
     [0971] NOV9a SNP Data:  
     [0972] One polymorphic variant of NOV9a has been identified and is shown in Table D6.  
                           TABLE D6                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379810   84   G   A   28   Lys   Lys                  
 
     [0973] NOV10a SNP Data:  
     [0974] Four polymorphic variants of NOv10a have been identified and are shown in Table D7.  
                           TABLE D7                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant                                                 13379776   3528   C   T   1150   Pro   Ser       13379775   3619   T   C   1180   Leu   Pro       13379785   4588   T   G   0       13379813   5742   A   G   0                  
 
     [0975] NOV11a SNP Data:  
     [0976] One polymorphic variant of NOV11a has been identified and is shown in Table D8.  
                           TABLE D8                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379811   62   C   T   21   Pro   Leu                  
 
     [0977] NOV12a SNP Data:  
     [0978] Two polymorphic variants of NOV12a have been identified and are shown in Table D9.  
                           TABLE D9                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13377332   461   T   C   145   Leu   Pro       13377331   473   T   C   149   Leu   Pro                  
 
     [0979] NOV13a SNP Data:  
     [0980] One polymorphic variant of NOV13a has been identified and is shown in Table D10.  
                           TABLE D10                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379842   236   T   C   79   Val   Ala                  
 
     [0981] NOV14a SNP Data:  
     [0982] Four polymorphic variants of NOV14a have been identified and are shown in Table D11.  
                           TABLE D11                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant                                                 13379829   14   T   C   0               13379827   124   C   T   37   Pro   Leu       13379825   576   C   T   188   Leu   Phe       13379824   675   C   T   221   Leu   Leu                  
 
     [0983] NOV15a SNP data:  
     [0984] Ten polymorphic variants of NOV15a have been identified and are shown in Table D12.  
                           TABLE D12                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant                                                 13379865   1039   A   G   290   Gly   Gly       13379864   1884   T   C   572   Val   Ala       13379863   3619   G   C   1150   Leu   Leu       13379860   7248   T   C   2360   Leu   Pro       13379859   7505   C   A   2446   Leu   Ile       13379858   8017   G   A   2616   Lys   Lys       13379857   8237   A   T   2690   Met   Leu       13379856   8515   T   C   2782   His   His       13379867   8611   G   A   2814   Pro   Pro       13379868   8689   T   C   2840   Phe   Phe                  
 
     [0985] NOV16a SNP data:  
     [0986] One polymorphic variant of NOV16a has been identified and is shown in Table D13.  
                           TABLE D13                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379817   1300   A   G   427   Ser   Gly                  
 
     [0987] NOV22a SNP data:  
     [0988] One polymorphic variant of NOV22a has been identified and is shown in Table D14.  
                           TABLE D14                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379940   1864   A   G   0                  
 
     [0989] NOV25a SNP data:  
     [0990] One polymorphic variant of NOV25a has been identified and is shown in Table D15.  
                           TABLE D15                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379938   994   T   C   332   Cys   Arg                  
 
     [0991] NOV27a SNP data:  
     [0992] Five polymorphic variants of NOV27a have been identified and are shown in Table D16.  
                           TABLE D16                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant               13379875   1309   T   C   403   Asn   Asn       13379874   1709   G   A   537   Asp   Asn       13379873   1713   A   G   538   Lys   Arg       13379872   1777   T   C   559   Asn   Asn       13379871   1843   C   T   581   Asp   Asp                  
 
     [0993] NOV28a SNP data:  
     [0994] Four polymorphic variants of NOV28a have been identified and are shown in Table D17.  
                           TABLE D17                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant                                                 13379839   248   C   T   78   Leu   Leu       13379838   880   C   T   288   Asn   Asn       13379837   883   C   G   289   Thr   Thr       13379836   1078   G   T   354   Val   Val                  
 
     [0995] NOV32a SNP data:  
     [0996] Eleven polymorphic variants of NOV32a have been identified and are shown in D18.  
                           TABLE D18                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant                                                 13378189   33   G   T   11   Leu   Leu       13378332   68   A   G   23   His   Arg       13375660   197   T   C   66   Ile   Thr       13376793   266   T   C   89   Leu   Pro       13379841   699   T   C   233   Phe   Phe       13375659   833   T   C   278   Phe   Ser       c110.5826   1145   G   C   382   Ser   Thr       c110.6324   1146   C   G   382   Ser   Arg       13377867   1193   G   A   398   Arg   Gln       13376792   1247   T   C   416   Leu   Pro       13374618   1264   G   A   422   Val   Ile                  
 
     [0997] NOV40a SNP data:  
     [0998] Two polymorphic variants of NOV40a have been identified and are shown in Table D19.  
                           TABLE D19                                      Nucleotides   Amino Acids                                             Base           Base                   Position           Position           of   Wild-       of   Wild-       Variant   SNP   type   Variant   SNP   type   Variant                                                 13379845   722   C   T   239   Asn   Asn       13379846   1298   C   T   431   Pro   Pro                  
 
     Example E  
     [0999] Each of the clones listed below is related to a clone or family of clones listed in Example A. The relationship is identifiable as the clone listed below will have the same NOVX number as the clones to which it is related. For example, NOV30g below is related to the NOV30 family of Example A.  
     [1000] The NOV30g and NOV30h clones were analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E1.  
                               TABLE E1                                      SEQ ID NO: 111   728 bp                             NOV30g,   AGTCTTGCCTTCTTTTGAGCCTAAGTCATGAGTTGGATGTTCCTCAGAGATCTCCTGAGT           CG56315-01       DNA Sequence   GGAGTAAATAAATACTCCACTGGGACTGGATGGATTTGGCTGGCTGTCGTGTTTGTCTTC                   CGTTTGCTGGTCTACATGGTGGCAGCAGAGCACGTGTGGAAAGATGAGCAGAAAGAGTTT                   GAGTGCAACAGTAGACAGCCCGGTTGCAAAAATGTGTGTTTTGATGACTTCTTCCCCATT                   TCCCAAGTCAGACTTTGGGCCTTACAACTGATAATGGTCTCCACACCTTCACTTCTGGTG                   GTTTTACATGTAGCCTATCATGAGGGTAGAGAGAAAAGGCACAGAAAGAAACTCTATGTC                   AGCCCAGGTACAATGGATGGGGGCCTATGGTACGCTTATCTTATCAGCCTCATTGTTAAA                   ACTGGTTTTGAAATTGGCTTCCTTGTTTTATTTTATAAGCTATATGATGGCTTTAGTGTT                   CCCTACCTTATAAAGTGTGATTTGAAGCCTTGTCCCAACACTGTGGACTGCTTCATCTCC                   AAACCCACTGAGAAGACGATCTTCATCCTCTTCTTGGTCATCACCTCATGCTTGTGTATT                   GTGTTGAATTTCATTGAACTGAGTTTTTTGGTTCTCAAGTGCTTTATTAAGTGCTGTCTC                   CAAAAATATTTAAAAAAACCTCAAGTCCTCAGTGTGTGAGTGCCACAGCCTCAGATATGT                   TGAATGTG                                         SEQ ID NO: 112   223 aa                             NOV30g,   MSWMFLRDLLSGVNKYSTGTGWIWLAVVFVFRLLVYMVAAEHVWKDEQKEFECNSRQPGC           CG56315-01       Protein Sequence   KNVCFDDFFPISQVRLWALQLIMVSTPSLLVVLHVAYHEGREKRHRKKLYVSPGTMDGGL                   WYAYLISLIVKTGFEIGFLVLFYKLYDGFSVPYLIKCDLKPCPNTVDCFISKPTEKTIFI                   LFLVITSCLCIVLNFIELSFLVLKCFIKCCLQKYLKKPQVLSV                                         SEQ ID NO: 113   727 bp                             NOV30h,   AGTCTTGCTTCTTTTGAGCCTAAGTCATGAGTTGGATGTTCCTCAGAGATCTCCTGAGTG           CG56315-02       DNA Sequence   GAGTAAATAAATACTCCACTGGGATTGGATGGATTTGGCTGGCTGTCGTGTTTGTCTTCC                   GTTTGCTGGTCTACATGGTGGCAGCAGAGCACGTGTGGAAAGATGAGCAGAAAGAGTTTG                   AGTGCAACAGTAGACAGCCCGGTTGCAAAAATGTGTGTTTTGATGACTTCTTCCCCATTT                   CCCAAGTCAGACTTTGGGCCTTACAACTGATAATGGTCTCCACACCTTCACTTCTGGTGG                   TTTTACATGTAGCCTATCATGAGGGTAGAGAGAAAAGGCACAGAAAGAAACTCTATGTCA                   GCCCAGGTACAATGGATGGGGGCCTATGGTACGCTTATCTTATCAGCCTCATTGTTAAAA                   CTGGTTTTGAAATTGGCTTCCTTGTTTTATTTTATAAGCTATATGATGGCTTTAGTGTTC                   CCTACCTTATAAAGTGTGATTTGAAGCCTTGTCCCAACACTGTGGACTGCTTCATCTCCA                   AACCCACTGAGAAGACGATCTTCATCCTCTTCTTGGTCATCACCTCATGCTTGTGTATTG                   TGTTGAATTTCATTGAACTGAGTTTTTTGGTTCTCAAGTGCTTTATTAAGTGCTGTCTCC                   AAAAATATTTAAAAAAACCTCAAGTCCTCAGTGTGTGAGTGCCACAGCCTCAGATATGTT                   GAATGTG                                         SEQ ID NO: 114   223 aa                             NOV30h,   MSWMFLRDLLSGVNKYSTGIGWIWLAVVFVFRLLVYMVAAEHVWKDEQKEFECNSRQPGC           CG56315-02       Protein Sequence   KNVCFDDFFPISQVRLWALQLIMVSTPSLLVVLHVAYHEGREKRHRKKLYVSPGTMDGGL                   WYAYLISLIVKTGFEIGFLVLFYKLYDGFSVPYLIKCDLKPCPNTVDCFISKPTEKTIFI                   LFLVITSCLCIVLNFIELSFLVLKCFIKCCLQKYLKKPQVLSV                  
 
     [1001] The NOV33g clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E2.  
                               TABLE E2                                      SEQ ID NO: 147   1120 bp                             NOV33g   GAGGCCATGCCCGCTTCCTCTCTTCCAGGAAAGCTCTGGTTCGTCCTCACGATGCTGCTG           CG57658-01       DNA Sequence   CGGATGCTGGTGATTGTCTTGGCGGGGCGACCCGTCTACCAGGACGAGCAGGAGAGGTTT                   GTCTGCAACACGCTGCAGCCGGGATGCGCCAATGTTTGCTACGACGTCTTCTCCCCCGTG                   TCTCACCTGCGGTTCTGGCTGATCCAGGGCGTGTGCGTCCTCCTCCCCTCCGCCGTCTTC                   AGCGTCTATGTCCTGCACCGAGGAGCCACGCTCGCCGCGCTGGGCCCCCGCCGCTGCCCC                   GACCCCCGGGAGCCGGCCTCCGGGCAGAGACGCTGCCCGCGGCCATTCGGGGAGCGCGGC                   GGCCTCCAGGTGCCCGACTTTTCGGCCGGCTACATCATCCACCTCCTCCTCCGGACCCTG                   CTGGAGGCAGCCTTCGGGGCCTTGCACTACTTTCTCTTTGGATTCCTGGCCCCGAAGAAG                   TTCCCTTGCACGCGCCCTCCGTGCACGGGCGTGGTGGACTGCTACGTGTCGCGGCCCACA                   GAGAAGTCCCTGCTGATGCTGTTCCTCTGGGCGGTCAGCGCGCTGTCTTTTCTGCTGGGC                   CTCGCCGACCTGGTCTGCAGCCTGCGGCGGCGGATGCGCAGGAGGCCGGGACCCCCCACA                   AGCCCCTCCATCCGGAAGCAGAGCGGAGCCTCAGGCCACGCGGAGGGACGCCGGACTGAC                   GAGGAGGGTGGGCGGGAGGAAGAGGGGGCACCGGCGCCCCCGGGTGCACGCGCCGGAGGG                   GAGGGGGCTGGCAGCCCCAGGCGTACATCCAGGGTGTCAGGGCACACGAAGATTCCGGAT                   GAGGATGAGAGTGAGGTGACATCCTCCGCCAGCGAAAAGCTGGGCAGACAGCCCCGGGGC                   AGGCCCCACCGAGAGGCCGCCCAGGACCCCAGGGGCTCAGGATCCGAGGAGCAGCCCTCA                   GCAGCCCCCAGCCGCCTGGCCGCGCCCCCTTCCTGCAGCAGCCTGCAGCCCCCTGACCCG                   CCTGCCAGCTCCAGTGGTGCTCCCCACCTGAGAGCCAGGAAGTCTGAGTGGGTGTGAAAA                   AAACAGCACCTGGCGGTGCCCCGGGGCTCACGCCTGTAAT                                         SEQ ID NO: 148   356 aa                             NOV33g,   MPASSLPGKLWFVLTMLLRMLVIVLAGRPVYQDEQERFVCNTLQPGCANVCYDVFSPVSH           CG57658-01       Protein Sequence   LRFWLIQGVCVLLPSAVFSVYVLHRGATLAALGPRRCPDPREPASGQRRCPRPFGERGGL                   QVPDFSAGYIIHLLLRTLLEAAFGALHYFLFGFLAPKKFPCTRPPCTGVVDCYVSRPTEK                   SLLMLFLWAVSALSFLLGLADLVCSLRRRMRRRPGPPTSPSIRKQSGASGHAEGRRTDEE                   GGREEEGAPAPPGARAGGEGAGSPRRTSRVSGHTKIPDEDESEVTSSASEKLGRQPRGRP                   HREAAQDPRGSGSEEQPSAAPSRLAAPPSCSSLQPPDPPASSSGAPHLRARKSEWV                  
 
