HODGKIN'S DISEASE ASSOCIATED MOLECULES AND USES THEREOF

Abstract: The invention describes identifications and isolation of molecules associated specifically with Hodgkin's Disease. Uses of the molecules are described as well.

Description: HODGKIN'S DISEASE ASSOCIATED MOLECULES AND USES THEREOF RELATED APPLICATIONS This application is a continuation-m-part of Serial No. 08/644,116 filed May 10, 1996, which is a contmuation- m-part of Serial No. 08/580,980, filed on January 3, 1996, which is a continuation-m-part of application Serial No. 08/479,328, filed on June 7, 1995, both of which are pending, and are incorporated by reference. FIELD OF THE INVENTION This invention relates to methodologies for identifying molecules of interest. In particularly preferred embodiments, the invention relates to the identification of molecules associated with pathological conditions such as cancer, (melanoma or renal cancer, e.g.) , Hodgkm's Disease, autoimmune diseases and so forth. Also a part of the invention are the isolated molecules found as a result of the inventive method, such as presented peptides. These molecules include, inter alia, protem-containmg molecules, isolated nucleic acid molecules encoding these, and antibodies which specifically bind to the protem-containmg molecules. For convenience, the method described herein will be referred to as "serological fishing". BACKGROUND AND PRIOR ART It is fairly well established that many pathological conditions, such as infections, cancer, autoimmune disorders, etc., are characterized by the inappropriate expression of certain molecules. These molecules thus serve as "markers" for a particular pathological or abnormal condition. Apart from their use as diagnostic "targets", i.e., materials to be identified to diagnose these abnormal conditions, the molecules serve as reagents which can be used to generate diagnostic and/or therapeutic agents. A by no means limiting example of this is the use of cancer markers to produce antibodies specific to a particular marker. Yet another non-limiting example is the use of a peptide which complexes with an MHC molecule, to generate cytolytic T cells against abnormal cells. Preparation of such materials, of course, presupposes a source of the reagents used to generate these. Purification from cells is one laborious, far from certain method of doing so. Another preferred method is the isolation of nucleic acid molecules which encode a particular marker, followed by the use of the isolated encoding molecule to express the desired molecule. To date, two strategies have been employed for the detection of such antigens in, e.g., human tumors. These will be referred to as the genetic approach and the biochemical approach. The genetic approach is exemplified by, e.g., DePlaen et al. , Proc. Natl . Acad. Sci. USA 85: 2275 (1988) , incorporated by reference. In this approach, several hundred pools of plasmids of a cDNA library obtained from a tumor are transfected into recipient cells, such as COS cells, or into antigen-negative variants of tumor cell lines which are tested for the expression of the specific antigen. The biochemical approach, exemplified by, e.g., Falk et al . , Nature 351: 290 (1991) , and Kawakami et al., Nature 369: 69 (1994) both of which are incorporated by reference, is based on acidic elution of peptides which are bound to MHC-I molecules of tumor cells, followed by reversed-phase high performance liquid chromotogaphy (R-HPLC) . Antigenic peptides are identified after they bind to empty MHC-I molecules of mutant cell lines which are defective in antigen processing, and induction of specific reactions in cytolytic T-lymphocytes. These reactions include CTL proliferation, TNF release, and lysis of target cells, measurable in an MTT assay, or a 51 Cr release assay. These two approaches to the molecular definition of antigens have the following disadvantages: first, they are enormously cumbersome, time-consuming and expensive; second, they depend on the establishment of cytolytic T cell lines (CTLs) with predefined specificity; third, their relevance m vivo for the course of the pathology or disease in question has not been proven, as the respective CTLs can be obtained not only from patients with the respective disease, but also from healthy individuals, depending on their T cell repertoire. The problems inherent to the two known approaches for the identification and molecular definition of antigens is best demonstrated by the fact that both methods have, so far, succeeded in defining only very few new antigens in human tumors. See, e.g., van der Bruggen et al . , Science 254: 1643-1647 (1991) ; Brichard et al . , J. Exp. Med. 178: 489-495 (1993) ; Coulie, et al . , J. Exp. Med. 180: 35-42 (1994) , Kawakami et al . , Proc. Natl. Acad. Sci. USA 91: 3515-3519 (1994) . It would be desirable to have available a method which can be used not only for detection of tumor-associated antigens, but to determine molecules associated with any abnormal or pathological condition. Such a method would also facilitate the identification of such molecules, thereby enabling their use on the generation of, e.g. , antibodies, cytolytic T cells, and so forth. It is therefore the purpose of the present invention to develop methods and reagents for the simple detection and molecular characterization of antigens in human tissues, especially in tumor cells, which are useful in the molecular diagnosis of diseases and/or for immunotherapy and gene therapy of infectious, autoimmune and malignant diseases. The invention is delineated in the disclosure which follows. BRIEF DESCRIPTION OF THE FIGURES Figure 1 shows the principles of the approach of the invention. Figure 2 shows a nitrocellulose membrane with a positive clone derived from the cDNA of a renal cell clear carcinoma that reacts with a 1:100 dilution of the patient's serum. Figure 3 shows, in bar graph form, the Northern Blot analysis of clone HOM-RCC-313 in renal cell carcinoma, normal kidney and other human tissues. Figure 4 shows the translated region of the gene coding for HOM-RCC-313. It is also SEQ ID NO: 4. DETAILED DESCRIPTION OF PREFERRED EMBODIMENTS The following disclosure describes a methodology referred to as serological fishing. In it, a cell sample is taken from a subject afflicted with a pathological condition. The cells preferably are exemplary of the pathology. For example, if the subject has melanoma, the cells are melanoma cells. If the subject is suffering from a neural disorder, e.g., then the cells are preferably a sample of the afflicted cells. This approach is warranted because the afflicted cells are most probably the best source of protem-containmg molecules of interest, i.e., such molecules which are specifically associated with the pathological condition of interest. Note that cells representative of pathological conditions are not the only cells which may be used m the inventive method. It is very important, e.g., to ascertain those cellular "markers" associated with differentiation and maturation of cells, for example. The example of hematopoietic stem cells comes to mind. Similarly, the invention contemplates the isolation of, e.g., receptor molecules for specific ligands. In effect, one can assay for the presence of any molecule of interest using this methodology. The cells chosen are then used to prepare a library of complementary DNA (i.e., "cDNA") . This methodology is well known to the skilled artisan, and need not be reiterated here. It is, of course, based upon the established fact that if proteins are expressed by the cells, then messenger RNA (mRNA) must be present. These mRNA molecules are not long lived, and are unstable, so they are not practical to work with. The stability brought to the molecules when cDNA is used is very helpful to the method. Once the cDNA is made, it is used to construct a vector library. In short, carrier vectors are treated, such as by cutting and splicing, to receive molecules of cDNA. The choice of vector may vary, as the skilled artisan is well familiar with many such examples. Especially preferred are virus based vectors. In the case of eukaryotic cells, retrovirus or adenovirus based vectors are preferred. Such vectors contain all or a part of a viral genome, such as long term repeats ("LTRs") , promoters (e.g., CMV promoter, SV40 promoter, RSV promoter) , enhancers, and so forth. When the host cell is a prokaryote, then bacterial viruses, i.e., phages, are preferred. Exemplary of such vectors are vectors based upon, e.g., lambda phage. In any case, the vector may comprise elements of more than one virus. The resulting vectors are transfected or transformed into a host cell, which may be eukaryotic or prokaryotic. Any cell normally used for transfection or transformation may be used in the protocol. Preferred materials include strains of E. coli, CHO cells such as CHO-1, COS cells such as COS-7, and so forth. Similarly, yeast cells, e.g., strains of Saccharomyces, strains of Pseudomonas, such as Pseudomonas aerugmosa. Bacillus bacteria, well known insect host cell Spodoptera frugiperda, and so forth, may all be used. Once the recipient cells receive the vectors, they are cultivated so as to express foreign, protein containing molecules. "Protein-contammg" is used herein because, while prokaryotes express only proteins, eukaryotic cells are well known for their ability to post-translationally modify proteins, so as to produce glycoprotems, lipoprotems, e.g. It must also be borne in mind that "protein containing" as used herein, also encompasses peptides, such as the peptides presented by MHC molecules. The processes now described below take place independently of the process described above, and no chronological relationship between the two facets of the invention is intended. In pathological conditions such as cancer and, e.g., autoimmune diseases, there is some immune reaction to molecules associated with the pathology. This reaction can include an antibody response, B cell proliferation, proliferation of specific T cell subpopulations, increases m cytokme production, and so forth. The molecules and cells associated with the response may be found m body fluids of a subject, such as his or her serum. The immune responders will react with the molecule of interest whether it is produced recombmantly or autologously. The problem is to find them. As the examples show, this is done in a unique way. First, the body fluid, or other sample of interest, is reacted with a sample of the same host cells used for transfection or transformation. In this first step, the host cells are not transfected or transformed. The effect of this is to strip any immunogenic binding partners specific for the host cell rather than the targeted molecule. This step is necessary because, as was pointed out, supra, the host cell may be one against which the subject has developed an immune response at some point. This first stripping removes these immune components. A second stripping step is then carried out. In this step, the previously stripped sample is now reacted with a sample of the same host cell as was described supra, this time having been transfected or transformed with the carrier vector lacking cDNA from the subject. The reason for this second stripping step is an observation made by one of the present inventors and not reported in the literature previously. The materials used as vectors, such as phages, viruses, etc., are useful because they naturally infect cells. Thus, E. coll, which inhabit the lower intestine of humans, are infected with lambda phage. It had not been considered, previously, that the immune response to E. coli includes a response to these infectious agents. Thus, applicants have surprisingly, achieved an ability to remove interfering immune components to an unprecedented degree by carrying out the two stripping steps. As noted, the first is against untransfected or untransformed host cells. The second is against host cells transfected or transformed with a vector which does not carry cDNA, wherein the vector is immunologically equivalent to the vector used to carry cDNA, as described supra. It is especially preferred to carry out each of these stripping steps using a plurality of similar, but different procedures. The experiments which follow, for example, show absorption on a solid phase column, and then absorption on nitrocellulose paper. Applicants do not wish to be bound by any theory as to why the use of two similar but different protocols produces the results described herein. It is to be borne in mind, hereafter, that whenever "contacting a sample" is used herein, it is not to be limited to one contact step only, but may refer to more than one, preferably different, contact protocols designed to remove interfering binding partners from a sample under scrutiny. It should be understood that these stripping steps may be done completely independently of the steps used to prepare the cDNA library. For example, if the test for an antigen is to be done at day "O", the stripping of sample may be done the day before, a week before, and so forth. One can also "bank" stripped sample from a donor or subject for future use. The sample used is preferably serum, but need not be. Any sample which contains immunogenic binding partners may be so used. In the next step of the method, lysed, transfected cells carrying the cDNA and expressing heterologous protein are contacted with the twice stripped sample. This sample should only contain immune components specific for the heterologous protein, and should bind thereto. This binding is facilitated if the cell lysates have been immobilized via contact to, e.g., activated filter paper, a solid phase column, etc., but this solid phase binding is not necessary, as the art will surely recognize that many, varied forms of assays are available for identifying a molecule of interest. Once the immune component binds to the target molecule, a further step is desirably, but not necessarily, carried out. This additional step involves the use of some binding partner for the first immune component, such as anti-IgG, carrying an identifiable label. The label may be a dye, an enzyme, a gold particle, a radiolabel, or any of the standard labels used in immunoassays . Once identification is carried out, the immune components are removed, leaving the target molecule. The target molecule is then studied, using any of the standard methodologies in the art. The artisan will note that the methodology also results in isolation of immune components which bind to the molecule of interest. Thus, in another aspect of the invention one can isolate antibodies, e.g., which are specific binding partners for the molecule of interest. Yet another immune component which may be identified and isolated following the invention is a cytolytic T cell ("CTL" hereafter) , specific for complexes of peptides derived from the identified molecule and MHC molecules to which these peptides bind, forming a complex. It is fairly well accepted that a CTL response involves the identification of complexes of MHC molecules and peptides, generally about 8-12 amiho acids in length, but most preferably 9 or 10 amino acids in length, by T cell receptors ("TCRs") on the surface of circulating T cells. The TCRs react by binding to these complexes, "setting m motion, " as it were, a series of reactions including the proliferation of CTLs specific for these complexes. One can produce and/or isolate such CTLs using the method of the invention, plus further steps. As is pointed out in the examples which follow as well as the disclosure in general, one can easily identify cDNA encoding an antigen of interest. Once the cDNA is identified, one uses it to transfect host cells which either already present desired MHC molecules on their surface, or which have been transfected with DNA encoding these MHC molecules. The cDNA for the molecule of interest is expressed, and the molecule is processed to antigenic peptides which are presented by MHC molecules, such as HLA molecules. CTLs directed against the complexes are obtained from lymphocytes, such as autologous lymphocytes. From responder cell populations, long-term CTL clones are then obtained by the well known technique of limiting dilution. Once a positive CTL response is observed, the specific peptides presented to the CTLs are identified using established methods for example, screening the specific of previously identified CTL clones. Alternatively, the more recently described method of studying the sequence of the molecule of interest to identify potential MHC-bmdmg motifs then analyzing these peptides, first for binding to the relevant MHC molecule and then, if positive for MHC-bmdmg, for their ability to generate CTLs recognizing the peptide MHC complex may be used. Of course the peptides can also be eluted from the cells and sequenced, using well known techniques. It will also be noted by the skilled artisan that one can correlate the expression of the molecule of interest back to a particular host cell or cells which expressed it. In so doing, one can remove the cDNA which expressed the molecule of interest, sequence it, and so forth. This aspect of the method is another feature of the invention. Specific embodiments of the invention will be seen m the examples which follow. Figure 1 depicts the method generally. Example 1 For the establishment of a cDNA library from human tissue total RNA was obtained from 0.5 ug of a renal clear cell carcinoma and established according to the method of Chomzynski, J. Analyt . Biochem. 