     [1002] The NOV34b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E3.  
                               TABLE E3                                      SEQ ID NO: 151   1400 bp                             NOV34b,   ATTCTCCCCAAACGCCAGGGATGGGGGTCATGGCTCCCCGAACCCTCCTCCTGCTGCTCT           CG57664-01       DNA Sequence   TGGGGGCCCTGGCCCTGACCGAGACCTGGGCCGGTGAGTGCGGGGTCGGGAGGGAAAGGG                   CCTCTGCGGGGAGAAGCGAGTGGCCCGCCCGGCCCGGGGAGCCGCGCCTCAGCCTCTCCT                   CGCCTCCAGGCTCCCACTCCTTGAGGTATTTCAGCACCGCAGTGTCCCAGCCCGGCCGCG                   GGGAGCCCCGGTTCATCGCCGTGGGCTACGTGGACGACACAGAGTTCGTGCGGTTCGACA                   GCGACTCCGTGAGTCCGAGGATGGAGCGGCGGGCGCCGTGGGTGGAGCAGGAGGGGCTGG                   AGTATTGGGACCAGGAGACACGGAACGCCAAGGGCCACGCGCAGATTTACCGAGTGAACC                   TGCGGACCCTGCTCCGCTATTACAACCAGAGCGAGGCCGGTGGTTCTCACACCATCCAGA                   GGAAGCATGACTGCGACGTGGGCCCGACAGGCGGGCCCGACAGGCGCCTCCTCCGCAGGT                   ATGAACAGTTCGCCTACGATGGCAAGGATTACATCGCCCTGAACGAGGACCTGCCCTCCT                   GGACCGCCGCGAACACAGCGGCTCAGATCTCCCAGCACAAGTGGGAAGCGGACAAATACT                   CAGAGCAGGTCAGGGCCTACCTGAGGGCAAGTGCATGGAGTGGCGAGGGCAAGTGCATGG                   AGTGGCTCCGCAGACACCTGGAGAACGGGAAGGAGACGCTGCAGCGCGCGTCAGATCCCC                   CAAAGGCACATGTGACCCAGCACCCCGTCTCTGACCATGAGGCCACCCTTGAGGTGCTGG                   GCCCTGGGCCTCTACCCTTGAGGTGCTGGGCCCTGGGCCTCTACCCTGCGGAGATCACAC                   TGACCTGGCAGCAGGATGGGGAGGACCAGACCCAGGACACGGAGCTTGTGGAGACCAGGC                   CTGCAGGGGACGGAACCTTCCAGAAGTGGGTGGCTGTAGTGGTGCCTTCCGGAGAGGAGC                   AGAGATACATGTGCCATGTGCAGCATGAGGGGCTGCCAGAGCCCCTCACCCTGAGATGGC                   CCTCACCTCCCTCTCCTTTCCCAGAGCCGTCTTCTCAGCCCACCATCCCCATCGTGGGCA                   TCGTTGCTGGCCTGTTTCTCCTTGGAGCTGTGGTCACTGGAGCTGTGGTTGCTGCTGTGA                   TGAAGAGGAAGAAAAGCTCAGGTAGGGAAGGGGTGAGAGGTGGGATCTGGGTTTTCTTGT                   TCCACTGTGGGTTTCAAGCCACAGGTAGAATTGTGACTTGCTTCATCACTGGGAAGCACC                   GTCCACACACAGGCCGACCTAGCCTGGGGCCCTGTGTGCCAACACTTGCTCTTTTGTGAA                   GCACATGTGAAAACGAAGGA                                         SEQ ID NO: 152   452 aa                             NOV34b,   MGVMAPRTLLLLLLGALALTETWAGECGVGRERASAGRSEWPARPGEPRLSLSSPPGSHS           CG57664-01       Protein Sequence   LRYFSTAVSQPGRGEPRFIAVGYVDDTEFVRFDSDSVSPRMERPAPWVEQEGLEYWDQET                   RNAKGHAQIYRVNLRTLLRYYNQSEAGGSHTIQRKHDCDVGPTGGPDRRLLRRYEQFAYD                   GKDYIALNEDLPSWTAANTAAQISQHKWEADKYSEQVRAYLRASAWSGEGKCMEWLRRHL                   ENGKETLQRASDPPKAHVTQHPVSDHEATLEVLGPGPLPLRCWALGLYPAEITLTWQQDG                   EDQTQDTELVETRPAGDGTFQKWVAVVVPSGEEQRYMCHVQHEGLPEPLTLRWPSPPSPF                   PEPSSQPTIPIVGIVAGLFLLGAVVTGAVVAAVMKRKKSSGREGVRGGIWVFLFHCGFQA                   TGRIVTCFITGKHRPHTGRPSLGPCVPTLALL                  
 
     [1003] The NOV35b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E4.  
                               TABLE E4                                      SEQ ID NO: 155   1159 bp                             NOV35b,   TCTCCCCAGACGCCGAGGATGGTGCTCATGGCGCCCCGAACCCTCCTCCTGCTGCTCTCA           CG57668-01       DNA Sequence   GGGGCCCTGACCCAGACCTGGGCGCGTTCCCACTCCATGAGGTATTTCTACACCACCATG                   TCCCGGCCCGGCCGCGGGGAGCCCCGCTTCATCTCCGTCGGCTACGTGGACTATACGCAG                   TTCGTGCGGTTCGACAGCGACGACGCGAGTCCGAGAGAGGAGCCGCGGGCGCCGTGGATG                   GAGCGGGAGGGGCCGGAGTATTGGGACCGGAACACACAGATCTGCAAGGCCCAAGCACGG                   ACTGAACGAGAGAACCTGCGGATCGCGCTCCGCTACTACAACCAGAGCGAGGGCGGTGGT                   TCCCACACCATGCAGGTGATGTATGGCTGCGACGTGGGGCCCGACGGGCGCTTCCTCCGC                   GGGTATGAACAGCACGCCTACGACGGCAAGGATTACATCGCTCTGAACGAGGACCTGCGC                   TCCTGGACCGCGGCGGACATGGCAGCTCAGATCACCAAGCGCAAGTGGGAGGCGGCCCGT                   GTGGCGGAGCAGCTGAGAGCCTACCTGGAGGGCGAGTTCGTGGAGTGGCTCCGCAGATAC                   CTGGAGAACGGGAAGGAGACGCTGCAGCGCGCGTCAGACCCCCCCAAGACACATATGACC                   CACTACCCCATCTCTGACCATGAGGCCACCCTGAGGTGCTGGGCCCTGGGCTTCTACCCT                   GCGGAGATCACACTGACCTGGCAGCGGGATGGGGAGGACCAGACCACGGAGCTCGTGGAG                   ACCAGGCCTGCAGGGGATGGAACCTTCCAGAAGTGGGCGGCTGTGGTGGTGCCTTCTGGA                   GAGGAGCAGAGATACACCTGCCATGTGCAGCATGAGGGTCTGCCCGAGCCCCTCACCCTG                   AGATGGCAGGGTCAGGGTCCCTCACCTTCCCCCCTTTTCCCAGAGCCATCTTCCCAGCCC                   ACCATCCCCATCGTGGGCATCATTGCTGGCCTGGTTCTACTTGTAGCTGTGGTCACTGGA                   GCTGTGGTCACTGCTGTAATGTGGAGGAAGAAGAGCTCAGGTAAGGAAGGGGATGGGTAT                   TCTACTCCAGGCGGCAACAGTGCCCAGGGCTCTGATGTGTCTCTCACGGCGTGAAAGGTG                   AGACCTTGGGGGGCCTGAT                                         SEQ ID NO: 156   371 aa                             NOV35b,   MVLMAPRTLLLLLSGALTQTWARSHSMRYFYTTMSRPGRGEPRFISVGYVDYTQFVRFDS           CG57668-01       Protein Sequence   DDASPREEPRAPWMEREGPEYWDRNTQICKAQARTERENLRIALRYYNQSEGGGSHTMQV                   MYGCDVGPDGRFLRGYEQHAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAARVAEQLR                   AYLEGEFVEWLRRYLENGKETLQRASDPPKTHMTHYPISDHEATLRCWALGFYPAEITLT                   WQRDGEDQTTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWQGQG                   PSPSPLFPEPSSQPTIPIVGIIAGLVLLVAVVTGAVVTAVMWRKKSSGKEGDGYSTPGGN                   SAQGSDVSLTA                  
 
     [1004] The NOV36b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E5.  
                               TABLE E5                                      SEQ ID NO: 159   1210 bp                             NOV36b,   TCGCTCACCCACCCGGACTCATTCTCCCCAGACGCCAAGGATGGTGGTCATGGCACCCCG           CG59256-01       DNA Seuence   AACCCTCTTCCTGCTACTCTCGGGGGCCCTGACCCTGACCGAGACCTGGGCGGGCTCCCA                   CTCCATGAGGTATTTCAGCGCCGCCGTGTCCCGGCCCGCCCGCCGGGAGCCCCGCTTCAT                   CGCCATGGGCTACGTGGACGACACGCAGTTCGTGCGGTTCGACAGCGACTCGGCGTGTCC                   GAGGATGGAGCCGCGGGCGCCGTGGGTGGAGCAGGAGGGGCCAGAGTATTGGGAAGAGGA                   GACACGGAACACCAAGGCCCACGCACAGACTGACAGAATGAACCTGCAGACCCTGCGCGG                   CTACTACAACCAGAGCGAGGGGGTGGGGCCAGGTTCTCATACCCTCCAGTGGATGATTGG                   CTGCGACCTGGGGTCCGACGGACGCCTCCTCCGCGGGTATGAACAGTATGCCTACGATGG                   CAAGGATTACCTCGCCCTGAACGAGGACCTGCGCTCCTGGACCGCACCGGACACTGCGGC                   TCAGATCTCCAAGCGCAAGTGTGAGGCGGCCAATGTGGCTGAACAAAGGAGAGCCTACCT                   GCACGGCACGTGCGTGGAGTGGCTCCACAGATACCTGGAGAACGGGAAGGAGATGCTGCA                   GCGCGCGGACCCCCCCAAGACACACGTGACCCACCACCCTGTCTTTGACTATCAGGCCAC                   CCTGAGGTGCTGGGCCCTGGGCTTCTACCCTGCGGAGATCATACTGACCTGGCACCGGGA                   TCGGGAGGACCAGACCCAGGACGTGGAGCTCGTGGAGACCAGGCCTGCAGGGGATGGAAC                   CTTCCAGAAGTGGCCAGCTGTGGTGGTGCCTTCTGGAGAGGAGCAGAGATACACGTGCCA                   TGTGCAGCATGAGGGGCTGCCGGAGCCCCTCATGCTGAGATGGGAGCAGTCTTCCCTGCC                   CACCATCCCCATCATGGGTATCGTTGCTGGTCTGGTTGTCCTTGCAGCTGTAGTCACTGG                   AGCTGCGGTCGCTGCTGTGCTGTGGAGGAAGAAGAGCTCAGGTAAGAAAGGAGGGAGCTA                   CTCTCAQGCTGCAAGTAGTGACAGTGCCCAGGGCTCTAATGTGTCTCTCACGGCTTGTAA                   ATGTGACACCCCGGGGGGCCTGATGTGTGTGGGTTGTTGAGGGAAACAGTGGACATAGCT                   GTGCTATGAC                                         SEQ ID NO: 160   379 aa                             NOV36b,   MVVMAPRTLFLLLSGALTLTETWAGSHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRF           CG59256-01       Protein Sequence   DSDSACPRMEPRAPWVEQEGPEYWEEEThNTKAHAQTDRMNLQTLRGYYNQSEGVGPGSH                   TLQWMIGCDLGSDGRLLRGYEQYAYDGKDYLALNEDLRSWTAADTAAQISKRKCEAANVA                   EQRRAYLEGTCVEWLHRYLENCKEMLQRADPPKTHVTHHPVFDYEATLRCWALGFYPAEI                   ILTWQRDGEDQTQDVELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLR                   WEQSSLPTIPIMGIVAGLVVLAAVVTGAAVAAVLWRKKSSGKKGGSYSQAASSDSAQGSN                   VSLTACKCDTPGGLMCVGC                  
 
     [1005] The NOV39b clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table E6.  
                               TABLE E6                                      SEQ ID NO: 173   1266 bp                                 NOV39b, ATGGCGCCCCGAACCCTCCTCCTGCTGCTCTCGGGGACCCTGGCCCTGGCCGAGACCTGG               CG94630-01,           DNA Sequence   GCGGGCTCCCACTCCATGAGGTATTTCAGCACCGCCGTTTCCTGGCCGGGCCGCGGGGAG                           CCCAGCTTCATTGCCGTGGGCTACGTGGACGACACGCAGTTCGTGCGGGTCGACAGTGAC                           GCCGTGAGTCTGACCATGAAGACGCGGGCGCGGTGGGTGGAGCAGGAGGGGCCGGAGTAT                           TGGGACCTACAGACACTGGGCGCCAAGGCCCAGGCACAGACTGACCGAGTGAACCTGCGG                           ACCCTGCTCCGCTACTACAACCAGAGCGAGGCGGGGTATCACATCCTCCAGGGAATGTTT                           GGCTGCGACCTGGGGCCCGACGGGCGTCTCCTCCGCGGGTATGAGCAGTATGCCTACGAC                           GGCAAGGATTACATCGCCCTGAACGAGGACCTCCCCTCCTGGACCGCCGCGGATACCGCG                           GCTCAGATTACCCAGCGCAAGTATGAGGCGGCCAATGTGGCTGAGCAAAGGAGAGCCTAC                           CTGGAGGGCACCTGCATGQAQTGGCTCCGCAGACACCTGGAGAACGGGAAGGAGACCCTG                           CAGCGCGCGGGCATAACGAGGTCCTGGGTTCTGGGCTTCTACCCTGCGGAGATCACATTG                           ACCTGGCAGCGGGATGGGGAGGACCAGACCCAGGACATGGAGCTCGTGGAGACCAGGCCC                           ACAGGGGATGGAACCTTCCAGAAGTGGGCGGTTGTGGTAGTGCCTTCTGGAGAGGAACAG                           AGATACACATGCCATGTGCAGCACAAGGGGCTGCCCAAGCCCCTCATCCTGAGATGGGAG                           CCCTCTCCCCAGCCCACCATCCCCATTGTGGGTATCATTGCTGGCCTGGTTCTCCTTGGA                           GCTGTGGTCACTGGAGCTGTGGTCACTGCTGTGATGTGGAGGAAGAAGAGCTCAGATAGA                           AAAGGAGGGAGCTACTCTCAGGCTGCAAAAAACATCATTAAAGTAAAAACAGAAAAATTT                           CTGGCCTTGTGGTGTATACGTTCTAGATGCAAGCTTGTCCAACCTGCAGCTCTCGGGCTG                           CGTGTGGCCCGGGACAGCTTTGAATTTCCCTCCCTTGACTCCATCAACATCGGCACCTGC                           CAGACGCCCACCACCCACCATCGAAGTGCTGAGAAGAAGTGCAAGGTACTCAACCTGCTC                           TGGGGATACAGCAGGAAAGCAGAGTGTTTACGGATTTCACATTCCATCAAAGAAAATCCA                           TTTTGA                                             SEQ ID NO: 174   421 aa                             NOV39b,   MAPRTLLLLLSGTLALAETWAGSHSMRYFSTAVSWPGRGEPSFIAVGYVDDTQFVRVDSD           CG94630-01       Protein Sequence   AVSLRMKTRARWVEQEGPEYWDLQTLGAKAQAQTDRVNLRTLLRYYNQSEAGYHILQGMF                   GCDLGPDGRLLRGYEQYAYDGKDYIALNEDLRSWTAADTAAQITQRKYEAANVAEQRRAY                   LEGTCMEWLRRHLENGKETLQRAGITRSNXTLGFYPAEITLTWQRDGEDQTQDMELVETRP                   TGDGTFQKWAVVVVPSGEEQRYTCHVQHKGLPKPLILRWEPSPQPTIPIVGIIAGLVLLG                   AVVTGAVVTAVMWRKKSSDRKGGSYSQAAKNIIKVKTEKFLALWCIRSRCKLVQPAALCL                   RVARDSFEFPSLDSINIGTCQTPTTHHRSAEKKCKVLNLLWGYSRKAECLRISHSIKENP                   F                  
 