162: 156-159 (1987) , incorporated by reference. The mRNA was extracted from total RNA with oligo-dT-cellulose . The synthesis of the first strand cDNA was accomplished by the method described by Gubler and Hoffmann, Gene 25: 263 (1983) using RNase H and DNA polymerase I . For adaptation of the cDNA Klenow enzyme, adaptors with EcoRI restriction enzyme sites were ligated to the cDNA ends using T4 DNA ligase (Ferretti L and Sgamerella V, Nucl . Acids Res. 9: 3695 (1981)) . Following restriction enzymatic digestion with the enzyme Xhol, cDNA molecules of different length were separated using Sephacryl 400 and transfected into λZAPII phage vectors (Short et al . , Nucleic Acids Res. 16: 7583 (1988)) . The recombinant phage DNA was packed into phages after ligation with packing extracts and used for the transfection of E. coli bacteria. The titration of the library resulted in 1.8 x 10 6 recombinant primary clones. The total cDNA library was transfected in E. coli and amplified. The titer of the cDNA library after amplification was 10 11 plaque forming units per ml (pfu/ml) . These transfected cells were used in experiments which follow. Example 2 In accordance with the invention as described, supra, identification of immunogenic material was achieved by using human sera which have been completely depleted of antibodies directed against antigens derived from native and lytic λ phage-transfected E. coli bacteria. To this end, the serum was "stripped" via absorption, as now described. E. coli bacteria of the strain XLl-Blue were cultured in 50 ml LB medium overnight. After achieving an optical density of OD 600 = 1.0, the bacteria were pelleted by centrifugation, resuspended in 5 ml phosphate buffered saline (PBS) , and sonicated by ultrasound to form a lysate. The bacterial lysate was bound onto a matrix of activated Sepharose, which was then put into a column and used for the absorption of the human serum. The serum was run over this column 10 times. A culture of E. coli XLl-Blue bacteria m the exponential growth phase was pelleted by centrifugation, transfected m 0.01 M magnesium sulfate with 10 6 λZAPII phages without a recombinant insert and incubated in 5 ml LB medium for four hours. The lysate of the transfected bacteria was used in the same manner as the untransfected bacteria, with the human serum described supra being passed through the column an additional ten times. To complete the depletion of the serum, interfering antibodies from lytically transfected E. coli bacteria were cultured on agar plates (10 hours, 37°C) and their proteins were blotted onto nitrocellulose membranes after this culturmg step. Following this, the serum which had been preabsorbed according to the above steps was transferred to the blotted nitrocellulose membrane, and the absorption procedure was repeated five times. The serum, which was processed in accordance with the invention, was totally depleted of antibodies directed against antigens derived from E. coli and phages. Example 3 In these experiments, a renal cancer-specific antigen was identified via the following steps. Bacteria of the strain E. coli XLl-Blue were transfected with recombinant phages derived from the described cDNA library and plated at a density of 4-5xl0 3 plaque forming units (PFUs) per plate in LB-medium with isopropylthiogalactopyranoside ("IPTG") . After 12 hours of incubation at 37°C, nitrocellulose membranes were put on top of the cultures, and the culture plates were incubated for another four hours. This was followed by incubation of the nitrocellulose membrane for one hour in Tris-buffered saline (TBS) with 5% milk powder. After washing the nitrocellulose membranes three times in TBS, the stripped human serum secured following Example 2 was diluted 1:1000 in TBS/0.5% milk powder (w/v) and incubated overnight with gentle shaking. After the incubation with the nitrocellulose membrane the serum was removed and kept for additional testing. Following incubation with serum, the nitrocellulose membranes were washed three times in TBS, and incubated with polyclonal alkaline phosphatase- conjugated goat anti-human IgG for one hour. Following this, the nitrocellulose membranes were washed repeatedly with TBS/0.01% Tween 20 (v/v) ) . The reaction was developed using nitroblue tetrazolium chloride and bromochloro- indoyl-phosphate in TBS. The binding of human antibodies to the expressed protein became visible by a blue, ring- formed color deposit on the nitrocellulose membrane. The efficient preabsorption of the serum made it possible to develop the membrane at 37°C over several hours without compromising the quality of the test because of background reactivity caused by antibodies against E. coli and phage antigens. Positive clones were localized on the agar plates, transferred into transfection buffer, and used for a second round of transfection and subcloning. A total of 1.8xl0 6 recombinant clones were subjected to screening and five different positive-reacting clones were identified. Example 4 Positive clones secured following Example 3, i.e., those which had bound antibodies derived from the processed human serum, were subcloned to monoclonality by repeated rounds of transfection and testing of reactivity with the processed human serum. P-bluescript phagemids with the respective cDNA inserts were cloned by in vivo excision (Hay and Short, Strategies 5: 16-19, 1992) from the λZAPII phage vectors and used for transfection of E. coli SOLR bacteria. Plasmids were isolated from the bacteria after alkaline lysis with NaOH m a modification of the method of Birnboim and Doly, J. Nucl . Acids Res. 7: 1513 (1979) . The recombinant plasmid DNA was sequenced according to the classic method of Sanger (Proc. Natl. Acad. Sci. USA 74: 5463 (1977)) using M13-forward and M13-reverse oligonucleotides. The DNA sequence obtained and the resulting ammo acid sequence were checked for in nucleic acid and protein data banks (Gene Bank, EMBL, Swiss Prot) . The sequencing of the cDNA inserts was continued using internal oligonucleotides. Analysis showed no homology with any sequences deposited m the data banks. The full length cDNA clone referred to as SK313, which had been cloned with the RACE method (Frohman MA, Dush MK, Martm GR, Proc. Natl. Acad Sci. USA 85: 8998 (1988)) , had a carbonic anhydrase domain at the 5' end. The nucleic acid sequence of this molecule is presented m SEQ ID NO: 1. Figure 2 shows a nitrocellulose membrane with a positive clone from these experiments. Example 5 As a follow up to these experiments, RNA was isolated from a spectrum of malignant and normal human tissues according to the method of Chomzynski and Sacchi, Analyt Biochem. 162: 156 (1987) . After denaturation, the total isolated RNA was separated on an agarose gel containing 1% formaldehyde by electrophoresis (Goldberg, Proc. Natl. Acad. Sci. USA 77: 5794 (1980)) and then blotted onto a nylon membrane according to a known method (Seed, Nucl. Acids Res. 10: 1799 (1982)) Radiolabeled cDNA inserts of the identified clones were used for hybridization. The hybridization was carried out according to a known method (Geoffrey and Berger, Enzymol . 152: 419 (1987)) . The presence of the respective RNA was demonstrated using autoradiography and X-ray films. The analysis demonstrated that the mRNA of clone HOM-RCC-313 was overexpressed in 4 out of 19 renal cell carcinomas compared to normal kidneys. Very weak expression was found only in colonic mucosal tissue and in normal kidney. Expression in other tissues could not be demonstrated. Example 6 To determine the incidence of antibodies against antigens which are identified in accordance with the invention, sera from healthy individuals and tumor patients were analyzed. To this end, the sera were processed as described, supra, and depleted of antibodies against antigens derived from E. coli and phages. For the detection of antigen-specific antibodies, phages derived from reactive clones were mixed with non-reactive phages derived from the same cDNA library at a ratio of 1:10 and tested as described supra, for reactivity with antibodies in the human test serum. The serum which had been used for the identification of the antigen was used as a positive clone. The non-reactive phages served as a negative control. A serum sample was positive for antigen reactive antibodies, if the expected percentage of the phage plaques showed a positive reaction. In the case of the renal cell carcinoma antigen represented by clone HOM-RCC-313, the analysis of a spectrum of human sera showed that only sera from renal cell carcinoma patients contained reactive antibodies. Sera from healthy controls and patients with other tumors did not contain such antibodies. The cDNA for clone HOM-RCC-313 was excised from the plasmid DNA by digestion with the restriction enzyme EcoRI , and separated by agarose gel electrophoresis, followed by extraction from the gel. This was then used to create a vector which expresses a fusion protein with the bacterial protein anthranilate synthetase. A relevant fragment in the exact open reading frame was cloned into pATH plasmid vectors (Koerner, et al, Meth. Enzymol . 194: 477 (1991) . Induction of protein expression was obtained after transformation of the plasmids into E. coli of strain BL21 as described (Spindler, et al, J. Virol. 49: 132 (1984)) . Expressed, fusion proteins were separated by SDS gel electrophoresis, excised from the gel, eluted and freeze dried. Rabbits were immunized by subcutaneous injection with 100 μg of the lyophilisate dissolved in Freund' s adjuvant. Immunization was repeated three times at two- week intervals using incomplete Freund' s adjuvant. The rabbit was bled and antiserum was obtained. The obtained antiserum was depleted from antibodies reactive with E. coli and phages in the manner described supra and tested for reactivity against the renal carcinoma antigen as described for the human serum. Reactivity was detected at dilutions of 1: > 100,000. Example 7 The protocols set forth in the preceding examples were followed, using biopsied tissue taken from different subjects suffering from (i) malignant melanoma, (ii) astrocytoma, and (iii) Hodgkin's Disease. Table 1, which follows, summarizes the results, including those obtained with the renal cancer study, set out in detail in Examples 1-6, supra. Table 1. Antibody reactivity of autologous sera with recombinant clones derived from human tumor cDNA. cDNA libraries were screened with autologous patient serum. Positive clones were subcloned to monoclonality. Inserts from each clone were amplified with plasmid primers and separated by agarose gel electrophoresis. Southern blots were performed by cross hybridization with the respective inserts. clones positive different tumor tested clones inserts malignant melanoma 1.0 x 10 6 40 10 renal cell carcinoma 1 8 x 10 6 7 5 astrocytoma 1.2 x 10 6 49 5 Hodgkin' s disease 1.0 x 10 6 14 4 Analysis of the different inserts showed that the melanoma cells expressed the known tumor rejection antigen precursor MAGE-1 (see van der Bruggen et al . , Science 254: 1643-7 (1991) , incorporated by reference) , as well as a new antigen. A portion of the cDNA sequence of this antigen is set forth m SEQ ID NO: 2. When the astrocytoma study was completed, the observed insert appeared to correspond to the previously described Tegt gene (Old, Cane. Res. 41: 361-375 (1981) , incorporated by reference) . When the Hodgkm's Disease study was completed, a previously unknown antigen was isolated, and cDNA encoding it was identified in the library, using standard methods. The antigen is a newly observed, lectm-like structure, a portion of the cDNA for which is set forth in SEQ ID NO: 3. Also observed were antibodies against restm, described by Bilbe, et al, EMBO J 11: 2103-13 (1992) . This is an intermediate filament associated protein, expression of which has been shown to be restricted to Hodgkm and Reed- Sternberg cells, as well as cultured monocytes. Example 8 A further study of occurrence of antibodies against the antigens described in Examples 1-7 was carried out. Table 2 summarizes these assays. In these studies, phages from positive clones were mixed with non-reactive phage (ratio: 1 : 10) , and then used to transfect bacteria (e. coli) . Dilutions of patient sera (1:200) , were used, in an enzyme linked immunosorbent assay (ELISA) , as described supra. "HOM-MEL-40" refers to the new melanoma antigen (SEQ ID NO: 2), while "HOM-MEL-55" refers to MAGE-1 (van der Bruggen et al . , supra) . "HOM-RCC 3.1.3" is the renal cancer antigen of SEQ ID NO: 1. "HOM-GLO-30.2.1" refers to the previously identified astrocytoma associated antigen, "HOM-HD-21" refers to the new, lectm-like antigen of SEQ ID NO: 3, and "HOM-HD-397" is the previously identified restm antigen. The fact that antibodies against the tumor antigens, excepting only restin, were detected, albeit at varying rates, only in the sera of patients diseased with the same type of tumor suggests that tumor growth is essential for the development of a humoral response against tumor antigens . The reason for the presence of restin in healthy controls is not clear. One may speculate that tolerance against respective antigens might be circumvented, because the antigen may have similar sequences to another antigen, the donor may have premalignant cells, or the antigen may be activated in normal cells under non-malignant conditions, such as viral infections, or other inflammatory processes. Example 9 In order to determine the expression pattern of the newly identified antigens described herein, Northern blot analysis was carried out, using a variety of human tissues. RNA was extracted from tissue samples (tumor and normal) using the well known guanidium isothiocyanate/phenol/chloroform method of Chomzynski, et al . , supra. The RNA integrity was checked via electrophoresis in formalin/MOPS gels. Then, gels containing 40 ug of RNA per lane were blotted onto nylon membranes. These Northern blots were then probed with the cDNA of SEQ ID NO: 1, 2 or 3. Hybridization was with 32 P labelled probes at 42°C, with formamide. The filters were washed at 65°C, at lxSSC, 0.2% SDS, and exposed for 16 hours. These are "stringent conditions" as defined hereafter. After exposure, filters were stripped and rehybridized with GAPDH. As will be seen, the new melanoma associated antigen is strongly expressed in melanoma, but not other tissues. Carbonic-anhydrase-like antigen was strongly expressed in about 20% of renal cell carcinomas, and only weakly in normal renal tissue. Tegt was overexpressed on 8/12 astrocytoma tissues compared to normal brain tissue. The mRNA for the lectin like molecule associated with Hodgkin's disease was increased about ten fold in diseased tonsils as compared to normal tonsils, suggesting that overexpression may be a frequent characteristic of proteins which elicit autologous B cell responses. Example 10 Further studies were carried out on the HOM-MEL- 40 sequence. Using standard genetic analysis techniques, the 5' region of the mRNA for HOM-MEL 40 was shown to have a tyrosine kinase binding domain. This suggests that HOM- MEL-40 may function as a receptor. The 3' portion of the RNA is identical with an RNA molecule for "SSX, " a molecule known to be involved in the SYT-SSX translocation in synovial tumors. Example 11 Additional experiments were also carried out to study HOM-MEL 40. Standard Northern blotting showed that, with