     Example F  
     [1006] Polynucleotide and Polypeptide Sequences, and Homology Data  
     Example 1  
     [1007] The NOV41 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table F1A.  
               TABLE F1A                       NOV41 Sequence Analysis                                                    SEQ ID NO: 177   1050 bp                             NOV41a,     TCGCC   ATG TACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAGGTGAT           CG55676-01       DNA Sequence   GCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATCGGGTCGCCCTG                   TGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTTCAATT                   TGGCCGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTATTACCT                   CAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCACGTTG                   GCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGACAGGTATT                   TCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCGGCTGG                   CATCCTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGCTGGAG                   AACCATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGAGTCGG                   CCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATOCCCCTCGGCATCAT                   CTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGGCCAGA                   CAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTTCATCA                   CATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCCTCGAG                   TGCCTGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCTACATG                   AACAGCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAAATTCT                   ACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCAAAAACACA                   AAGGCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTGTGGCA                   AATAGTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTGGCACT                     GA   ACAA                                           ORE Start: ATG at 6   ORE Stop: TGA at 1044                                         SEQ ID NO: 178   346 aa   MW at 39294.8kD                             NOV41a,   MYNGSCCRIEGDTISQVNPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA           CG55676-01       Protein Sequence   VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFK                   VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAN                   GWHDIMPQLEFPMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC                   YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN                   KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH                                         SEQ ID NO: 179   1104 bp                             NOV41b,     GTGCCATTGTGGGGACTCCCTGGGCTGCTCTGCACCCGGACACTTGCTCTGTCCCCGC             CG55676-02       DNA Sequence     C   ATG TACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAGGTGATGCCG                   CCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCGCCCTGTGTG                   GTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTTCAATTTGGC                   CGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTATTACCTCAOA                   CGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCACGTTGGCCA                   TGAACAGGGCCGGCAGCATCGTGTTCCTTACGGTGGTGGCTGCGGGCAGGTATTTCAA                   AGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCGGCTGGCATC                   GTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGCTGGAGAACC                   ATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGAGTCGGCCAA                   TGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGCATCATCTTA                   TTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGGCCAGACAGG                   CTCGGATGAAGAAGGCGACCCGCTTCATCATGGTGGTGGCAATTGTGTTCATCACATG                   CTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCCTCGAGTGCC                   TGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCTACATGAACA                   GCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAAATTCTACAA                   CAAGCTCAAAATCTGCACTCTGAAACCCAAGCAGCCAGGACACTCAAAAACACAAAGG                   CCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTGTGGCAAATA                   GTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTGGCAC TGA   AC                       AA                                           ORF Start: ATG at 60   ORF Stop: TGA at 1098                                         SEQ ID NO: 180   346 aa   MW at 39236.8kD                             NOV41b,   MYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA           CG55676-02       Protein Sequence   VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAAGRYFK                   VVHPHHAVNTTSTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESEIMESAN                   GWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC                   YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN                   KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH                                         SEQ ID NO: 181   1104 bp                             NOV41c,     GTGCCATTGTGGGGACTCCCTGGGCTGCTCTGCACCCGGACACTTGCTCTGTCCCCGC             CG55676-03       DNA Sequence     C   ATG TACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAGGTGATGCCG                   CCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGACAATGGGGTCCCCCTGTGTG                   GTTTCTGCTTCCACATGAAGACCTGGPAGCCCAGCACTGTTTACCTTTTCAATTTGGC                   CGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTATTACCTCAGA                   CGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTCGGGCTCTTCACGTTGGCCA                   TGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGCCAGGTATTTCAA                   AGTGGTCCACCCCCACCACCCGGTGAACACTATCTCCACCCGGGTGGCGGCTGGCATC                   GTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGCTGGAGAACC                   ATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGAGTCGGCCAA                   TGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGCATCATCTTA                   TTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGGCCAGACAGG                   CTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTTCATCACATG                   CTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCCTCGAGTGCC                   TGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCTACATGAACA                   GCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAAATTCTACAA                   CAAGCTCAAAATCTGCAGTCTGAAACCCPAGCAGCCAGGACACTCAAAAACACAAAGG                   CCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTGTGGCAAATA                   GTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTGGCAC TGA   AC                       AA                                           ORF Start: ATG at 60   ORF Stop: TGA at 1098                                         SEQ ID NO: 182   346 aa   MW at 39294.8kD                             NOV41c,   MYNGSCCRIEGDTISQVMPPLLIVAFVLGALDNGVALCGFCFHMKTWKPSTVYLFNLA           CG55676-03       Protein Sequence   VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAAGRYFK                   VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAN                   GWHDIMFQLEFPMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC                   YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN                   KLKICSLKRKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH                                         SEQ ID NO: 183   1057 bp                             NOV41d,     CACCAGATCT   ATG TACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAG           CG55676-04       DNA Sequence   GTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCG                   CCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTT                   CAATTTGGCCGTGGCTGATTTCCTCCTTATCATCTGCCTGCCTTTTCGGACAGACTAT                   TACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCA                   CGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTCGTCGCTGCGGACAG                   GTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCG                   GCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGC                   TGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGA                   GTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGC                   ATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCACCAGCTGG                   CCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTT                   CATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCC                   TCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCT                   ACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAA                   ATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCAAAA                   ACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTCCATCAGTG                   TGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGCGATCCCCACATTGTTGAGTG                   GCAC AAG   CTTGGC                                           ORF Start: ATG at 11   ORF Stop: at 1049                                         SEQ ID NO: 184   346 aa   MW at 39294.8kD                             NOV41d,   MYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA           CG55676-04       Protein Sequence   VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFK                   VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAN                   GWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC                   YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN                   KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSPQSQSDGQWDPHIVEWH                                         SEQ ID NO: 185   961 bp                             NOV41e,     CACCAGATCT   AAT GGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG           CG55676-05       Protein Sequence   CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC                   TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC                   CTGCCGAGTGGGGCTCTTCACGTTCGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT                   ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA                   CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT                   TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG                   AGTTCTTTATCCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCT                   GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC                   ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCT                   ATTTCCTCTGGACGGTGCCCTCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCA                   CATAACCCTCAGCTTCACCTACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTT                   TCAAGCCCCTCCTTTCCCAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCA                   AGCAGCCAGGACACTCAAAAACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGG                   TCGCAGGAGTTGCATCAGTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGG                   GATCCCCACATTGTTGAGTGGCAC AAG   CTTGGC                                           ORE Start: at 11   ORE Stop: at 953                                         SEQ ID NO: 186   314 aa   MW at 35943.9kD                             NOV41e,   NGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRV           CG55676-05       Protein Sequence   GLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTV                   YLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRR                   QQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVPSSACDPSVHGALHITL                   SFTYMNSMLDPLVYYFSSPSFPKFYNKLKICSLKPKQPGHSKTQRPEEMPISNLGRRS                   CISVANSPQSQSDGQWDPHIVEWH                                         SEQ ID NO: 187   1060 bp                             NOV41f,     CACCTCGCGAACC   ATG TACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCC           CG55676-06       DNA Sequence   CAGGTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGG                   TCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCACCACTGTTTACCT                   TTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGCACAGAC                   TATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGCCTCT                   TCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGA                   CAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTG                   GCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGCGAACAGTCTATCTTT                   TGCTGGAGAACCATCTCTGCGTGCAACAGACCCCCGTCTCCTGTGAGAGCTTCATCAT                   GGAGTCGGCCAATGGCTGGCATGACATCATGTTCCACCTGCAGTTCTTTATCCCCCTC                   GGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGC                   TGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGT                   GTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTG                   CCCTCGAGTGCCTGCQATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCA                   CCTACATGAACAGCATGCTGGATCCCCTGGTCTATTATTTTTCAAGCCCCTCCTTTCC                   CAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCA                   AAAACACAAACCCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCA                   GTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGA                   GTGCCAC GTC   GACGGC                                           ORF Start: at 14   ORF Stop: at 1052                                         SEQ ID NO: 188   346 aa   MW at 39294.8kD                             NOV41f,   MYNGSCCRIEGDTISQVNPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLA           CG55676-06       Protein Sequence   VADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFK                   VVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESAV                   GWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITC                   YLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYN                   KLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH                                         SEQ ID NO: 189   961 bp                             NOV41g,     C   ACC TCGCGAAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG           CG556676-07       DNA Sequence   CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC                   TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC                   CTGCCGAGTGGGGCTCTTCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT                   ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA                   CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT                   GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC                   TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG                   AGTTCTTTATGCCCCTCGGCATCATCTTATTTTCCTCCTTCAAGATTGTTTGGAGCCT                   GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC                   ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCT                   ATTTCCTCTGGACGGTGCCCTCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCA                   CATAACCCTCAGCTTCACCTACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTT                   TCAAGCCCCTCCTTTCCCAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCA                   AGCAGCCAGGACACTCAAAAACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGG                   TCGCAGGAGTTGCATCAGTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGG                   GATCCCCACATTGTTGAGTGGCACGTCGACGGC                                         ORF Start: at 2   ORF Stop: end of sequence                                         SEQ ID NO: 190   320 aa   MW at 36559.5kD                             NOV41g,   TSRNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIP           CG55676-07       Protein Sequence   CRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVIL                   GTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSL                   RRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVPSSACDPSVHGALH                   ITLSPTYMNSMLDPLVYYFSSRSFRKFYNKLKICSLKPKQPGHSKTQRPEEMPISNLG                   RRSCISVANSFQSQSDGQWDPHIVEWHVDG                                         SEQ ID NO: 191   1057 bp                             NOV41h,     C   ACC AGATCTATGTACAACGGGTCGTGCTGCCGCATCGAGGGGGACACCATCTCCCAG           248209538 DNA       Sequence   GTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCG                   CCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAGCCCAGCACTGTTTACCTTTT                   CAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCGGACAGACTAT                   TACCTCAGACGTAGACACTGGGCTTTTGGGCACATTCCCTGCCGAGTGGGGCTCTTCA                   CGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCCGACAG                   GTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCG                   GCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGC                   TGCAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCCTGTGAGAGCTTCATCATGGA                   GTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATCCCCCTCGGC                   ATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGACGCGGAOGCAGCAGCTGG                   CCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTCGTCCCAATTGTGTT                   CATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCTATTTCCTCTGGACGGTGCCC                   TCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCACATAACCCTCAGCTTCACCT                   ACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTTTCAAGCCCCTCCTTTCCCAA                   ATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCAAGCAGCCAGGACACTCAAAA                   ACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGGTCGCAGGAGTTGCATCAGTG                   TGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGGGATCCCCACATTGTTGAGTG                   GCACAAGCTTGGC                                         ORE Start: at 2   ORF Stop: end of sequence                                         SEQ ID NO: 192   352 aa   MW at 39937.6kD                             NOV41h,   TRSMYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLF           24820938       Protein Sequence   NLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADR                   YFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIME                   SANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVF                   ITCYLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPK                   FYNKLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEW                   HKLG                                         SEQ ID NO: 193   961 bp                             NOV41j,     C   ACC AGATCTAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG           248209591 DNA       Sequence   CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC                   TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC                   CTGCCGAGTGGGGCTCTTCACCTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT                   ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA                   CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT                   GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC                   TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG                   AGTTCTTTATGCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGACCCT                   GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCCGATGAAGAAGGCGACCCGGTTCATC                   ATGGTGGTCGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCT                   ATTTCCTCTGGACGGTGCCCTCGAGTGCCTGCGATCCCTCTGTCCATGGGGCCCTGCA                   CATAACCCTCAGCTTCACCTACATGAACAGCATGCTGGATCCCCTGGTGTATTATTTT                   TCAAGCCCCTCCTTTCCCAAATTCTACAACAAGCTCAAAATCTGCAGTCTGAAACCCA                   AGCAGCCAGGACACTCAAAAACACAAAGGCCGGAAGAGATGCCAATTTCGAACCTCGG                   TCGCAGGAGTTGCATCAGTGTGGCAAATAGTTTCCAAAGCCAGTCTGATGGGCAATGG                   GATCCCCACATTGTTGAGTGGCACAAGCTTGGC                                         ORE Start: at 2   ORF Stop: end of sequence                                         SEQ ID NO: 194   320 aa   MW at 36586.6kD                             NOV41i,   TRSNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIP           248209591       Protein Sequence   CRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVIL                   GTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSL                   RRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVP2SACDPSVHGALH                   ITLSFTYMNSMLDPLVYYFSSPSFPKFYNKLKICSLKPKQPGHSKTQRREEMPISNLG                   RRSCISVANSFQSQSDGQWDPHIVEWHKLG                                         SEQ ID NO: 195   742 bp                             NOV41j,     C   ACC AGATCTATGTACAACGGCTCGTCCTCCCCCATCCACCGCGACACCATCTCCCAG           248209663 DNA       Sequence   GTGATGCCGCCGCTGCTCATTGTGGCCTTTGTGCTGGGCGCACTAGGCAATGGGGTCG                   CCCTGTGTGGTTTCTGCTTCCACATCAAGACCTGGAAGCCCAGCACTGTTTACCTTTT                   CAATTTGGCCGTCGCTGATTTCCTCCTTATGATCTGCCTGCCTTTTCCGACAGACTAT                   TACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCCCTGCCGAGTGGGGCTCTTCA                   CGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTTACGGTGGTGGCTGCGGACAG                   GTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACACTATCTCCACCCGGGTGGCG                   GCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCTGGGAACAGTGTATCTTTTGC                   TGGAGAACCATCTCTGCGTGCAAGAGACCGCCGTCTCCTGTGAGAGCTTCATCATGGA                   GTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGGAGTTCTTTATGCCCCTCGGC                   ATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCTGAGGCGGAGGCAGCAGCTGG                   CCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATCATGGTGGTGGCAATTGTGTT                   CATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCAAGCTTGGC                                         ORE Start: at 2   ORE Stop: end of sequence                                         SEQ ID NO: 196   247 aa   MW at 27932.0kD                             NOV41j,   TRSMYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLF           248209663       Protein Sequence   NLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADR                   YFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIME                   SANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVF                   ITCYLPSVSARLKLG                                         SEQ ID NO: 197   646 bp                             NOV41k,     C   ACC AGATCTAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGGAAG           24809745 DNA       Sequence   CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC                   TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC                   CTGCCGAGTGGGGCTCTTCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT                   ACGGTGGTGGCTGCGGACAGGTATTTCAAAGTGGTCCACCCCCACCACGCGGTGAACA                   CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT                   GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC                   TGTGAGAGCTTCATCATGGAGTCGGCCAATGGCTGGCATGACATCATGTTCCAGCTGG                   AGTTCTTTATGCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCCT                   GAGGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC                   ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCA                   AGCTTGGC                                         ORE Start: at 2   ORF Stop: end of sequence                                         SEQ ID NO: 198   215 aa   MW at 24581.1kD                             NOV41k,   TRSNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIP           24809745       Protein Sequence   CRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVIL                   GTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSL                   RRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLKLG                  
 
     [1008] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table F1B.  
               TABLE F1B                          Comparison of NOV41a against NOV41b through NOV41k.                                         Identities/           Protein   NOV41a Residues/   Similarities for           Sequence   Match Residues   the Matched Region                       NOV41b   1 . . . 346   333/346 (96%)               1 . . . 346   333/346 (96%)           NOV41c   1 . . . 346   332/346 (95%)               1 . . . 346   332/346 (95%)           NOV41d   1 . . . 346   334/346 (96%)               1 . . . 346   334/346 (96%)           NOV41e   33 . . . 346    302/314 (96%)               1 . . . 314   302/314 (96%)           NOV41f   1 . . . 346   334/346 (96%)               1 . . . 346   334/346 (96%)           NOV41g   33 . . . 346    302/314 (96%)               4 . . . 317   302/314 (96%)           NOV41h   1 . . . 346   334/346 (96%)               4 . . . 349   334/346 (96%)           NOV41i   33 . . . 346    302/314 (96%)               4 . . . 317   302/314 (96%)           NOV41j   1 . . . 241   229/241 (95%)               4 . . . 244   229/241 (95%)           NOV41k   33 . . . 241    197/209 (94%)               4 . . . 212   197/209 (94%)                      
 
     [1009] Further analysis of the NOV41a protein yielded the following properties shown in Table F1C.  
               TABLE F1C                       Protein Sequence Properties NOV41a                                        PSort   0.6850 probability located in endoplasmic reticulum       analysis:   (membrane); 0.6400 probability located in plasma           membrane; 0.4600 probability located in Golgi body;           0.1000 probability located in endoplasmic reticulum           (lumen)       SignalP   Cleavage site between residues 33 and 34       analysis:                  
 
     [1010] A search of the NOV41a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table F1D.  
               TABLE F1D                          Geneseq Results for NOV41a                                         NOV41a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               ABB08596   Human lipocyte-originated G   1 . . . 346   346/346 (100%)   0.0           protein-coupled receptor protein   1 . . . 346   346/346 (100%)           TGR13 -  Homo sapiens , 346 aa.           [WO200202767-A1, 10 JAN 2002]       AAO14788   Human purinergic-like G-protein   1 . . . 346   346/346 (100%)   0.0           coupled receptor (AXOR87) -   1 . . . 346   346/346 (100%)             Homo sapiens , 346 aa.           [GB2365868-A, 27 FEB 2002]       AAE17077   Human G-protein coupled receptor   1 . . . 346   346/346 (100%)   0.0           (GPCRx14) protein -  Homo     1 . . . 346   346/346 (100%)             sapiens , 346 aa.           [WO200198330-A2, 27 DEC 2001]       AAE16172   Human G-protein coupled receptor 3   1 . . . 346   346/346 (100%)   0.0           (GCREC-3) protein -  Homo     1 . . . 346   346/346 (100%)             sapiens , 346 aa.           [WO200187937-A2, 22 NOV 2001]       AAU11401   HM74-like G-protein coupled receptor   1 . . . 346   346/346 (100%)   0.0           (GPCR) -  Homo sapiens , 346 aa.   1 . . . 346   346/346 (100%)           [WO200177320-A2, 18 OCT 2001]                  
 
     [1011] In a BLAST search of public sequence datbases, the NOV41a protein was found to have homology to the proteins shown in the BLASTP data in Table F1E.  
               TABLE F1E                          Public BLASTP Results for NOV41a                                         NOV41a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched   Expect       Number   Protein/Organism/Length   Residues   Portion   Value               Q9BXC0   Putative chemokine receptor   1 . . . 346    346/346 (100%)   0.0           (G protein-coupled receptor)   1 . . . 346    346/346 (100%)           (Putative G-protein coupled           receptor) -  Homo sapiens  (Human),           346 aa.       Q8TDS4   Putative G-protein coupled receptor -   5 . . . 340   180/341 (52%)   6e−94             Homo sapiens  (Human), 363 aa.   17 . . . 355    227/341 (65%)       BAC06083   Seven transmembrane helix   5 . . . 340   178/341 (52%)   1e−93           receptor -  Homo sapiens  (Human),   17 . . . 355    227/341 (66%)           387 aa.       P49019   Probable G protein-coupled   5 . . . 340   178/341 (52%)   1e−93           receptor HM74 -  Homo sapiens     17 . . . 355    227/341 (66%)           (Human), 387 aa.       Q9EP66   Putative seven transmembrane   5 . . . 316   176/317 (55%)   4e−92           spanning receptor -  Mus musculus     14 . . . 329    215/317 (67%)           (Mouse), 360 aa.                  
 
     [1012] PFam analysis predicts that the NOV41a protein contains the domains shown in the Table F1F.  
               TABLE F1F                          Domain Analysis of NOV41a                                             Identities/                       Similarities for           Pfam   NOV41a   the Matched   Expect           Domain   Match Region   Region   Value                       7tm_1   32 . . . 278   72/272 (26%)   5.3e−42                   175/272 (64%)                       
 
     Example 2  
     [1013] The NOV42 clone was analyzed, and the nucleotide and encoded polypeptide sequences are shown in Table F2A.  
               TABLE F2A                       NOV42 Sequence Analysis                                                    SEQ ID NO: 199   1012 bp                             NOV42a,     GCATTCACAAGCAGG   ATG TTCCTTCCCAATGACACCCAGTTTCACCCCTCCTCCTTCC           CG53677-01       DNA Sequence   TGTTGCTGGGGATCCCAGGACTAGAAACACTTCACATCTGGATCGGCTTTCCCTTCTG                   TGCTGTGTACATGATCGCACTCATAGGGAACTTCACTATTCTACTTGTGATCAAGACT                   GACAGCAGCCTACACCAGCCCATGTTCTACTTCCTGGCCATGTTGGCCACCACTGATG                   TGGGTCTCTCAACAGCTACCATCCCTAAGATGCTTGGAATCTTCTGGATCAACCTCAG                   AGGGATCATCTTTGAAGCCTGCCTCACCCAGATGTTTTTTATCCACAACTTCACACTT                   ATGGAGTCAGCAGTCCTTGTGGCAATGGCTTATGACAGCTATGTGGCCATCTGCAATC                   CACTCCAATATAGCGCCATCCTCACCAACAAGGTTGTTTCTGTGATTGGTCTTGGTGT                   GTTTGTGAGGGCTTTAATTTTCGTCATTCCCTCTATACTTCTTATATTGCGGTTGCCC                   TTCTGTGGGAATCATGTAATTCCCCACACCTACTGTGAGCACATGGGTCTTGCTCATC                   TATCTTGTGCCAGCATCAAAATCAATATTATTTATGGTTTATGTGCCATTTGTAATCT                   GQTGTTTGACATCACAGTCATTGCCCTCTCTTATGTGCATATTCTTTGTGCTGTTTTC                   CGTCTTCCTACTCATGAGCCCCGACTCAAGTCCCTCAGCACATGTGGTTCACATGTGT                   GTGTAATCCTTGCCTTCTATACACCAGCCCTCTTTTCCTTTATGACTCATTGCTTTGG                   CCGAAATGTGCCCCGCTATATCCATATACTCCTAGCCAATCTCTATGTTGTGGTGCCA                   CCAATGCTCAATCCTGTCATATATGGAGTCAGAACCAAGCAGATCTATAAATGTGTAA                   AGAAAATATTATTGCAGGAACAAGGAATGGAAAAGGAAGAGTACCTAATACATACGAG                   GTTC TGA   ATGCAATTTTATGAAATTT                                           ORF Start: ATG at 16   ORE Stop: TGA at 991                                         SEQ ID NO: 200   325 aa   MW at 36602.5kD                             NOV42a,   MFLPNDTQFHPSSFLLLGIPGLETLHIWIGFPFCAVYMIALIGNFTILLVIKTDSSLH           CG53677-01       Protein Sequence   QPMFYFLAMLATTDVGLSTATIPKMLGIFWINLRGIIFEACLTQMFFIHNFTLMESAV                   LVANAYDSYVAICNPLQYSAILTNKVVSVIGLGVFVRALIFVIPSILLILRLPFCGNH                   VIPHTYCEHMGLAHLSCASIKINIIYGLCAICNLVFDITVIALSYVHILCAVFRLPTH                   EPRLKSLSTCGSHVCVILAFYTPALFSFMTHCFGRNVPRYIHILLANLYVVVPPMLNP                   VIYGVRTKQIYKCVKKILLQEQGMEKEEYLIHTRF                                         SEQ ID NO: 201   988 bp                             NOV42b,     TAGG   ATG TTCCTTCCCAATGACACCCAGTTTCACCCCTCCTCCTTCCTGTTGCTGGGG           CG53677-02       DNA Sequence   ATCCCAGGACTAGAAACACTTCACATCTGGATCGGCTTTCCCTTCTGTGCTGTGTACA                   TGATCGCACTCATAGGGAACTTCACTATTCTACTTGTGATCAAGACTGACAGCAGCCT                   ACACCAGCCCATGTTCTACTTCCTGGCCATGTTGGCCACCACTGATGTGGGTCTCTCA                   ACAGCTACCATCCCTAAGATGCTTGGAATCTTCTGGATCAACCTCAGAGGGATCATCT                   TTGAAGCCTGCCTCACCCAGATGTTTTTTATCCACAACTTCACACTTATGCAGTCAGC                   AGTCCTTGTGGCAATGGCTTATGACAGCTATGTGGCCATCTGCAATCCACTCCAATAT                   AGCGCCATCCTCACCAACAAGGTTGTTTCTGTGATTGGTCTTGGTGTGTTTGTGAGGG                   CTTTAATTTTCGTCATTCCCTCTATACTTCTTATATTGCGGTTGCCCTTCTGTGGGAA                   TCATGTAATTCCCCACACCTACTGTGAGCACATGGGTCTTGCTCATCTATCTTGTGCC                   AGCATCAAAATCAATATTATTTATGGTTTATGTGCCATTTGTAATCTAGTGTTTGACA                   TCACAGTCATTGCCCTTTCTTATGTGCATATTCTTTGTGCTGTTTTCCGTCTTCCTAC                   TCATGAAGCCCGACTCAAGTCCCTCAGCACATGTGGTTCACATGTGTGTGTAATCCTT                   GCCTTCTATACACCAGCCCTCTTTTCCTTTATGACTCATCGCTTTGGCCGAAATGTGC                   CCCGCTATATCCATATACTCCTAGCCAATCTCTATGTTGTGGTGCCACCAATGCTCAA                   TCCTGTCATATATGGAGTCAGAACCAAGCAGATCTATAAATGTGTGAAGAAAATATTA                   TTGCAGCAACAAGGAATGGAAAAGGAAGAGTACCTAATACATACGAGGTTC TGA   ATGC                       AA                                           ORF Start: ATG at 5   ORE Stop: TGA at 980                                         SEQ ID NO: 202   325 aa   MW at 36629.6kD                             NOV42b,   MFLPNDTQFHPSSFLLLGIPGLETLHIWIGFPFCAVYMIALIGNFTILLVIKTDSSLH           CG53677-02       Protein Sequecne   QPMFYFLAMLATTDVGLSTATIPKMLGIPWINLRGIIFEACLTQMFFIHNFTLMESAV                   LVAMAYDSYVAICNPLQYSAILTNKVVSVIGLGVFVRALIFVIPSILLILRLPPCGNH                   VTPHTYCEHMGLAHLSCASIKINIIYGLCAICNLVFDITVIALSYVHILCAVFRLPTH                   EARLKSLSTCGSHVCVILAFYTPALFSFMThRFGRNVPRYIHILLANLYVVVPPMLNPI                   VIYGVRTKQIYKCVKKILLQEQGMEKEEYLILHTRF                                         SEQ ID NO: 203   646 bp                             NOV42c,     CACCAGATCTAATGGGGTCGCCCTGTGTGGTTTCTGCTTCCACATGAAGACCTGCAAG             116781634 DNA       Sequence     CCCAGCACTGTTTACCTTTTCAATTTGGCCGTGGCTGATTTCCTCCTTATGATCTGCC                       TGCCTTTTCGGACAGACTATTACCTCAGACGTAGACACTGGGCTTTTGGGGACATTCC                       CTGCCGAGTGGGGCTCTTCACGTTGGCCATGAACAGGGCCGGGAGCATCGTGTTCCTT                       ACGGTGGTGGCTGCGGACAGGTATTTcAAAGTGGTCCACCCCCACCACGCGGTGA   ACA                     CTATCTCCACCCGGGTGGCGGCTGGCATCGTCTGCACCCTGTGGGCCCTGGTCATCCT                   GGGAACAGTGTATCTTTTGCTGGAGAACCATCTCTGCGTGCAAGAGACGGCCGTCTCC                   TGTGAGAGCTTCATCATGGAGTCGGCCAATCGCTGGCATGACATCATGTTCCAGCTGG                   AGTTCTTTATGCCCCTCGGCATCATCTTATTTTGCTCCTTCAAGATTGTTTGGAGCC T                       GA   GGCGGAGGCAGCAGCTGGCCAGACAGGCTCGGATGAAGAAGGCGACCCGGTTCATC                               ATGGTGGTGGCAATTGTGTTCATCACATGCTACCTGCCCAGCGTGTCTGCTAGACTCA                       AGCTTGGC                                           ORF Start: at 288   ORE Stop: TGA at 522                                         SEQ ID NO: 204   78 aa   MW a 8506.6kD                             NOV42c,   TLSPPGWRLASSAPCGPWSSWEQCIFCWRTISACKRRPSPVRASSWSRPMAGMTSCSS           116781634       Protein Sequence   WSSLCPSASSYFAPSRLFGA                  
 
     [1014] Sequence comparison of the above protein sequences yields the following sequence relationships shown in Table F2B.  
               TABLE F2B                          Comparison of NOV42a against NOV42b and NOV42c.                                         Identities/                   Similarities for           Protein   NOV42a Residues/   the Matched           Sequence   Match Residues   Region                       NOV42b   1 . . . 325   323/325 (99%)               1 . . . 325   323/325 (99%)                             NOV42c   No Significant Alignment Found.                      
 