the exception of testis, HOM-MEL 40 was not expressed in normal tissues. In contrast, it was expressed in 50% of melanomas, 20% of prostate cancers, 20% of gastric cancers, 26% of colorectal cancers, 12% of the lung cancers and 20% of breast and hepatacellular cancer. It was also found in 1/10 gastric, and 1/5 thyroid carcinomas. Additional Western blotting work was carried out, showing that antibodies against HOM-MEL 40 were present in 10 of 89 melanoma patients tested, but only 3 out of 49 healthy male subjects. In yet further studies, it was observed that HLA- A2 positive tumor cells presented a nonamer derived from HOM-MEL. This suggests that HOM-MEL 40 specific vaccines, useful m inducing CTLs, are possible. Example 12 The phage assay described m the prior examples is not appropriate for screening large numbers of serum samples . In order to do so , a modif ication of the standard Western Blot was developed . This variation is based upon His - tagged , recombinant HOM-MEL 40 , as is herein described . HOM-MEL-40 was ampl if ied, over 20 cycles , using pfu polymerase , on plasmid cDNA prepared from melanoma tissue . The ol igonucleot ide primers used were : 5 ' -GCCAAATACTTCTCTAAGGAAGAGTGG- 3 ' ( SEQ ID NO : 5 ) , ( sense) 5 ' -TTCACTGTTGTGAACACTTGCTTTCAC- 3 (SEQ ID NO : 6 ) ; ( antisense ) Polymerase chain reaction (PCR) was carried out at 95°C/l minute; 60°C/l minute; and 72°C/l minute, followed by a final extension at 72°C for 10 minutes. The amplification product was gel purified, using art recognized techniques, and then ligated in frame to Smal digested, dephosphory- lated and gel purified pQE32 vector. This results in production of a fusion protein having a "tail" of 6 histidme molecules at the N-terminus. The construct was then transformed into E. coli SG13009 (pREP4) strain, followed by selection on plates containing kanamycm and ampicillin. Individual colonies were picked, and expressed on a small scale by inducing these with 2 mM isopropyl thiogalactoside (IPTG) . This permits checking for protein expression. Small scale purification over Ni-NTA columns was then performed, for each clone. One clone was identified as expressing a protein of expected length. This clone was isolated and sequenced using well known techniques. It was verified as HOM-MEL- 40. Following the identification, large scale induction of recombinant protein was carried out. Specifically, cells were induced with 2 mM IPTG, and harvested five hours later. Cells were lysed, by combining with a buffer of 8 M urea, 100 mM Na 2 P0 4 , 10 mM Tπs-HCl (pH8) , 0.01% Triton X, overnight. Any cellular debris was spun down, and supernatant was loaded onto pre-equilibrated Ni-NTA resin. Washes were performed with two volumes of the afore¬ mentioned buffer, at pH8, and then at least 10 volumes of the buffer, at pH6.3. Protein was then eluted, using the buffer described herein, plus 250 mM lmidazole. Yields ranged from 15 to 40 mg of His-tagged protein per liter of bacterial culture. Western Blotting was then carried out, using the His- labeled protein. In these assays, 5 ug of recombinant His- tagged proteins, which served as internal negative controls, were mixed with 2xSDS sample buffer (0.1 M Tris- HC1, pH 6.8, 0.2M dithiothreitol, 4% SDS, 0.2% bromophenol blue, 20% glycerol) , and were then electrophoresed in 12% SDS-PAGE, followed by blotting to nylon membranes using semi-dry transfer. After blocking of any unspecified binding with 5% low fat milk in PBS (1 hour) , membranes were incubated with 1:100 diluted sera from tumor patients or healthy controls. Blots were then incubated for one hour with alkaline phosphatase conjugated mouse antl-human IgG. The membrane was then incubated, consecutively, with rabbit anti-mouse IgG (30 minutes) , anti-alkalme phosphatase, and then 0.25 mg/ml of alkaline phosphatase. After each incubation step, the membranes were washed extensively with TBS and 0.1% Tween. Visualization was performed by staining with 5- bromo-4-chloro-3-mdolyl-phosphate (BCIP) , and nitroblue tetrazolium. The sera were analyzed in random order (healthy/melanoma positive) , with the observer blind to the status of the sample. All analyses were carried out m duplicate. The blotting showed a product with a molecular weight of about 24 kD by SDS-PAGE, which is consistent with a calculated molecular weight of 21.6 kD, based upon predicted ammo acid sequence. The lmmunoblottmg described supra, was carried out on 89 melanoma samples, six ovarian cancer samples, and ten renal carcinoma samples. Of these, 11 melanoma samples, one ovarian cancer sample, and three renal cell carcinoma samples were positive. Sera from subjects with colorectal , lung, breast, gastric, or pancreatic cancer were negative. A total of 41 healthy controls were also analyzed, of which three were positive. Any sera which were reactive in the Western blot, as well as twenty negative serum samples were then reassessed, using the phage assay, described supra. The reactivity was confirmed for 10 of the 11 melanoma patients and the positive ovarian cancer patient. The renal cell cancer patient and the healthy controls were negative, and were all samples negative in the Western blot. There were 16 melanoma patients who provided both serum and tumor specimens. It was found that HOM-MEL-40 expression by the tumor could be compared with antibody reactivity in the sample. As will be seen in the table which follows, eight of the sixteen patients had HOM-MEL-40 positive tumors, but only three had antibodies against the antigen in their serum. No antibodies were detected in the serum of patients with HOM-MEL-40 negative tumors. Example 13 The result observed in Example 7 were of interest, and additional experiments were then carried out. The serological analysis described supra was carried out on various Hodgkm's Disease cell samples. One cDNA clone, identified using the methods described supra, was compared to the known cDNA sequence for restin, and was found to correspond to a truncated form of the known cDNA. Specifically, the truncated cDNA, presented herein as SEQ ID NO: 7, encodes for a protein truncated at the carboxy terminus, leading to disruption of the α-helical rod domain. This domain is known to be important for the formation of filaments. Northern blot analysis was carried out, using protocols set forth, and this analysis showed that the transcript was specifically expressed in Hodgkin's Disease associated tissues, but not normal tissues. These results were then confirmed, using single cell RT-PCR, using transcript specific oligonucleotides. A final set of confirming experiments were carried out via Western blotting, using polyclonal antibody serum which was produced using recombinantly produced antigen. Example 14 Rammensee, et al . , Immunogenetics 41: 178-228 (1995) , incorporated by reference, disclose many peptides which bind to HLA-A2.1, and some which also provoke CTL proliferation. Some of these are of formula: XaaLeu(Xaa) 6 (lie,Leu,Val) (SEQ ID NO: 8) . The deduced amino acid sequence for HOM- MEL-40 was screened for sequences which might act as HLA- A2.1 binders/CTL stimulators, and the following were found: Arg Leu Gin Gly He Ser Pro Lys He (SEQ ID NO: 9) ; Arg Leu Arg Glu Arg Lys Gin Leu Val (SEQ ID NO: 10) ; Lys He Gin Lys Ala Phe Asp Asp He (SEQ ID NO: 11) These peptides were synthesized, using well known techniques and Fmoc protected amino acids. The peptides were then purified, using Sephadex G25, followed by reverse phase HPLC on a C-18 column. T2 cells, which are deficient in transporters associated with antigen presentation (DeMars, et al . , Proc. Natl. Acad. Sci. USA 82: 8183-8187 (1985) ; Slater, et al . , Immunogenetics 21: 235-241 (1990)) , were used in peptide binding assays, as follows. A sample of 5xl0 5 T2 cells were incubated for 4 hours at 37°C, in the presence or absence of 100 uM of the HOM-MEL- 40 peptides. Positive controls were an EBV LMP2 derived peptide: Cys Leu Gly Gly Leu Leu Thr Met Val (SEQ ID NO: 12) and an HIV reverse transcriptase derived peptide: He Leu Lys Glu Pro Val Gly Val (SEQ ID NO: 13) Upregulation of HLA-A2.1 on T2 cells was measured by labelling with an anti-HLA-A2.1 specific monoclonal antibody (i.e., BB7.2) , followed by incubation with an FITC