     [1015] Further analysis of the NOV42a protein yielded the following properties shown in Table F2C.  
               TABLE F2C                       Protein Sequence Properties NOV42a                                                PSort   0.6850 probability located in endoplasmic reticulum           analysis:   (membrane); 0.6400 probability located in plasma               membrane; 0.4600 probability located in Golgi               body; 0.1000 probability located in endoplasmic               reticulum (lumen)           SignalP   Cleavage site between residues 56 and 57           analysis:                      
 
     [1016] A search of the NOV42a protein against the Geneseq database, a proprietary database that contains sequences published in patents and patent publication, yielded several homologous proteins shown in Table F2D.  
               TABLEF2D                          Geneseq Results for NOV42a                                         NOV42a   Identities/                   Residues/   Similarities for       Geneseq   Protein/Organism/Length   Match   the Matched   Expect       Identifier   [Patent #, Date]   Residues   Region   Value               AAU95728   Human olfactory and pheromone G   1 . . 325   325/325 (100%)   0.0           protein-coupled receptor #215 -   1 . . 325   325/325 (100%)             Homo sapiens , 325 aa.           [WO200224726-A2, 28 MAR.           2002]       AAU85190   G-coupled olfactory receptor #51 -   1 . . 325   325/325 (100%)   0.0             Homo sapiens , 325 aa.   1 . . 325   325/325 (100%)           [WO200198526-A2, 27 DEC.           2001]       AAU24570   Human olfactory receptor   1 . . 325   325/325 (100%)   0.0           AOLFR60 -  Homo sapiens , 325 aa.   1 . . 325   325/325 (100%)           [WO200168805-A2, 20 SEP. 2001]       ABB44531   Human GPCR6a polypeptide SEQ   1 . . 325   325/325 (100%)   0.0           ID NO 22 -  Homo sapiens , 325 aa.   1 . . 325   325/325 (100%)           [WO200174904-A2, 11 OCT.           2001]       ABB44532   Human GPCR6b polypeptide SEQ   1 . . 325   323/325 (99%)    0.0           ID NO 24 -  Homo sapiens , 325 aa.   1 . . 325   323/325 (99%)            [WO200174904-A2, 11 OCT.           2001]                  
 
     [1017] In a BLAST search of public sequence datbases, the NOV42a protein was found to have homology to the proteins shown in the BLASTP data in Table F2E.  
               TABLE F2E                          Public BLASTP Results for NOV42a                                         NOV42a   Identities/           Protein       Residues/   Similarities for       Accession       Match   the Matched       Number   Protein/Organism/Length   Residues   Portion   Expect Value               BAC06019   Seven transmembrane helix   1 . . 325   324/325 (99%)   0.0           receptor -  Homo sapiens     1 . . 325   324/325 (99%)           (Human), 325 aa.       Q8VGV8   Olfactory receptor MOR32-3 -   1 . . 317   264/317 (83%)   e−155             Mus musculus  (Mouse), 317 aa.   1 . . 317   284/317 (89%)       BAC06020   Seven transmembrane helix   5 . . 311   216/307 (70%)   e−126           receptor -  Homo sapiens     2 . . 308   252/307 (81%)           (Human), 308 aa       Q8VG26   Olfactory receptor MOR32-5 -   1 . . 308   216/308 (70%)   e−124             Mus musculus  (Mouse), 313 aa.   1 . . 308   251/308 (81%)       BAC06036   Seven transmembrane helix   5 . . 312   211/308 (68%)   e−124           receptor -  Homo sapiens     5 . . 312   251/308 (80%)           (Human), 312 aa.                  
 
     [1018] PFam analysis predicts that the NOV42a protein contains the domains shown in the Table F2F.  
               TABLE F2F                          Domain Analysis of NOV42a                                             Identities/                   NOV42a   Similarities           Pfam   Match   for the   Expect           Domain   Region   Matched Region   Value                       7tm_1   43 . . 293   54/270 (20%)   6.3e−11                   166/270 (61%)                       
 
     Example G  
     [1019] Quantitative Expression Analysis of Clones in Various Cells and Tissues  
     [1020] The quantitative expression of various clones was assessed using microtiter plates containing RNA samples from a variety of normal and pathology-derived cells, cell lines and tissues using real time quantitative PCR (RTQ PCR). RTQ PCR was performed on an Applied Biosystems ABI PRISM® 7700 or an ABI PRISM® 7900 HT Sequence Detection System. Various collections of samples are assembled on the plates, and referred to as Panel 1 (containing normal tissues and cancer cell lines), Panel 2 (containing samples derived from tissues from normal and cancer sources), Panel 3 (containing cancer cell lines), Panel 4 (containing cells and cell lines from normal tissues and cells related to inflammatory conditions), Panel 5D/5I (containing human tissues and cell lines with an emphasis on metabolic diseases), AI_comprehensive_panel (containing normal tissue and samples from autoimmune diseases), Panel CNSD.01 (containing central nervous system samples from normal and diseased brains) and CNS_neurodegeneration_panel (containing samples from normal and Alzheimer&#39;s diseased brains).  
     [1021] RNA integrity from all samples is controlled for quality by visual assessment of agarose gel electropherograms using 28S and 18S ribosomal RNA staining intensity ratio as a guide (2:1 to 2.5:1 28s:18s) and the absence of low molecular weight RNAs that would be indicative of degradation products. Samples are controlled against genomic DNA contamination by RTQ PCR reactions run in the absence of reverse transcriptase using probe and primer sets designed to amplify across the span of a single exon.  
     [1022] First, the RNA samples were normalized to reference nucleic acids such as constitutively expressed genes (for example, β-actin and GAPDH). Normalized RNA (5 ul) was converted to cDNA and analyzed by RTQ-PCR using One Step RT-PCR Master Mix Reagents (Applied Biosystems; Catalog No. 4309169) and gene-specific primers according to the manufacturer&#39;s instructions.  
     [1023] In other cases, non-normalized RNA samples were converted to single strand cDNA (sscDNA) using Superscript 11 (Invitrogen Corporation; Catalog No. 18064-147) and random hexamers according to the manufacturer&#39;s instructions. Reactions containing up to 10 μg of total RNA were performed in a volume of 20 μl and incubated for 60 minutes at 42° C. This reaction can be scaled up to 50 μg of total RNA in a final volume of 100 μl. sscDNA samples are then normalized to reference nucleic acids as described previously, using 1×TaqMan® Universal Master mix (Applied Biosystems; catalog No. 4324020), following the manufacturer&#39;s instructions.  
     [1024] Probes and primers were designed for each assay according to Applied Biosystems Primer Express Software package (version 1 for Apple Computer&#39;s Macintosh Power PC) or a similar algorithm using the target sequence as input. Default settings were used for reaction conditions and the following parameters were set before selecting primers: primer concentration=250 nM, primer melting temperature (Tm) range 58°-60° C., primer, optimal Tm=59° C., maximum primer difference=2° C., probe does not have 5′G, probe Tm must be 10° C. greater than primer Tm, amplicon size 75 bp to 100 bp. The probes and primers selected (see below) were synthesized by Synthegen (Houston, Tex., USA). Probes were double purified by HPLC to remove uncoupled dye and evaluated by mass spectroscopy to verify coupling of reporter and quencher dyes to the 5′ and 3′ ends of the probe, respectively. Their final concentrations were: forward and reverse primers, 900 nM each, and probe, 200 nM.  
     [1025] PCR conditions: When working with RNA samples, normalized RNA from each tissue and each cell line was spotted in each well of either a 96 well or a 384-well PCR plate (Applied Biosystems). PCR cocktails included either a single gene specific probe and primers set, or two multiplexed probe and primers sets (a set specific for the target clone and another gene-specific set multiplexed with the target probe). PCR reactions were set up using TaqMan® One-Step RT-PCR Master Mix (Applied Biosystems, Catalog No. 4313803) following manufacturer&#39;s instructions. Reverse transcription was performed at 48° C. for 30 minutes followed by amplification/PCR cycles as follows: 95° C. 10 min, then 40 cycles of 95° C. for 15 seconds, 60° C. for 1 minute. Results were recorded as CT values (cycle at which a given sample crosses a threshold level of fluorescence) using a log scale, with the difference in RNA concentration between a given sample and the sample with the lowest CT value being represented as 2 to the power of delta CT. The percent relative expression is then obtained by taking the reciprocal of this RNA difference and multiplying by 100.  
     [1026] When working with sscDNA samples, normalized sscDNA was used as described previously for RNA samples. PCR reactions containing one or two sets of probe and primers were set up as described previously, using 1×TaqMan® Universal Master mix (Applied Biosystems; catalog No. 4324020), following the manufacturer&#39;s instructions. PCR amplification was performed as follows: 95° C. 10 min, then 40 cycles of 95° C. for 15 seconds, 60° C. for 1 minute. Results were analyzed and processed as described previously.  
     [1027] Panels 1, 1.1, 1.2, and 1.3D  
     [1028] The plates for Panels 1, 1.1, 1.2 and 1.3D include 2 control wells (genomic DNA control and chemistry control) and 94 wells containing cDNA from various samples. The samples in these panels are broken into 2 classes: samples derived from cultured cell lines and samples derived from primary normal tissues. The cell lines are derived from cancers of the following types: lung, cancel, breast cancer, melanoma, colon cancel, prostate cancer, CNS cancer, squamous cell carcinoma, ovarian cancer, liver cancer, renal cancer, gastric cancer and pancreatic cancer. Cell lines used in these panels are widely available through the American Type Culture Collection (ATCC), a repository for cultured cell lines, and were cultured using the conditions recommended by the ATCC. The normal tissues found on these panels are comprised of samples derived from all major organ systems from single adult individuals or fetuses. These samples are derived from the following organs: adult skeletal muscle, fetal skeletal muscle, adult heart, fetal heart, adult kidney, fetal kidney, adult liver, fetal liver, adult lung, fetal lung, various regions of the brain, the spleen, bone marrow, lymph node, pancreas, salivary gland, pituitary gland, adrenal gland, spinal cord, thymus, stomach, small intestine, colon, bladder, trachea, breast, ovary, uterus, placenta, prostate, testis and adipose.  
     [1029] In the results for Panels 1, 1.1, 1.2 and 1.3D, the following abbreviations are used:  
     [1030] ca.=carcinoma,  
     [1031] *=established from metastasis,  
     [1032] met=metastasis,  
     [1033] s cell var=small cell variant,  
     [1034] non-s=non-sm=non-small,  
     [1035] squam=squamous,  
     [1036] pl. eff=pl effusion=pleural effusion,  
     [1037] glio=glioma,  
     [1038] astro=astrocytoma, and  
     [1039] neuro=neuroblastoma.  
     [1040] General_screening_panel_v1.4  
     [1041] The plates for Panel 1.4 include 2 control wells (genomic DNA control and chemistry control) and 94 wells containing cDNA from various samples. The samples in Panel 1.4 are broken into 2 classes: samples derived from cultured cell lines and samples derived from primary normal tissues. The cell lines are derived from cancers of the following types: lung cancer, breast cancer, melanoma, colon cancer, prostate cancer, CNS cancer, squamous cell carcinoma, ovarian cancer, liver cancer, renal cancer, gastric cancer and pancreatic cancer. Cell lines used in Panel 1 4 are widely available through the American Type Culture Collection (ATCC), a repository for cultured cell lines, and were cultured using the conditions recommended by the ATCC. The normal tissues found on Panel 1.4 are comprised of pools of samples derived from all major organ systems from 2 to 5 different adult individuals or fetuses. These samples are derived from the following organs: adult skeletal muscle, fetal skeletal muscle, adult heart, fetal heart, adult kidney, fetal kidney, adult liver, fetal liver, adult lung, fetal lung, various regions of the brain, the spleen, bone marrow, lymph node, pancreas, salivary gland, pituitary gland, adrenal gland, spinal cord, thymus, stomach, small intestine, colon, bladder, trachea, breast, ovary, uterus, placenta, prostate, testis and adipose. Abbreviations are as described for Panels 1, 1.1, 1.2, and 1.3D.  
     [1042] Panels 2D and 2.2  
     [1043] The plates for Panels 2D and 2.2 generally include 2 control wells and 94 test samples composed of RNA or cDNA isolated from human tissue procured by surgeons working in close cooperation with the National Cancer Institute&#39;s Cooperative Human Tissue Network (CHTN) or the National Disease Research Initiative (NDRI). The tissues arc derived from human malignancies and in cases where indicated many malignant tissues have “matched margins” obtained from noncancerous tissue just adjacent to the tumor. These are termed normal adjacent tissues and are denoted “NAT” in the results below. The tumor tissue and the “matched margins” are evaluated by two independent pathologists (the surgical pathologists and again by a pathologist at NDRI or CHTN). This analysis provides a gross histopathological assessment of tumor differentiation grade. Moreover, most samples include the original surgical pathology report that provides information regarding the clinical stage of the patient. These matched margins are taken from the tissue surrounding (i.e. immediately proximal) to the zone of surgery (designated “NAT”, for normal adjacent tissue, in Table RR). In addition, RNA and cDNA samples were obtained from various human tissues derived from autopsies performed on elderly people or sudden death victims (accidents, etc.). These tissues were ascertained to be free of disease and were purchased from various commercial sources such as Clontech (Palo Alto, Calif.), Research Genetics, and Invitrogen.  
     [1044] Panel 3D  
     [1045] The plates of Panel 3D are comprised of 94 cDNA samples and two control samples. Specifically, 92 of these samples are derived from cultured human cancer cell lines, 2 samples of human primary cerebellar tissue and 2 controls. The human cell lines arc generally obtained from ATCC (American Type Culture Collection), NCI or the German tumor cell bank and fall into the following tissue groups: Squamous cell carcinoma of the tongue, breast cancer, prostate cancer, melanoma, epidermoid carcinoma, sarcomas, bladder carcinomas, pancreatic cancers, kidney cancers, leukemias/lymphomas, ovarian/uterine/cervical, gastric, colon, lung and CNS cancel cell lines. In addition, there are two independent samples of cerebellum. These cells are all cultured under standard recommended conditions and RNA extracted using the standard procedures. The cell lines in panel 3D and 1.3D are of the most common cell lines used in the scientific literature.  
     [1046] Panels 4D, 4R, and 4.1D  
     [1047] Panel 4 includes samples on a 96 well plate (2 control wells, 94 test samples) composed of RNA (Panel 4R) or cDNA (Panels 4D/4.1D) isolated from various human cell lines or tissues related to inflammatory conditions. Total RNA from control normal tissues such as colon and lung (Stratagene, La Jolla, Calif.) and thymus and kidney (Clontech) was employed. Total RNA from liver tissue from cirrhosis patients and kidney from lupus patients was obtained from BioChain (Biochain Institute, Inc., Hayward, Calif.). Intestinal tissue for RNA preparation from patients diagnosed as having Crohn&#39;s disease and ulcerative colitis was obtained from the National Disease Research Interchange (NDRI) (Philadelphia, Pa.).  
     [1048] Astrocytes, lung fibroblasts, dermal fibroblasts, coronary artery smooth muscle cells, small airway epithelium, bronchial epithelium, microvascular dermal endothelial cells, microvascular lung endothelial cells, human pulmonary aortic endothelial cells, human umbilical vein endothelial cells were all purchased from Clonetics (Walkersville, Md.) and grown in the media supplied for these cell types by Clonetics. These primary cell types were activated with various cytokines or combinations of cytokines for 6 and/or 12-14 hours, as indicated. The following cytokines were used; IL-1 beta at approximately 1-5 ng/ml, TNF alpha at approximately 5-10 ng/ml, IFN gamma at approximately 20-50 ng/ml, IL-4 at approximately 5-10 ng/ml, IL-9 at approximately 5-10 ng/ml, IL-13 at approximately 5-10 ng/ml. Endothelial cells were sometimes starved for various times by culture in the basal media from Clonetics with 0.1% serum.  
     [1049] Mononuclear cells were prepared from blood of employees at CuraGen Corporation, using Ficoll. LAK cells were prepared from these cells by culture in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco/Life Technologies, Rockville, Md.), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and Interleukin 2 for 4-6 days. Cells were then either activated with 10-20 ng/ml PMA and 1-2 μg/ml ionomycin, IL-12 at 5-10 ng/ml, IFN gamma at 20-50 ng/ml and IL-18 at 5-10 ng/ml for 6 hours. In some cases, mononuclear cells were cultured for 4-5 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) with PHA (phytohemagglutinin) or PWM (pokeweed mitogell) at approximately 5 μg/ml. Samples were taken at 24, 48 and 72 hours for RNA preparation. MLR (mixed lymphocyte reaction) samples were obtained by taking blood from two donors, isolating the mononuclear cells using Ficoll and mixing the isolated mononuclear cells 1:1 at a final concentration of approximately 2×10 6 cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol (5.5×10 −5 M) (Gibco), and 10 mM Hepes (Gibco). The MLR was cultured and samples taken at various time points ranging from 1-7 days for RNA preparation.  
     [1050] Monocytes were isolated from mononuclear cells using CD14 Miltenyi Beads, +ve VS selection columns and a Vario Magnet according to the manufacturer&#39;s instructions. Monocytes were differentiated into dendritic cells by culture in DMEM 5% fetal calf serum (FCS) (Hyclone, Logan, Utah), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco), 50 ng/ml GMCSF and 5 ng/ml IL-4 for 5-7 days. Macrophages were prepared by culture of monocytes for 5-7 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), 10 mM Hepes (Gibco) and 10% AB Human Serum or MCSF at approximately 50 ng/ml. Monocytes, macrophages and dendritic cells were stimulated for 6 and 12-14 hours with lipopolysaccharide (LPS) at 100 ng/ml. Dendritic cells were also stimulated with anti-CD40 monoclonal antibody (Pharmingen) at 10 μg/ml for 6 and 12-14 hours.  
     [1051] CD4 lymphocytes, CD8 lymphocytes and NK cells were also isolated from mononuclear cells using CD4, CD8 and CD56 Miltenyi beads, positive VS selection columns and a Vario Magnet according to the manufacturer&#39;s instructions. CD45RA and CD45RO CD4 lymphocytes were isolated by depleting mononuclear cells of CD8, CD56, CD14 and CD19 cells using CD8, CD56, CD14 and CD19 Miltenyi beads and positive selection. CD45RO beads were then used to isolate the CD45RO CD4 lymphocytes with the remaining cells being CD45RA CD4 lymphocytes. CD45RA CD4, CD45RO CD4 and CD8 lymphocytes were placed in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and plated at 10 6 cells/ml onto Falcon 6 welt tissue culture plates that had been coated overnight with 0.5 μg/ml anti-CD28 (Pharmingen) and 3 ug/ml anti-CD3 (OKT3, ATCC) in PBS. After 6 and 24 hours, the cells were harvested for RNA preparation. To prepare chronically activated CD8 lymphocytes, we activated the isolated CD8 lymphocytes for 4 days on anti-CD28 and anti-CD3 coated plates and then harvested the cells and expanded them in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and IL-2. The expanded CD8 cells were then activated again with plate bound anti-CD3 and anti-CD28 for 4 days and expanded as before. RNA was isolated 6 and 24 hours after the second activation and after 4 days of the second expansion culture. The isolated NK cells were cultured in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco) and IL-2 for 4-6 days before RNA was prepared.  
     [1052] To obtain B cells, tonsils were procured from NDRI. The tonsil was cut up with sterile dissecting scissors and then passed through a sieve. Tonsil cells were then spun down and resupended at 10 6  cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco). To activate the cells, we used PWM at 5 μg/ml or anti-CD40 (Pharmingen) at approximately 10 μg/ml and IL-4 at 5-10 ng/ml. Cells were harvested for RNA preparation at 24, 48 and 72 hours.  
     [1053] To prepare the primary and secondary Th1/Th2 and Tr1 cells, six-well Falcon plates were coated overnight with 10 μg/ml anti-CD28 (Pharmingen) and 2 μg/ml OKT3 (ATCC), and then washed twice with PBS. Umbilical cord blood CD4 lymphocytes (Poietic Systems, German Town, Md.) were cultured at 10 5 -10 6  cells/ml in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), 10 mM Hepes (Gibco) and IL-2 (4 ng/ml). IL-12 (5 ng/ml) and anti-IL4 (1 μg/ml) were used to direct to Th1, while IL-4 (5 ng/ml) and anti-IFN gamma (1 μg/ml) were used to direct to Th2 and IL-10 at 5 ng/ml was used to direct to Tr1. After 4-5 days, the activated Th1, Th2 and Tr1 lymphocytes were washed once in DMEM and expanded for 4-7 days in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5×10 −5 M (Gibco), 10 mM Hepes (Gibco) and IL-2 (1 ng/ml). Following this, the activated Th1, Th2 and Tr1 lymphocytes were re-stimulated for 5 days with anti-CD28/OKT3 and cytokines as described above, but with the addition of anti-CD95L (1 μg/ml) to prevent apoptosis. After 4-5 days, the Th1, Th2 and Tr1 lymphocytes were washed and then expanded again with IL-2 for 4-7 days. Activated Th1 and Th2 lymphocytes were maintained in this way for a maximum of three cycles. RNA was prepared from primary and secondary Th1, Th2 and Tr1 alter 6 and 24 hours following the second and third activations with plate bound anti-CD3 and anti-CD28 mAbs and 4 days into the second and third expansion cultures in Interleukin 2.  
     [1054] The following leukocyte cells lines were obtained from the ATCC: Ramos, EOL-1, KU-812. EOL cells were further differentiated by culture in 0.1 mM dbcAMP at 5×10 5 cells/ml for 8 days, changing the media every 3 days and adjusting the cell concentration to 5×10 5 cells/ml. For the culture of these cells, we used DMEM or RPMI (as recommended by the ATCC), with the addition of 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), 10 mM Hepes (Gibco). RNA was either prepared from resting cells or cells activated with PMA at 10 ng/ml and ionomycin at 1 μg/ml for 6 and 14 hours. Keratinocyte line CCD106 and an airway epithelial tumor line NCI-H292 were also obtained from the ATCC. Both were cultured in DMEM 5% FCS (Hyclone), 100 μM non essential amino acids (Gibco), 1 mM sodium pyruvate (Gibco), mercaptoethanol 5.5×10 −5 M (Gibco), and 10 mM Hepes (Gibco). CCD1106 cells were activated for 6 and 14 hours with approximately 5 ng/ml TNF alpha and 1 mg/ml IL-1 beta, while NCI-H292 cells were activated for 6 and 14 hours with the following cytokines: 5 ng/ml IL-4, 5 ng/ml IL-9, 5 ng/ml IL-13 and 25 ng/ml IFN gamma.  
     [1055] For these cell lines and blood cells, RNA was prepared by lysing approximately 10 7  cells/ml using Trizol (Gibco BRL). Briefly, 1/10 volume of bromochloropropane (Molecular Research Corporation) was added to the RNA sample, vortexed and after 10 minutes at room temperature, the tubes were spun at 14,000 rpm in a Sorvall SS34 rotor. The aqueous phase was removed and placed in a 15 ml Falcon Tube. An equal volume of isopropanol was added and left at −20° C. overnight. The precipitated RNA was spun down at 9,000 rpm for 15 min in a Sorvall SS34 rotor and washed in 70% ethanol. The pellet was redissolved in 300 μl of RNAse-free water and 35 μl buffer (Promega) 5 μl DTT, 7 μl RNAsin and 8 μl DNAse were added. The tube was incubated at 37° C. for 30 minutes to remove contaminating genomic DNA, extracted once with phenol chloroform and re-precipitated with 1/10 volume of 3M sodium acetate and 2 volumes of 100% ethanol. The RNA was spun down and placed in RNAse flee water. RNA was stored at −80° C.  
     [1056] AI_comprehensive panel_v1.0  
     [1057] The plates for AI_comprehensive panel_v1.0 include two control wells and 89 test samples comprised of cDNA isolated from surgical and postmortem human tissues obtained from the Backus Hospital and Clinomics (Frederick, Md.). Total RNA was extracted from tissue samples from the Backus Hospital in the Facility at CuraGen. Total RNA from other tissues was obtained from Clinomics.  
     [1058] Joint tissues including synovial fluid, synovium, bone and cartilage were obtained from patients undergoing total knee or hip replacement surgery at the Backus Hospital. Tissue samples were immediately snap frozen in liquid nitrogen to ensure that isolated RNA was of optimal quality and not degraded. Additional samples of osteoarthritis and rheumatoid arthritis joint tissues were obtained from Clinomics. Normal control tissues were supplied by Clinomics and were obtained during autopsy of trauma victims.  
     [1059] Surgical specimens of psoriatic tissues and adjacent matched tissues were provided as total RNA by Clinomics. Two male and two female patients were selected between the ages of 25 and 47. None of the patients were taking prescription drugs at the time samples were isolated.  
     [1060] Surgical specimens of diseased colon from patients with ulcerative colitis and Crohns disease and adjacent matched tissues were obtained from Clinomics. Bowel tissue from three female and three male Crohn&#39;s patients between the ages of 41-69 were used. Two patients were not on prescription medication while the others were taking dexamethasone, phenobarbital, or tylenol. Ulcerative colitis tissue was from three male and four female patients. Four of the patients were taking lebvid and two were on phenobarbital.  
     [1061] Total RNA from post mortem lung tissue from trauma victims with no disease or with emphysema, asthma or COPD was purchased from Clinomics. Emphysema patients ranged in age from 40-70 and all were smokers, this age range was chosen to focus on patients with cigarette-linked emphysema and to avoid those patients with alpha-lanti-trypsin deficiencies. Asthma patients ranged in age from 36-75, and excluded smokers to prevent those patients that could also have COPD. COPD patients ranged in age from 35-80 and included both smokers and non-smokers. Most patients were taking corticosteroids, and bronchodilators.  
     [1062] In the labels employed to identify tissues in the AI_comprehensive panel_v1.0 panel, the following abbreviations are used:  
     [1063] AI=Autoimmunity  
     [1064] Syn=Synovial  
     [1065] Normal=No apparent disease  
     [1066] Rep22 /Rep20=individual patients  
     [1067] RA=Rheumatoid arthritis  
     [1068] Backus=From Backus Hospital  
     [1069] OA=Osteoarthritis  
     [1070] (SS)(BA)(MF)=Individual patients  
     [1071] Ad=Adjacent tissue  
     [1072] Match control=adjacent tissues  
     [1073] -M=Male  
     [1074] -F=Female  
     [1075] COPD=Chronic obstructive pulmonary disease  
     [1076] Panels 5D and 5I  
     [1077] The plates for Panel 5D and 5I include two control wells and a variety of cDNAs isolated from human tissues and cell lines with an emphasis on metabolic diseases. Metabolic tissues were obtained from patients enrolled in the Gestational Diabetes study. Cells were obtained during different stages in the differentiation of adipocytes from human mesenchymal stem cells. Human pancreatic islets were also obtained.  
     [1078] In the Gestational Diabetes study subjects are young (18 - 40 years), otherwise healthy women with and without gestational diabetes undergoing routine (elective) Caesarean section. After delivery of the infant, when the surgical incisions were being repaired/closed, the obstetrician removed a small sample (&lt;1 cc) of the exposed metabolic tissues during the closure of each surgical level. The biopsy material was rinsed in sterile saline, blotted and fast frozen within 5 minutes from the time of removal. The tissue was then flash frozen in liquid nitrogen and stored, individually, in sterile screw-top tubes and kept on dry ice for shipment to or to be picked up by CuraGen. The metabolic tissues of interest include uterine wall (smooth muscle), visceral adipose, skeletal muscle (rectus) and subcutaneous adipose. Patient descriptions are as follows:  
                                                      Patient 2   Diabetic Hispanic, overweight, not on insulin           Patient 7-9   Nondiabetic Caucasian and obese (BMI &gt; 30)           Patient 10   Diabetic Hispanic, overweight, on insulin           Patient 11   Nondiabetic African American and overweight           Patient 12   Diabetic Hispanic on insulin                      
 