conjugated goat anti-mouse antibody. The samples were analyzed by flow cytometry, with upregulation of HLA-A2.1 being given by the ratio: mean fluorescence intensity in sample with peptide mean fluorescence intensity in sample without peptide Each of the three peptides were seen to bind to HLA-A2.1, with SEQ ID NO: 8 showing strongest HLA-A2.1 upregulation by far, as determined by FACS analysis. As the foregoing shows, the invention relates to a method for determining or isolating an immunoreactive substance. "Immunoreactive substance" as used herein refers to any material which provokes some form of immune response in the subject which produces it. This response may be based upon either a B cell or a T cell response. Such immunoreactive substances include proteins, peptides, glycoproteins, lipoproteins, peptide containing complexes (e.g., MHC/peptide complexes) , antibodies, and so forth. To determine such substances, a cDNA library is prepared from cells of a subject, using well known, standard methods. The cDNA is then inserted into an appropriate vector, such as a eukaryotic cell specific virus or a phage (i.e., a bacterial virus) , to form a transfecting/trans- forming library, which is then incorporated into a host cell . The host cells are treated so that they express the library component (cloned cDNA) they receive. The host cells are then lysed, so that the expressed material is available for further treatment. The lysed material is then contacted with a "stripped" sample believed to contain an immunogenic binding partner for the immunoreactive substance. "Immunogenic binding partner" as used herein refers to any immune system associated material which binds to the target, i.e., the immunoreactive substance. Such binding partners include, but are not limited to, antibodies, T cells, cytokmes, ligands, receptors, and so forth, as well as truncated portions of these molecules, complementary nucleic acid molecules, and so forth. Note that for some of these components, such as T cells, further steps including those recited herein are required. The stripped sample, as indicated supra, has been treated by contact with both (1) non-transfected or transformed host cells, and (n) host cells transfected or transformed with vectors which do not contain the pertinent cDNA. The stripped sample is useful for identifying binding partners for the expressed material because many of the immune components which would otherwise interfere with the specific immunological reaction desired have been removed via the absorption steps described herein. The identification of the expressed material may be followed by isolation of the cDNA encoding it. One can punch holes through a membrane such as a nitrocellulose membrane, placed on top of Petπ dishes containing colonies of host cells, then use the immune reaction to give position on the solid phase. Each colony is based upon limited cDNA transfection, thereby facilitating isolation and identification of relevant cDNA. The invention also relates to the isolated nucleic acid molecules of SEQ ID NO: 1, 2, 3 or 7 which encode for molecules which are associated with particular conditions. In addition to their role as coding materials, these molecules can also be used as probes to identify cells expressing the relevant antigens, as it has been shown that these cDNA molecules (SEQ ID NO: 1, 2, 3, and 7) are based upon mRNA which translated to the antigen. Also a part of the invention are isolated nucleic acid molecules, the complementary sequences of which hybridize to one of SEQ ID NO: 1, 2, 3 or 7, and which encode a protein equivalent to those encoded by SEQ ID NO: 1, 2, 3 or 7. "Stringent conditions" as used herein, refers to conditions at least as stringent as hybridization at 50 μl/cm 2 of 3.5xSSC, IxDenhardt' s solution, 25 mM sodium phosphate buffer (pH 7.0) , using a 32 P-labelled probe, for 18 hours at 65°C, followed by four washes (one hour, each wash, at 65°C, 2xSSC, 0.1% SDS) , and a final wash for 30 minutes at 1.OxSSC 0.2% SDS. The final wash can be changed to 0.5xSSC to 0.2xSSC, or even O.lxSSC, and SDS can be lowered to 0.1% to increase stringency, if desired. The invention also includes those peptides associated with tumor antigens, such as those of SEQ ID NOS : 9, 10 and 11, which bind to HLA-A2.1 molecules, thereby provoking lysis by cytolytic T cells. Also a part of the invention are peptides of formula Xaa Leu Xaa 7 (SEQ ID NO: 14) wherein the sixth amino acid residue is Ser, Lys or Phe, and the ninth amino acid residue is Val or He. These molecules can also serve, very simply, as markers for HLA- A2.1 cells, as it is well known that peptide/MCH complex formation is quite specific. Other features of the invention will be clear to the skilled artisan and need not be reiterated here. The terms and expressions which have been employed are used as terms of description and not of limitation, and there is no intention in the use of such terms and expressions of excluding any equivalents of the features shown and described or portions thereof, it being recognized that various modifications are possible within the scope of the invention. (1) GENERAL INFORMATION: (i) APPLICANTS: Pfreundschuh, Michael (ii) TITLE OF INVENTION: Hodgkin' s Disease Associated Molecules And Uses Thereof (iii) NUMBER OF SEQUENCES: 14 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: Felfe & Lynch (B) STREET: 805 Third Avenue (C) CITY: New York City (D) STATE: New York (F) ZIP: 10022 (v) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Diskette, 3.5 inch, 360 kb storage (B) COMPUTER: IBM (C) OPERATING SYSTEM: PC-DOS (D) SOFTWARE: Wordperfect (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: (B) FILING DATE: (vii) PRIOR APPLICATION DATA: (A) APPLICATION NUMBER: 08/644,116 (B) FILING DATE: 10-MAY-1996 (C) CLASSIFICATION: 435 (vii) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: 08/668,128 (B) FILING DATE: 21-JUNE-1996 (vii) PRIOR APPLICATION DATA: (A) APPLICATION NUMBER: 08/580,980 (B) FILING DATE: 03-JANUARY-1996 (vii) PRIOR APPLICATION DATA: (A) APPLICATION NUMBER: 08/479,328 (B) FILING DATE: 07-JUNE-1995 (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: Hanson, Norman D. (B) REGISTRATION NUMBER: 30,946 (C) REFERENCE/DOCKET NUMBER: LUD 5441-PCT (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: (212) 688-9200 (B) TELEFAX: (212) 838-3884 (2) INFORMATION FOR SEQUENCE ID NO: 1: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2679 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double-stranded (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 1: CGCGAAGATG CCCCGGCGCA GCCTGCACGC GGCGGCCGTG CTCCTGCTGG 50 TGATCTTAAA GGAACAGCCT TCCAGCCCGG CCCCAGTGAA CGGTTCCAAG 100 TGGACTTATT TTGGTCCTGA TGGGGAGAAT AGCTGGTCCA AGAAGTACCC 150 GTCGTGTGGG GGCCTGCTGC AGTCCCCCAT AGACCTGCAC AGTGACATCC 200 TCCAGTATGA CGCCAGCCTC ACGCCCCTCG AGTTCCAAGG CTACAATCTG 250 TCTGCCAACA AGCAGTTTCT CCTGACCAAC AATGGCCATT CAGTGAAGCT 300 GAACCTGCCC TCGGACATGC ACATCCAGGG CCTCCAGTCT CGCTACAGTG 350 CCACGCAGCT GCACCTGCAC TGGGGGAACC CGAATGACCC GCACGGCTCT 400 GAGCATACCG TCAGCGGACA GCACTTCTCC GCCGAGCTGC ACATTGTCCA 450 TTATAACTCA GACCTTTATC CTGACGACAG NACTGCCAGC AACAAGTCAG 500 AAGACCTCGC TGTCCTGGGT GCTCTCATTG AGATGGGCTC CTTCAATCCG 550 TCCTATGACA AGATCTTCAG TCACCTTCAA CATGTAAAGT ACAAAGGCCA 600 GGAAGCATTC GTCCCGGGAT TCAACATTGA AGAGCTGCTT CCGGAGAGGA 650 CCGCTGAATA TTACCGCTAC CGGGGGTCCC TGATCACACC CCCTTGCAAC 700 CCCACTGTGC TCTGGACAGT TTTCCGAAAC CCCGTGCAAA TTTCCCAGGA 750 GCAGCTGCTG GCTTTGGAGA CAGCCCTGTA CTGCACACAC ATGGACGACC 800 CTTCCCCCAG AGAAATGATC AACAACTTCC GGCAGGTCCA GAAGTTCGAT 850 GAGAGGCTGG TATACACCTC CTTCTCCCAA GTGCAAGTCT GTACTGCGGC 900 AGGACTGAGT CTGGGCATCA TCCTCTCACT GGCCCTGGCT GGCATTCTTG 950 GCATCTGTAT TGTGGTGGTG GTGTCCATTT GGCTTTTCAG AAGGAAGAGT 1000 ATCAAAAAAG GTGATAACAA GGGAGTCATT TACAAGCCAG CCACCAAGAT 1050 GGAGACTGAG GCCCACGCTT GAGGTCCCCG GAGCTCCCGG GCACATCCAG 1100 GAAGGACCTT GCTTTGGACC CTACACACTT CGGCTCTCTG GACACTTGCG 1150 ACACCTCAAG GTGTTCTCTG TAGCTCAATC TGCAAACATG CCAGGCCTCA 1200 GGGATCCTCT GCTGGGTGCC TCCTTGTCTT GGGACCATGG NCACCCCAGA 1250 GCCATCCGAT CGATGGATGG GATGCACTCT CAGACCAAGC AGCAGGAATT 1300 CAAAGCTGCT TGCTGTAATT GTGTGAGATT GTGAAGTGGT CTGAATTCTG 1350 GAATCACAAA CCAACCATGC TGGTGGGCCA TTAATGGTTG GAAAACACTT 1400 CCATCCGGGG CTTTGCCAGA