     [1079] Adipocyte differentiation was induced in donor progenitor cells obtained from Osirus (a division of Clonetics/BioWhittaker) in triplicate, except for Donor 3U which had only two replicates. Scientists at Clonetics isolated, grew and differentiated human mesenchymal stem cells (HuMSCs) for CuraGen based on the published protocol found in Mark F. Pittenger, et al., Multilineage Potential of Adult Human Mesenchymal Stem Cells Science Apr. 2, 1999: 143-147. Clonetics provided Trizol lysates or frozen pellets suitable for mRNA isolation and ds cDNA production. A general description of each donor is as follows:  
     [1080] Donor 2 and 3 U: Mesenchymal Stem cells, Undifferentiated Adipose  
     [1081] Donor 2 and 3 AM: Adipose, AdiposeMidway Differentiated  
     [1082] Donor 2 and 3 AD: Adipose, Adipose Differentiated  
     [1083] Human cell lines were generally obtained from ATCC (American Type Culture Collection), NCI or the German tumor cell bank and fall into the following tissue groups: kidney proximal convoluted tubule, uterine smooth muscle cells, small intestine, liver HepG2 cancer cells, heart primary stromal cells, and adrenal cortical adenoma cells. These cells are all cultured under standard recommended conditions and RNA extracted using the standard procedures. All samples were processed at CuraGen to produce single stranded cDNA.  
     [1084] Panel 5I contains all samples previously described with the addition of pancreatic islets from a 58 year old female patient obtained from the Diabetes Research Institute at the University of Miami School of Medicine. Islet tissue was processed to total RNA at an outside source and delivered to CuraGen for addition to panel 5I.  
     [1085] In the labels employed to identify tissues in the 5D and 5I panels, the following abbreviations are used:  
     [1086] GO Adipose=Greater Omentum Adipose  
     [1087] SK=Skeletal Muscle  
     [1088] UT=Uterus  
     [1089] Plt=Placenta  
     [1090] AD=Adipose Differentiated  
     [1091] AM=Adipose Midway Differentiated  
     [1092] U=Undifferentiated Stem Cells  
     [1093] Panel CNSD.01  
     [1094] The plates for Panel CNSD.01 include two control wells and 94 test samples comprised of cDNA isolated from postmortem human brain tissue obtained from the Harvard Brain Tissue Resource Center. Brains are removed from calvazia of donors between 4 and 24 hours after death, sectioned by neuroanatomists, and frozen at −80° C. in liquid nitrogen vapor. All brains are sectioned and examined by neuropathlologists to confirm diagnoses with clear associated neuropathology.  
     [1095] Disease diagnoses are taken from patient records. The panel contains two brains from each of the following diagnoses: Alzheimer&#39;s disease, Parkinson&#39;s disease, Huntington&#39;s disease, Progressive Supernuclear Palsy, Depression, and “Normal controls”. Within each of these brains, the following regions are represented: cingulate gyrus, temporal pole, globus palladus, substantia nigra, Brodman Area 4 (primary motor strip), Brodman Area 7 (parietal cortex), Brodman Area 9 (prefrontal cortex), and Brodman area 17 (occipital cortex). Not all brain regions are represented in all cases; e.g., Huntington&#39;s disease is characterized in part by neurodegeneration in the globus palladus, thus this region is impossible to obtain from confirmed Huntington&#39;s cases. Likewise Parkinson&#39;s disease is characterized by degeneration of the substantia nigra making this region more difficult to obtain. Normal control brains were examined for neuropathology and found to be free of any pathology consistent with neurodegeneration.  
     [1096] In the labels employed to identify tissues in the CNS panel, the following abbreviations are used:  
     [1097] PSP=Progressive supranuclear palsy  
     [1098] Sub Nigra=Substantia nigra  
     [1099] Glob Palladus=Globus palladus  
     [1100] Temp Pole=Temporal pole  
     [1101] Cing Gyr=Cingulate gyrus  
     [1102] BA 4=Brodman Area 4  
     [1103] Panel CNS_Neurodegeneration_V1.0  
     [1104] The plates for Panel CNS_Neurodegeneration_V1.0 include two control wells and 47 test samples comprised of cDNA isolated from postmortem human brain tissue obtained from the Harvard Brain Tissue Resource Center (McLean Hospital) and the Human Brain and Spinal Fluid Resource Center (VA Greater Los Angeles Healthcare System). Brains are removed from calvaria of donors between 4 and 24 hours after death, sectioned by neuroanatomists, and frozen at −80° C. in liquid nitrogen vapor. All brains are sectioned and examined by neuropathologists to confirm diagnoses with clear associated neuropathology.  
     [1105] Disease diagnoses are taken from patient records. The panel contains six brains from Alzheimer&#39;s disease (AD) patients, and eight brains from “Normal controls” who showed no evidence of dementia prior to death. The eight normal control brains are divided into two categories: Controls with no dementia and no Alzheimer&#39;s like pathology (Controls) and controls with no dementia but evidence of severe Alzheimer&#39;s like pathology, (specifically senile plaque load rated as level 3 on a scale of 0-3; 0=no evidence of plaques, 3=severe AD senile plaque load). Within each of these brains, the following regions are represented: hippocampus, temporal cortex (Brodman Area 21), parietal cortex (Brodman area 7), and occipital cortex (Brodman area 17). These regions were chosen to encompass all levels of neurodegeneration in AD. The hippocampus is a region of early and severe neuronal loss in AD; the temporal cortex is known to show neurodegeneration in AD after the hippocampus; the parietal cortex shows moderate neuronal death in the late stages of the disease; the occipital coitex is spared in AD and therefore acts as a “control” region within AD patients. Not all brain regions are represented in all cases.  
     [1106] In the labels employed to identify tissues in the CNS_Neurodegeneration_V1.0 panel, the following abbreviations are used:  
     [1107] AD=Alzheimer&#39;s disease brain; patient was demented and showed AD-like pathology upon autopsy  
     [1108] Control=Control brains; patient not demented, showing no neuropathology  
     [1109] Control (Path)=Control brains; patient not demented but showing sever AD-like pathology  
     [1110] SupTemporal Ctx=Superior Temporal Cortex  
     [1111] Inf Temporal Ctx=Inferior Temporal Cortex  
     [1112] GA. NOV41b and NOV41c (CG55676-02 and CG55676-03): GPCR-like  
     [1113] Expression of genes CG55676-02 and CG55676-03 were assessed using the primer-probe set Ag2378, described in Table GA. Results of the RTQ-PCR runs are shown in Tables GB-GF.  
                   TABLE GA                          Probe Name Ag2378                                                     Start               Primers   Sequences   Length   Position   SEQ ID No                                             Forward   5′-GTTCAGTGCCACTCAACAATG-3′   21   3   325                   Probe   FAM-5′-ATCCCATTGCCCATCAGACTGGCTTT-3′-   26   29   326           TAMRA               Reverse   5′-GCATCAGTGTGGCAAATAGTTT-3′   22   57   327                  
 