GCGTGCTTTC AAGTGTCCTG GAAATTCTGC 1450 TGCTTCTCCA AGCTTTCAGA CAAGAATGTG CACTCTCTGC TTAGGTTTTG 1500 CTTGGGAAAC TCAACTTCTT TCCTCTGGAG ACGGGACATC TCCCTCTGAT 1550 TTCCTTCTGC TATGCAAAAC CTTTAATCTG CACCTTACAN ACTCGGGGAC 1600 AAATGGGGAC AGGAAGGATC AAGTTGTAGA GNAGAAAAAG AAAACAAGAG 1650 ATATACATTG TGATATATAT TAGGGACACT TTCACAGTCC TGTCCTCTGG 1700 ATCACAGACA CTGCACAGAC CTTAGGGAAA TGGCAGGTTC AAAGTTCCAC 1750 TTCTTGGTGG GGATGAGAAG GGAGAGAGAG CTAGAGGGAC AAAGAGAATG 1800 AGAAGACATG GATGATCTGG GAGAGTCTCA CTTCGGAATC AGAATTGGAA 1850 TCACATTCTG TTTATCAAGC CATAATGTAA GGACAGAATA ATACAATAAT 1900 AAGTCCAAAT CCAACCTCCT GTCAGTGGAA CAGTTATGTT TTATACTCTA 1950 CAGATTTTAC AAATANATGA GGCTNGTTCC TTGAAAANTG TGTTGNNTTG 2000 CTGTNGTCCN NTGGAGGAGA CATGAGTTCC GAGATGACCA ACTCNNGCNT 2050 TGNATNCTNG GAGGNAATAN GGCAGAACCA AAATGACTGT AGAACTTATT 2100 CTCTGTAGGC CAAATTTCAT TTCAGCCACT TCTGCAGGAT CCTACTGCCA 2150 ACCTGGAATG GAGACTTTTA TCTACTTCTC TCTCTCTGAA GATGTCAAAT 2200 CGTGGTTTAG ATCAAATATA TTTCAAGCTA TAAAAGCAGG AGGTTATCTG 2250 TGCAGGGGGC TGGCATCATG TATTTAGGGG CAAGTAATAA TGGAATGCTA 2300 CTAAGATACT CCATATTCTT CCCCGAATCA CACAGACAGT TTCTGACAGG 2350 CGCAACTCCT CCATTTTCCT CCCGCAGGTG AGAACCCTGT GGAGATGAGT 2400 CAGTGCCATG ACTGAGAAGG AACCGACCCC TAGTTGAGAG CACCTTGCAG 2450 TTCCCCGAGA ACTTTCTGAT TGCACAGTCT CATTTTGACA GCATGAAATG 2500 TCCTCTTGAA GCATAGCTTT TTAAATATCT TTTTCCTTCT ACTCCTCCCT 2550 CTGACTCTAG GAATTCTCTC TTCTGGAATC GCTTGAACCC AGGAGGCGGA 2600 GGTTGCAGTA AGCCAAGGTC ATGCCACTGC ACTCTAGCCT GGGTGACAGA 2650 GCGAGACTCC ATCTCAAAAA AAAAAAAAA 2679 (2) INFORMATION FOR SEQUENCE ID NO: 2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 931 base pairs (B) TYPE: nucleic acid (C)STRANDEDNESS: double-stranded (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 2; ACTTTCTCTC TCTTTCGATT CTTCCATACT CAGAGTACGC ACGGTCTGAT 50 TTTCTCTTTG GATTCTTCCA AAATCAGAGT CAGACTGCTC CCGGTGCCAT 100 GAACGGAGAC GACGCCTTTG CAAGGAGACC CACGGTTGGT GCTCAAATAC 150 CAGAGAAGAT CCAAAAGGCC TTCGATGATA TTGCCAAATA CTTCTCTAAG 200 GAAGAGTGGG AAAAGATGAA AGCCTCGGAG AAAATCTTCT ATGTGTATAT 250 GAAGAGAAAG TATGAGGCTA TGACTAAACT AGGTTTCAAG GCCACCCTCC 300 CACCTTTCAT GTGTAATAAA CGGGCCGAAG ACTTCCAGGG GAATGATTTG 350 GATAATGACC CTAACCGTGG GAATCAGGTT GAACGTCCTC AGATGACTTT 400 CGGCAGGCTC CAGGGAATCT CCCCGAAGAT CATGCCCAAG AAGCCAGCAG 450 AGGAAGGAAA TGATTCGGAG GAAGTGCCAG AAGCATCTGG CCCACAAAAT 500 GATGGGAAAG AGCTGTGCCC CCCGGGAAAA CCAACTACCT CTGAGAAGAT 550 TCACGAGAGA TCTGGACCCA AAAGGGGGGA ACATGCCTGG ACCCACAGAC 600 TGCGTGAGAG AAAACAGCTG GTGATTTATG AAGAGATCAG CGACCCTGAG 650 GAAGATGACG AGTAACTCCC CTCAGGGATA CGACACATGC CCATGATGAG 700 AAGCAGAACG TGGTGACCTT TCACGAACAT GGGCATGGCT GCGGACCCCT 750 CGTCATCAGG TGCATAGCAA GTGAAAGCAA GTGTTCACAA CAGTGAAAAG 800 TTGAGCGTCA TTTTTCTTAG TGTGCCAAGA GTTCGATGTT AGCGTTTACG 850 TTGTATTTTC TTACACTGTG TCATTCTGTT AGATACTAAC ATTTCATTGA 900 TGACGAAGAC ATACTTAATC GATATTTGGT T 931 (2) INFORMATION FOR SEQUENCE ID NO: 3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1692 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double-stranded (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 3: GATCCCCCGG GCTGCAGGAA TTCGGCACGA GCAAAGGACT TCCTAGTGGG 50 TGTGAAAGGC AGCGGTGGCC ACAGAGGCGG CGGAGAGATG GCCTTCAGCG 100 GTTCCCAGGC TCCCTACCTG AGTCCAGCTG TCCCCTTTTC TGGGACTATT 150 CAAGGAGGTC TCCAGGACGG ACTTCAGATC ACTGTCAATG GGACCGTTCT 200 CAGCTCCAGT GGAACCAGGT TTGCTGTGAA CTTTCAGACT GGCTTCAGTG 250 GAAATGACAT TGCCTTCCAC TTCAACCCTC GGTTTGAAGA TGGAGGGTAC 300 TTGGTGTCCA ACACGAGGCA GAACGGAAGC TGGGGGCCCG AGGAGAGGAA 350 GACACACATG CCTTNCCAGA AGGGGATGCC CTTTGACCTC TGCTTCCTGG 400 TGCAGAGCTC AGATTTCAAG GTGATGGTGA ACGGGATCCT CTTCGTGCAG 450 TACTTCACAT CTCGTCATGC CCTGTCCACC GTTGTGGACA CCATCTCCGT 500 CAATGGCTCT GTGCAGCTGT CCTACATCAG CTTCCAGCCT CCCGGCGTGT 550 GGCCTGCCAA CCCGGCTCCC ATTACCCAGA CAGNNNTCAT CCACACAGTN 600 GCAGAGCGCC CNCTGGACAG ATGTCTCTAC TCCCGCCATC CCACCTATGA 650 TGTACCCCCA CCCCGCCTAT CCGATGCCTT TCATCACCAC CATTCTGGGA 700 GGGCTGTACC CATCCAAGTC CATCCTCCTG TCAGGCACTG TNCTGCCCAG 750 TGCTCANGAG GTTCCACATC NAACCTGTGC NCTGGGAACC ACATCGCCTT 800 CCACCTGAAC CCCCGTTTTG ATGAGAATGC TGTGGTCCGC AACACCCAGA 850 TCGACAACTC CTGGGGGTCT CAGGAGCGAA GTCTGCCCCG AAAAATGCCC 900 TTCGTCCGTG GCCAGAGCTT CTCAGTGTGG ATCTTGTGTG AAGCTCACTG 950 CCTCAAGGTG GCCGTGGATG GTCAGCACCT GTTTGAATAC AACCATCGCC 1000 TGAGGAACCT GCCCACCATC AACAGACTGG AAGTGGGGGG CGACATCCAG 1050 CTGACCATGT GCAGACATAG GCGGCTTCCT GGCCCTGGGG CCGGGGGCTG 1100 GGGTGTGGGG CAGTCTGGGT CCTCTCATCA TCCCCACTTC CCAGGCCCAG 1150 CCTTTCCAAC CCTGCCTGGG ATCTGGGCTT TAATGCAGAG GCCATGTCCT 1200 TGTCTGGTCC TGCTTCTGGC TACAGCCACC CTGGAACGGA GAAGGCAGCT 1250 GACGGGGATT GCCTCCTCAG CCGCAGCAGC ACCTGGGGCT CCAGCTGCTG 1300 GAATCCTACC ATCCCAGGAY GCAGGCACAG CCAGGGAGAG GGGAGGNGTG 1350 GGCAGTGAAG ATGAAGCCCC ATGCTCAGTC CCCTCCCATC CCCCACGCAG 1400 CTCCACCCCA GTCCCAAGCC ACCAGCTGTC TGCTCCTGGT GGGAGGTGGC 1450 CTCCTCAGCN CCTCCTCTCT GACCTTTAAC CTNACTCTCA CCTTGCACCG 1500 TGCACCAACC CTTCACCCCT CCTGGAAAGC AGGCCTGATG GCTTCCCACT 1550 GGCCTCCACC ACCTGACCAG AGTGTTCTCT TCAGAGGACT GGCTCCTTTC 1600 CCAGTGTCCT TAAAATAAAG AAATGAAAAT NCTTGTTGGC AAAAAAAAAA 1650 AAAAAAAAAC TCGAGGGGCN NCCCNGTACC CAATTCGCCC TA 1692 (2) INFORMATION FOR SEQUENCE ID NO: 4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1190 base pairs (B) TYPE: nucleic acid (C)STRANDEDNESS: double-stranded (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 4: ATCTGCAGAA TTCGGCTTCG ATCTAGAACT AGTGGATCCC CCGGGCTGCA 50 GGAATTCGGC ACGAGCGGTT CCAAGTGGAC TTATTTTGGT CCTGATGGGG 100 AGAATAGCTG GTCCAAGAAG TACCCGTCGT GTGGGGGCCT GCTGCAGTCC 150 CCCATAGACC TGCACAGTGA CATCCTCCAG TATGACGCCA GCCTCACGCC 200 CCTCGAGTTC CAAGGCTACA ATCTGTCTGC CAACAAGCAG TTTCTCCTGA 250 CCAACAATGG CCATTCAGTG AAGCTGAACC TGCCCTCGGA CATGCACATC 300 CAGGGCCTCC AGTCTCGCTA CAGTGCCACG CAGCTGCACC TGCACTGGGG 350 GAACCCGAAT GACCCGCACG GCTCTGAGCA TACCGTCAGC GGACAGCACT 400 TCTCCGCCGA GCTGCACATT GTCCATTATA ACTCAGACCT TTATCCTGAC 450 GACAGNACTG CCAGCAACAA GTCAGAAGAC CTCGCTGTCC TGGGTGCTCT 500 CATTGAGATG GGCTCCTTCA ATCCGTCCTA TGACAAGATC TTCAGTCACC 550 TTCAACATGT AAAGTACAAA GGCCAGGAAG CATTCGTCCC GGGATTCAAC 600 ATTGAAGAGC TGCTTCCGGA GAGGACCGCT GAATATTACC GCTACCGGGG 650 GTCCCTGATC ACACCCCCTT GCAACCCCAC TGTGCTCTGG ACAGTTTTCC 700 GAAACCCCGT GCAAATTTCC CAGGAGCAGC TGCTGGCTTT GGAGACAGCC 750 CTGTACTGCA CACACATGGA CGACCCTTCC CCCAGAGAAA TGATCAACAA 800 CTNCCGGCAG GTCCAGAAGT TCGNTGAGAG GCTGGTATAC ACCTCCTTCT 850 CNCAAGTGCA AGTCTGTACT GCGGCAGGAC TGAGTCTGGG CATCATCCTC 900 TCACTGGCCC TGGCTGGCAT TCTTGGCATC TGTATTGTGG TGGTGGTGTC 950 CATTTGGCTT TTCAGAAGGA AGAGTANCCC CNAAAGGTGA TAACAAGGGA 1000 GTCATTTACA AGCCANCCAC CAAGATGGAG ACTGAGGCCC ACGCTTGAGG 1050 TCCCCGGAGC TCCCGGGCAC ATCCAGGAAG GACCTTGCTT TTGGACCCTA 1100 CACACTTCGG CTCTCTGGAC ACTTGCGACA CCTCAAGGTG TTCTCTGTAG 1150 CTCAATCTGC AAACATGCCA GGCCTCAGGG ATCCTCTGCT 1190 (2) INFORMATION FOR SEQUENCE ID NO: 5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 base pairs (B) TYPE: nucleic acid (C)STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 5: GCCAAATACT TCTCTAAGGA AGAGTGG 27 (2) INFORMATION FOR SEQUENCE ID NO: 6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 base pairs (B) TYPE: nucleic acid (C)STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 6: TTCACTGTTG TGAACACTTG CTTTCAC 27 (2) INFORMATION FOR SEQUENCE ID NO: 7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2085 base pairs (B) TYPE: nucleic acid (C)STRANDEDNESS: single (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 7: G GAG CTC CAC CGC GGT GGC GGC CGC TCT AGA ACT AGT GGA TCC CCC 46 Glu Leu His Arg Gly Gly Gly Arg Ser Arg Thr Ser Gly Ser Pro 5 10 15 GGG CTG CAG GAA TTC GGC ACG AGC TGC TGC TCA CAG AGG AGG CCC AGT 94 Gly Leu Gin Glu Phe Gly Thr Ser Cys Cys Ser Gin Arg Arg Pro Ser 20 25 30 CGG ACA GGA CTA TTG ACT GAA ACC TCC CGT TAC GCC AGG AAG ATC TCC 142 Arg Thr Gly Leu Leu Thr Glu Thr Ser Arg Tyr Ala Arg Lys lie Ser 35 40 45 GGT ACC ACT GCC CTC CAG GAG GCC CTG AAG GAG AAG CAG CAG CAC ATT 190 Gly Thr Thr Ala Leu Gin Glu Ala Leu Lys Glu Lys Gin Gin His lie 50 55 60 GAG CAG CTG CTG GCG GAA CGG GAT CTG GAG AGG GCG GAG GTG GCC AAG 238 Glu Gin Leu Leu Ala Glu Arg Asp Leu Glu Arg Ala Glu Val Ala Lys 65 70 75 GCC ACG AGC CAC GTG GGG GAG ATA GAG CAG GAG CTA GCT CTG GCC CGG 286 Ala Thr Ser His Val Gly Glu lie Glu Gin Glu Leu Ala Leu Ala Arg 80 85 90 95 GAC GGA CAT GAC CAG CAT GTC CTG GAA TTG GAA GCC AAA ATG GAC CAG 334 Asp Gly His Asp Gin His Val Leu Glu Leu Glu Ala Lys Met Asp Gin 100 105 110 CTG CGA ACA ATG GTG GAA GCT GCT GAC AGG GAG AAG GTG GAG CTT CTC 382 Leu Arg Thr Met Val Glu Ala Ala Asp Arg Glu Lys Val Glu Leu Leu 115 120 125 AAC CAG CTT GAA GAG GAG AAA AGG AAG GTT GAG GAC CTT CAG TTC CGG 430 Asn Gin Leu Glu Glu Glu Lys Arg Lys Val Glu Asp Leu Gin Phe Arg 130 135 140 GTT GAA GAA GAA TCA ATT ACC AAA GGT GAT CTT GAG ACG CAG ACC AAA 478 Val Glu Glu Glu Ser lie Thr Lys Gly Asp Leu Glu Thr Gin Thr Lys 145 150 155 CTG GAG CAT GCC CGC ATT AAG GAG CTT GAA CAG AGC CTG CTC TTT GAA 526 Leu Glu His Ala Arg lie Lys Glu Leu Glu Gin Ser Leu Leu Phe Glu 160 165 170 175 AAG ACC AAA GCT GAC AAA CTC CAG AGG GAG TTA GAA GAC ACT AGG GTG 574 Lys Thr Lys Ala Asp Lys Leu Gin Arg Glu Leu Glu Asp Thr Arg Val 180 185 190 GCT ACA GTT TCA GAA AAG TCA CGT ATA ATG GAA CTG GAG AAA GAC CTA 622 Ala Thr Val Ser Glu Lys Ser Arg lie Met Glu Leu Glu Lys Asp Leu 195 200 205 GCA TTG AGA GTA CAG GAA GTA GCT GAG CTC CGA AGA AGG CTA GAG TCC 670 Ala Leu Arg Val Gin Glu Val Ala Glu Leu Arg Arg Arg Leu Glu Ser 210 215 220 AAT AAG CCT GCT GGG GAT GTG GAC ATG TCA CTT TCC CTT TTG CAA GAG 718 Asn Lys Pro Ala Gly Asp Val Asp Met Ser Leu Ser Leu Leu Gin Glu 225 230 235 ATA AGC TCT TTG CAA GAA AAG TTA GAA GTC ACC CGT ACT GAC CAC CAG 766 lie Ser Ser Leu Gin Glu Lys Leu Glu Val Thr Arg Thr Asp His Gin 240 245 250 255 AGA GAA ATA ACT TCT CTG AAG GAG CAT TTT GGA GCC CGG GAA GAA ACT 814 Arg Glu lie Thr Ser Leu Lys Glu His Phe Gly Ala Arg Glu Glu Thr 260 265 270 CAT CAG AAG GAG ATA AAG GCT CTG TAT ACC GCC ACG GAA AAG CTT TCC 862 His Gin Lys Glu lie Lys Ala Leu Tyr Thr Ala Thr Glu Lys Leu Ser 275 280 285 AAA GAG AAC GAG TCA TTG AAA AGC AAG CTG GAG CAT GCC AAC AAA GAG 910 Lys Glu Asn Glu Ser Leu Lys Ser Lys Leu Glu His Ala Asn Lys Glu 290 295 300 AAC TCA GAT GTG ATA GCT CTA TGG AAG TCC AAA CTG GAG ACT GCC ATC 958 Asn Ser Asp Val lie Ala Leu Trp Lys Ser Lys Leu Glu Thr Ala lie 305 310 315 GCA TCC CAC CAG CAG GCG ATG GAA GAA CTG AAG GTA TCT TTC AGC AAA 1006 Ala Ser His Gin Gin Ala Met Glu Glu Leu Lys Val Ser Phe Ser Lys 320 325 330 335 GGG CTT GGA ACA GAG ACG GCA GAA TTT GCT GAA CTA AAA ACA CAA ATA 1054 Gly Leu Gly Thr Glu Thr Ala Glu Phe Ala Glu Leu Lys Thr Gin He 340 345 350 GAG AAA ATG AGA CTA GAT TAC CAA CAC GAA ATA GAA AAT TTG CAG AAT 1102 Glu Lys Met Arg Leu Asp Tyr Gin His Glu He Glu Asn Leu Gin Asn 355 360 365 CAA CAA GAC TCT GAA CGG GCT GCC CAT GCT AAA GAG ATG GAA GCC TTG 1150 Gin Gin Asp Ser Glu Arg Ala Ala His Ala Lys Glu Met Glu Ala Leu 370 375 380 AGG GCT AAA CTG ATG AAA GTT ATT AAA GAA AAG GAA AAC AGT CTG GAA 1198 Arg Ala Lys Leu Met Lys Val He Lys Glu Lys Glu Asn Ser Leu Glu 385 390 395 GCC ATC AGG TCG AAA CTG GAC AAA GCA GAA GAC CAG CAT CTC GTA GAA 1246 Ala He Arg Ser Lys Leu Asp Lys Ala Glu Asp Gin His Leu Val Glu 400 405 410 415 ATG GAA GAC ACG TTA AAC AAA TTA CAG GAA GCT GAA ATA AAG GTA AAG 1294 Met Glu Asp Thr Leu Asn Lys Leu Gin Glu Ala Glu He Lys Val Lys 420 425 430 GAG CTA GAG GTA CTG CAA GCC AAA TGC AAT GAA CAA ACC AAG GTT ATT 1342 Glu Leu Glu Val Leu Gin Ala Lys Cys Asn Glu Gin Thr Lys Val He 435 440 445 GAT AAT TTT ACA TCA CAG CTC AAG GCT ACT GAA GAA AAG CTC TTG GAT 1390 Asp Asn Phe Thr Ser Gin Leu Lys Ala Thr Glu Glu Lys Leu Leu Asp 450 455 460 CTT GAT GCA CTT CGG AAA GCC AGT TCC GAA GGT AAA TCG GAA ATG AAG 1438 Leu Asp Ala Leu Arg Lys Ala Ser Ser Glu Gly Lys Ser Glu Met Lys 465 470 475 AAA CTT AGA CAG CAG CTT GAG GCA GCT GAG AAA CAG ATT AAA CAT TTA 1486 Lys Leu Arg Gin Gin Leu Glu Ala Ala Glu Lys Gin He Lys His Leu 480 485 490 495 GAG ATT GAA AAG AAT GCT GAA AGT AGC AAG GCT AGT AGC ATT ACC AGA 1534 Glu He Glu Lys Asn Ala Glu Ser Ser Lys Ala Ser Ser He Thr Arg 500 505 510 GAG CTC CAG GGG AGA GAG CTA AAG CTT ACT AAC CTT CAG GAA AAT TTG 1582 Glu Leu Gin Gly Arg Glu Leu Lys Leu Thr Asn Leu Gin Glu Asn Leu 515 520 525 AGT GAA GTC AGT CAA GTG AAA GAG ACT TTG GAA AAA GAA CTT CAG ATT 1630 Ser Glu Val Ser Gin Val Lys Glu Thr Leu Glu Lys Glu Leu Gin He 530 535 540 TTG AAA GAA AAG TTT GCT GAA GCT TCA GAG GAG GCA GTC TCT GTT CAG 1678 Leu Lys Glu Lys Phe Ala Glu Ala Ser Glu Glu Ala Val Ser Val Gin 545 550 560 AGA AGT ATG CAA GAA ACT GTA AAT AAG TTA CAC CAA AAG GAG GAA CAG 1726 Arg Ser Met Gin Glu Thr Val Asn Lys Leu His Gin Lys Glu Glu Gin 565 570 575 580 TTT AAC ATG CTG TCT TCT GAC TTG GAG AAG CTG AGA GAA AAC TTA GCA 1774 Phe Asn Met Leu Ser Ser Asp Leu Glu Lys Leu Arg Glu Asn Leu Ala 585 590 595 GAT ATG GAG GCA AAA TTT AGA GAG AAA GAT GAG AGA GAA GAG CAG CTG 1822 Asp Met Glu Ala Lys Phe Arg Glu Lys Asp Glu Arg Glu Glu Gin Leu 600 605 610 ATA AAG GCA AAG GAA AAA CTG GAA AAT GAC ATT GCA GAA ATA ATG AAG 1870 He Lys Ala Lys Glu Lys Leu Glu Asn Asp He Ala Glu He Met Lvs 615 620 625 ATG TCA GGA GAT AAC TCT TCT "CAG CTG ACA AAA ATG AAC GAT GAA TTA 1918 Met Ser Gly Asp Asn Ser Ser Gin Leu Thr Lys Met Asn Asp Glu Leu 630 635 640 CGT CTG AAA GAA AGA GAT GTA GAA GAA TTA CAG CTA AAA CTT ACA AAG 1966 Arg Leu Lys Glu Arg Asp Val Glu Glu Leu Gin Leu Lys Leu Thr Lvs 645 650 655 660 GCT AAT GAA AAT GCA AGT TTT CTG CAA AAA AGT ATT GAG GAC ATG ACT 2014 Ala Asn Glu Asn Ala Ser Phe Leu Gin Lys Ser He Glu Asp Met Thr 665 670 675 GTC AAA GCT GAA CAG AGC CAG CAA GAA GCA GCT AAA AAG CAT GGA AAT 2062 Val Lys Ala Glu Gin Ser Gin Gin Glu Ala Ala Lys Lys His Gly Asn 680 685 690 TAAGCACCCA CCACTGCCCT GGG 2085 (2) INFORMATION FOR SEQUENCE ID NO: 8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 8: Xaa Leu Xaa Xaa Xaa Xaa Xaa Xaa Xaa 5 (2) INFORMATION FOR SEQUENCE ID NO: 9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 9: Arg Leu Gin Gly He Ser Pro Lys He 5 (2) INFORMATION FOR SEQUENCE ID NO: 10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 10: Arg Leu Arg Glu Arg Lys Gin Leu Val 5 (2) INFORMATION FOR SEQUENCE ID NO: 11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 11: Lys He Gin Lys Ala Phe Asp Asp He 5 (2) INFORMATION FOR SEQUENCE ID NO: 12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 12: Cys Leu Gly Gly Leu Leu Thr Met Val 5 (2) INFORMATION FOR SEQUENCE ID NO: 13: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 13: He Leu Lys Glu Pro Val Gly Val 5 (2) INFORMATION FOR SEQUENCE ID NO: 14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ix) FEATURE: The sixth amino acid is Ser, Lys or Phe. The ninth amino acid is Val or He (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 14: Xaa Leu Xaa Xaa Xaa Xaa Xaa Xaa Xaa 5

Claims: Claims : 1. Isolated nucleic acid molecule consisting of the nucleotide sequence of SEQ ID NO: 7. 2. Isolated nucleic acid molecule which encodes a protein encoded by SEQ ID NO: 7, and which hybridizes to the nucleotide sequence of SEQ ID NO: 7, under stringent conditions. 3. Expression vector comprising the isolated nucleic acid molecule of claim 1, operably linked to a promoter. 4. Expression vector comprising the isolated nucleic acid molecule of claim 2, operably linked to a promoter. 5. Transformed or transfected cell which comprises the isolated nucleic acid molecule of claim 1. 6. Transformed or transfected cell which comprises the isolated nucleic acid molecule of claim 2. 7. Transformed or transfected cell which comprises the expression vector of claim 3. 8. Transformed or transfected cell which comprises the expression vector of claim 4. 9. Method for screening for Hodgkin' s Disease, comprising contacting a cell sample with the isolated nucleic acid molecule of claim 2, and determining hybridization of said isolated nucleic acid molecule to a target as an indication of possible Hodgkin' s Disease. 10. The method of claim 9, wherein said isolated nucleic acid molecule consists of SEQ ID NO: 7. 11. Isolated protein encoded by the isolated nucleic acid molecule of claim 2. 12. Antibody which specifically binds to the isolated protein of claim 11. 13. The antibody of claim 12, wherein said antibody is a monoclonal antibody. 14. Method for screening for Hodgkin' s Disease, comprising contacting a cell sample with the antibody of claim 11, and determining binding of said antibody to a target as an indication of possible Hodgkin' s Disease.

Inventors: PFREUNDSCHUH MICHAEL, PFREUNDSCHUH, MICHAEL
Applicants: LUDWIG INST CANCER RES, LUDWIG INSTITUTE FOR CANCER RESEARCH
Application year: 1997
Main classification: C07H21
IPC codes: A61K38, C07H21, C07K14, C07K16, C12N1, C12N5, C12N15, C12P21, C12Q1, G01N33