     [1114]               TABLE GB                          Panel A/I                                 Rel. Exp. (%)               tm8262f —             Tissue Name   Ag2378_A2                                         110967 COPD-F   2.0           110980 COPD-F   0.0           110968 COPD-M   1.7           110977 COPD-M   2.6           110989 Emphysema-F   3.1           110992 Emphysema-F   0.9           110993 Emphysema-F   2.2           110994 Emphysema-F   1.1           110995 Emphysema-F   2.9           110996 Emphysema-F   1.1           110997 Asthma-M   1.5           111001 Asthma-F   0.7           111002 Asthma-F   0.7           111003 Atopic Asthma-F   3.5           111004 Atopic Asthma-F   3.8           111005 Atopic Asthma-F   2.2           111006 Atopic Asthma-F   0.9           111417 Allergy-M   2.3           112347 Allergy-M   0.7           112349 Normal Lung-F   0.1           112357 Normal Lung-F   5.6           112354 Normal Lung-M   2.4           112374 Crohns-F   0.3           112389 Match Control Crohns-F   1.1           112375 Crohns-F   0.3           112732 Match Control Crohns-F   0.0           112725 Crohns-M   0.0           112387 Match Control Crohns-M   0.4           112378 Crohns-M   1.1           112390 Match Control Crohns-M   3.1           112726 Crohns-M   3.4           112731 Match Control Crohns-M   7.3           112380 Ulcer Col-F   2.5           112734 Match Control Ulcer Col-F   0.0           112384 Ulcer Col-F   1.6           112737 Match Control Ulcer Col-F   3.6           112386 Ulcer Col-F   0.0           112738 Match Control Ulcer Col-F   0.0           112381 Ulcer Col-M   1.3           112735 Match Control Ulcer Col-M   0.0           112382 Ulcer Col-M   1.1           112394 Match Control Ulcer Col-M   0.0           112383 Ulcer Col-M   3.3           112736 Match Control Ulcer Col-M   1.3           112423 Psoriasis-F   0.7           112427 Match Control Psoriasis-F   2.6           112418 Psoriasis-M   0.4           112723 Match Control Psoriasis-M   2.6           112419 Psoriasis-M   3.0           112424 Match Control Psoriasis-M   2.6           112420 Psoriasis-M   4.9           112425 Match Control Psoriasis-M   2.3           104689 (MF) OA Bone-Backus   30.4           104690 (MF) Adj “Normal” Bone-Backus   56.1           104691 (MF) OA Synovium-Backus   11.4           104692 (BA) OA Cartilage-Backus   5.0           104694 (BA) OA Bone-Backus   9.0           104695 (BA) Adj “Normal” Bone-Backus   75.1           104696 (BA) OA Synovium-Backus   10.1           104700 (SS) OA Bone-Backus   19.4           104701 (SS) Adj “Normal” Bone-Backus   23.4           104702 (SS) OA Synovium-Backus   100.0           117093 OA Cartilage Rep7   1.8           112672 OA Bone5   3.1           112673 OA Synovium5   1.1           112674 OA Synovial Fluid cells5   0.5           117100 OA Cartilage Rep 14   0.0           112756 OA Bone9   55.5           112757 OA Synovium9   0.9           112758 OA Synovial Fluid Cells9   0.4           117125 RA Cartilage Rep2   1.2           113492 Bone2 RA   5.9           113493 Synovium2 RA   1.1           113494 Syn Fluid Cells RA   3.5           113499 Cartilage4 RA   1.0           113500 Bone4 RA   2.2           113501 Synovium4 RA   0.2           113502 Syn Fluid Cells4 RA   0.3           113495 Cartilage3 RA   2.6           113496 Bone3 RA   1.6           113497 Synovium3 RA   1.1           113498 Syn Fluid Cells3 RA   1.7           117106 Normal Cartilage Rep20   0.1           113663 Bone3 Normal   0.3           113664 Synovium3 Normal   0.1           113665 Syn Fluid Cells3 Normal   0.2           117107 Normal Cartilage Rep22   1.2           113667 Bone4 Normal   0.8           113668 Synovium4 Normal   1.3           113669 Syn Fluid Cells4 Normal   1.3                        
     [1115]               TABLE GC                          Panel 1.3D                                 Rel. Exp., %               1.3dx4tm4870f —             Tissue Name   ag2378_a1                                         Liver adenocarcinoma   0           Pancreas   0           Pancreatic ca. CAPAN 2   4.1           Adrenal gland   0.2           Thyroid   0.5           Salivary gland   0.5           Pituitary gland   0.2           Brain (fetal)   0           Brain (whole)   0           Brain (amygdala)   0           Brain (cerebellum)   0           Brain (hippocampus)   0.1           Brain (substantia nigra)   0           Brain (thalamus)   0           Cerebral Cortex   0.9           Spinal cord   1           glio/astro U87-MG   0           glio/astro U-118-MG   0           astro SW1783   0.2           neuro; met SK-N-AS   0           astro SF-539   0.2           astro SNB-75   2.3           glio SNB-19   0           glio U251   0           glio SF-295   0           Heart (fetal)   0           Heart   0           Fetal Skeletal   2.4           Skeletal muscle   0.1           Bone marrow   0           Thymus   2.2           Spleen   1.9           Lymph node   0.2           Colorectal   0.4           Stomach   0.3           Small intestine   0           Colon SW480   0           Colon SW620(SW480 met)   0           Colon HT29   41.3           Colon HCT-116   0           Colon CaCo-2   9.4           Colon Ca. tissue(ODO3866)   100           Colon HCC-2998   0           Gastric(liver met) NCI-N87   2.8           Bladder   0.2           Trachea   2.1           Kidney   1           Kidney (fetal)   0.8           Renal 786-0   0           Renal A498   0           Renal RXF 393   0.2           Renal ACHN   0           Renal UO-31   4.9           Renal TK-10   0           Liver   0           Liver (fetal)   0.2           Liver (hepatoblast) HepG2   8.7           Lung   0.5           Lung (fetal)   0.4           Lung (small cell) LX-1   0           Lung (small cell) NCI-H69   0           Lung (s. cell var.) SHP-77   9.6           Lung (large cell)NCI-H460   0           Lung (non-sm. cell) A549   0           Lung (non-s. cell) NCI-H23   1           Lung (non-s. cell) HOP-62   1.6           Lung (non-s. cl) NCI-H522   0           Lung (squam.) SW 900   6.1           Lung (squam.) NCI-H596   0.2           Mammary gland   7.6           Breast (pl. ef) MCF-7   19.6           Breast (pl. ef) MDA-MB-231   0.3           Breast (pl. ef) T47D   4.2           Breast BT-549   0.8           Breast MDA-N   0           Ovary   2.5           Ovarian OVCAR-3   1.3           Ovarian OVCAR-4   0           Ovarian OVCAR-5   9.6           Ovarian OVCAR-8   0.2           Ovarian IGROV-1   0           Ovarian (ascites) SK-OV-3   0           Uterus   0           Plancenta   0.5           Prostate   0.9           Prostate (bone met)PC-3   2.3           Testis   1.1           Melanoma Hs688(A).T   0           Melanoma (met) Hs688(B).T   0           Melanoma UACC-62   0           Melanoma M14   0           Melanoma LOXIMVI   0           Melanoma (met) SK-MEL-5   0           Adipose   6.3                        
     [1116]               TABLE GD                          Panel 2D                                 Rel. Expr., %               2dx4tm4693f —             Tissue Name   ag2378_a2                                         Normal Colon   1.7           CCa 1   1.1           CCa 1 Margin   0.2           CCa 2   0           CCa 2 Margin   0.1           CCa 3   2.4           CCa 3 Margin   0.3           CCa 4   0.1           CCa 4 Margin   0.2           CCa 5 Metastasis   0           CCa 5 Margin (Liver)   0           CCa 6 Metastatsis   1.1           CCa 6 Margin (Lung)   0.6           Normal Prostate   14.6           PCa 1   2.2           PCa 1 Margin   3.7           PCa 2   1.2           PCa 2 Margin   1.5           Normal Lung   2.1           LCa 1 Metastasis   8           LCa 1 Margin (muscle)   0.7           LCa 2   3.9           LCa 2 Margin   0.6           LCa 3   0.7           LCa 3 Margin   1.9           LCa 4   1.6           LCa 4 Margin   0.6           LCa 5   3.2           LCa 5 Margin   0.3           Ocular Melanoma Metastasis   0.3           Liver Margin   0           Melanoma Metastasis   0.1           Lung Margin   1.2           Normal Kidney   3.2           RCC 1   0.6           RCC 1 Margin   2.1           RCC 2   1.1           RCC 2 Margin   2.6           RCC 3   0.2           RCC 3 Margin   2.3           RCC 4   0.2           RCC 4 Margin   1.4           RCC 5   0.4           RCC 5 Margin   0.8           RCC 6   3.1           RCC 6 Margin   5           RCC 7   0.1           RCC 7 Margin   1.2           RCC 8   19.2           RCC 8 Margin   2           RCC 9   3.2           RCC 9 Margin   1.5           Normal Uterus   0           UtCa   0.4           Normal Thyroid   3.6           ThyCa 1   2.6           ThyCa 2   2.1           ThyCa 2 Margin   4.8           Normal Breast   28.2           BCa 1   30.2           BCa 2   37.3           BCa 3 Metastasis   27.6           BCa 4 Metastasis   100           BCa 5   4.1           BCa 6   63.1           BCa 7   73.3           BCa 7 Margin   37.8           BCa 8   24           BCa 8 Margin   14           Normal Liver   0           HCC 1   0           HCC 2   0.2           HCC 3   0           HCC 4   0           HCC 4 Margin   0.5           HCC 5   0           HCC 5 Margin   0           Normal Bladder   0.5           TCC 1   0.3           TCC 2   0.3           TCC 3   25.9           TCC 3 Margin   0           Normal Ovary   1.3           OVCa 2   0           OVCa 2 Margin   0.7           Normal Stomach   1.9           GaCa 1   0.3           GaCa 1 Margin   1.3           GaCa 2   0           GaCa 2 Margin   0.6           GaCa 3   0           GaCa 3 Margin   0.8           GaCa 4   3.3                        
     [1117]               TABLE GE                          Panel 3D                                 Rel. Exp., %               3dx4tm5123f —             Tissue Name   ag2378_b1                                         Daoy- Medulloblastoma   0           TE671- Medulloblastoma   0           D283 Med- Medulloblastoma   0           PFSK-1- Primitive Neuroectodermal   0.9           XF-498- CNS   0.5           SNB-78- Glioma   0           SF-268- Glioblastoma   0           T98G- Glioblastoma   0           SK-N-SH- Neuroblastoma (metastasis)   0           SF-295- Glioblastoma   0           Cerebellum   0.1           Cerebellum   0.2           NCI-H292- Mucoepidermoid lung carcinoma   12.3           DMS-114- Small cell lung cancer   0           DMS-79- Small cell lung cancer   100           NCI-H146- Small cell lung cancer   1.6           NCI-H526- Small cell lung cancer   16.9           NCI-N417- Small cell lung cancer   0           NCI-H82- Small cell lung cancer   0           NCI-H157- Squamous cell lung cancer   0.2           (metastasis)           NCI-H1155- Large cell lung cancer   0.6           NCI-H1299- Large cell lung cancer   0           NCI-H727- Lung carcinoid   6.4           NCI-UMC-11- Lung carcinoid   0           LX-1- Small cell lung cancer   0           Colo-205- Colon cancer   0.4           KM12- Colon cancer   0           KM20L2- Colon cancer   29.9           NCI-H716- Colon cancer   0           SW-48- Colon adenocarcinoma   0           SW1116- Colon adenocarcinoma   0           LS 174T- Colon adenocarcinoma   0.3           SW-948- Colon adenocarcinoma   0           SW-480- Colon adenocarcinoma   0           NCI-SNU-5- Gastric carcinoma   0           KATO III- Gastric carcinoma   1           NCI-SNU-16- Gastric carcinoma   3.7           NCI-SNU-1- Gastric carcinoma   0.5           RF-1- Gastric adenocarcinoma   0           RF-48- Gastric adenocarcinoma   0.1           MKN-45- Gastric carcinoma   7.2           NCI-N87- Gastric carcinoma   8.7           OVCAR-5- Ovarian carcinoma   7.7           RL95-2- Uterine carcinoma   0           HelaS3- Cervical adenocarcinoma   0           Ca Ski- Cervical epidermoid carcinoma   0           (metastasis)           ES-2- Ovarian clear cell carcinoma   0.4           Ramos- Stimulated with PMA/ionomycin 6 h   0           Ramos- Stimulated with PMA/ionomycin 14 h   0           MEG-01- Chronic myelogenous leukemia   0           (megokaryoblast)           Raji- Burkitt&#39;s lymphoma   0           Daudi- Burkitt&#39;s lymphoma   0           U266- B-cell plasmacytoma   0           CA46- Burkitt&#39;s lymphoma   0           RL- non-Hodgkin&#39;s B-cell lymphoma   0           JM1- pre-B-cell lymphoma   0           Jurkat- T cell leukemia   0.2           TF-1- Erythroleukemia   0           HUT 78- T-cell lymphoma   0.1           U937- Histiocytic lymphoma   0           KU-812- Myelogenous leukemia   0           769-P- Clear cell renal carcinoma   0           Caki-2- Clear cell renal carcinoma   0           SW 839- Clear cell renal carcinoma   0           G401- Wilms&#39; tumor   0           Hs766T- Pancreatic carcinoma (LN   11.8           metastasis)           CAPAN-1- Pancreatic adenocarcinoma   9.7           (liver metastasis)           SU86.86- Pancreatic carcinoma (liver   15.1           metastasis)           BxPC-3- Pancreatic adenocarcinoma   14.4           HPAC- Pancreatic adenocarcinoma   8.8           MIA PaCa-2- Pancreatic carcinoma   0           CFPAC-1- Pancreatic ductal adenocarcinoma   24.4           PANC-1- Pancreatic epithelioid ductal   0           carcinoma           T24- Bladder carcinma (transitional cell)   10.3           5637- Bladder carcinoma   12.6           HT-1197- Bladder carcinoma   4           UM-UC-3- Bladder carcinma (transitional   0           cell)           A204- Rhabdomyosarcoma   17.4           HT-1080- Fibrosarcoma   0           MG-63- Osteosarcoma   0.1           SK-LMS-1- Leiomyosarcoma (vulva)   0           SJRH30- Rhabdomyosarcoma (met to   0           bone marrow)           A431- Epidermoid carcinoma   0           WM266-4- Melanoma   1.6           DU 145- Prostate carcinoma (brain   0           metastasis)           MDA-MB-468- Breast adenocarcinoma   4.9           SCC-4- Squamous cell carcinoma of tongue   0.5           SCC-9- Squamous cell carcinoma of tongue   0           SCC-15- Squamous cell carcinoma of tongue   0           CAL27- Squamous cell carcinoma of tongue   0                        
     [1118]               TABLE GF                          Panel 4D                                 Rel. Exp., %               4dx4tm4604f —             Tissue Name   ag2378_b2                                         Secondary Th1 act   10.3           Secondary Th2 act   20.2           Secondary Tr1 act   13.4           Secondary Th1 rest   0.4           Secondary Th2 rest   1.4           Secondary Tr1 rest   2.5           Primary Th1 act   38.1           Primary Th2 act   46.1           Primary Tr1 act   65.3           Primary Th1 rest   11           Primary Th2 rest   9.2           Primary Tr1 rest   4.2           CD45RA CD4 lymphocyte act   2.8           CD45RO CD4 lymphocyte act   10.4           CD8 lymphocyte act   0.4           Secondary CD8 lymphocyte rest   0.5           Secondary CD8 lymphocyte act   0.8           CD4 lymphocyte none   0           2ry Th1/Th2/Tr1_anti-CD95 CH11   9.7           LAK cells rest   0.9           LAK cells IL-2   0.9           LAK cells IL-2 + IL-12   2.5           LAK cells IL-2 + IFN gamma   2.9           LAK cells IL-2 + IL-18   2           LAK cells PMA/ionomycin   5.4           NK Cells IL-2 rest   0           Two Way MLR 3 day   0           Two Way MLR 5 day   0.8           Two Way MLR 7 day   1.9           PBMC rest   0           PBMC PWM   2.8           PBMC PHA-L   4.2           Ramos (B cell) none   0           Ramos (B cell) ionomycin   0           B lymphocytes PWM   8.3           B lymphocytes CD40L and IL-4   0.5           EOL-1 dbcAMP   0           EOL-1 dbcAMP PMA/ionomycin   0           Dendritic cells none   0.2           Dendritic cells LPS   0           Dendritic cells anti-CD40   0           Monocytes rest   0           Monocytes LPS   0           Macrophages rest   0           Macrophages LPS   0.4           HUVEC none   0           HUVEC starved   0           HUVEC IL-1beta   0.3           HUVEC IFN gamma   0           HUVEC TNF alpha + IFN gamma   0           HUVEC TNF alpha + IL4   0           HUVEC IL-11   0           Lung Microvascular EC none   1.3           Lung Microvascular EC TNFalpha +   0.3           IL-1beta           Microvascular Dermal EC none   0           Microsvasular Dermal EC TNFalpha +   0           IL-1beta           Bronchial epithelium TNFalpha +   0.3           IL1beta           Small airway epithelium none   0.4           Small airway epithelium TNFalpha +   4.4           IL-1beta           Coronery artery SMC rest   0.3           Coronery artery SMC TNFalpha +   0.5           IL-1beta           Astrocytes rest   0           Astrocytes TNFalpha + IL-1beta   0.7           KU-812 (Basophil) rest   0           KU-812 (Basophil) PMA/ionomycin   0           CCD1106 (Keratinocytes) none   1.3           CCD1106 (Keratinocytes) TNFalpha +   1.3           IL-1beta           Liver cirrhosis   1.4           Lupus kidney   0.3           NCI-H292 none   100           NCI-H292 IL-4   64.9           NCI-H292 IL-9   90.2           NCI-H292 IL-13   28.6           NCI-H292 IFN gamma   38.3           HPAEC none   0           HPAEC TNF alpha + IL-1 beta   0           Lung fibroblast none   2.2           Lung fibroblast TNF alpha + IL-1 beta   1.5           Lung fibroblast IL-4   0           Lung fibroblast IL-9   0.4           Lung fibroblast IL-13   0           Lung fibroblast IFN gamma   0.4           Dermal fibroblast CCD1070 rest   0.7           Dermal fibroblast CCD1070 TNF alpha   0.5           Dermal fibroblast CCD1070 IL-1 beta   0           Dermal fibroblast IFN gamma   0           Dermal fibroblast IL-4   0           IBD Colitis 1   0           IBD Colitis 2   0           IBD Crohn&#39;s   0           Colon   1.3           Lung   2           Thymus   11.8           Kidney   8.8                        
     [1119] Expression in panel 4D: CG55676-02 is expressed highly during initial activation and polarization of T cells regardless of whether polarization is to Th1, Th2 or Tr1 pathway. It is not expressed in untreated CD4 T cells and the level of expression is much less in chronically activated T cells.  
     [1120] Role in inflammation: CG55676-02 is a putative GPCR and may play an important role in the regulation of or cell polarization, differentiation, and T cell trafficking.  
     [1121] Potential therapeutic value: Antagonistic antibodies, preferably fully human monoclonal antibodies directed against the protein encoded for by CG55676-02 could reduce or block inflammation by blocking ligand interaction with this putative GPCR and preventing T cell function in diseases such as asthma, emphysema, allergy, arthritis, diabetes, and psoriasis. Alternatively, if this putative GPCR down regulates T cell activation then agonistic antibodies (Ligand-like) could also block inflammation in these diseases (Bromley et al, J. Immunol. 165(1) 15-9).  
     [1122] Expression in panel of relevance to Oncology 1.3D and 2D: In Panel 1.3D, CG55676-02 is expressed in tumor derived cell lines especially from colon, lung, ovarian and breast cancers. In panel 2D it is overexpressed in breast, lung and bladder tumor tissues compared to normal adjacent tissues.  
     [1123] Role in inflammation: CG55676-02 is a putative GPCR and may play a role tumor cell growth  
     [1124] Potential therapeutic value: Antagonistic antibodies, preferably fully human monoclonal antibodies directed against the protein encoded for by CG55676-02 could reduce or block tumor growth by blocking ligand interaction with this putative GPCR resulting in therapeutic treatment for tumor like lung, breast, bladder, kidney and colon.  
     [1125] A/I panel: The transcript of CG55676-03 is found in bone of 4 out of 4 patients with osteoarthritis and in synovium from 1 out of 4 patients.  
     [1126] Role in inflammation: CG55676-03 encodes a transcript for a putative GPCR that is expressed on cells within the bone and in the synovium of patients with osteoarthritis.  
     [1127] Potential therapeutic value: Antagonistic antibodies, preferably fully human monoclonal antibodies or small molecule therapeutics directed against the protein encoded for by CG55676-03 could reduce or block inflammation by preventing ligand interaction with this putative GPCR and as asthma, emphysema, allergy, arthritis, diabetes, and psoriasis.  
     [1128] Other Embodiments  
     [1129] Although particular embodiments have been disclosed herein in detail, this has been done by way of example for purposes of illustration only, and is not intended to be limiting with respect to the scope of the appended claims, which follow. In particular, it is contemplated by the inventors that various substitutions, alterations, and modifications may be made to the invention without departing from the spirit and scope of the invention as defined by the claims. The choice of nucleic acid starting in aterial, clone of interest, or library type is believed to be a matter of routine for a person of ordinary skill in the art with knowledge of the embodiments described herein. Other aspects, advantages, and modifications considered to be within the scope of the following claims. The claims presented are representative of the inventions disclosed herein. Other, unclaimed inventions are also contemplated. Applicants reserve the right to pursue such inventions in later claims.