36P6D5: SECRETED TUMOR ANTIGEN

Abstract: Described is a gene and its encoded secreted tumor antigen, termed 36P6D5, and to diagnostic and therapeutic methods and compositions useful in the management of various cancers which express 36P6D5, particularly including cancers of the bladder, kidney, prostate, breast, colon, ovary and pancreas.

Description: 36P6D5: SECRETED TUMOR ANTIGEN This application claims the benefit of United States provisional patent application number 60/162,417, filed October 28, 1999, the entire contents of which are incorporated herein by reference. FIELD OF THE INVENTION The invention described herein relates to a gene and its encoded tumor antigen, termed 36P6D5, and to diagnostic and therapeutic methods and compositions useful in the management of various cancers that express 36P6D5 gene products. BACKGROUND OF THE INVENTION Cancer is the second leading cause of human death next to coronary disease. Worldwide, millions of people die from cancer every year. In the United States alone, cancer causes the death of well over a half-million people each year, with some 1.4 million new cases diagnosed per year. While deaths from heart disease have been declining significandy, those resulting from cancer generally are on the rise. In the early part of the next century, cancer is predicted to become the leading cause of death. Worldwide, several cancers stand out as the leading killers. In particular, carcinomas of the lung, prostate, breast, colon, pancreas, and ovary represent the primary causes of cancer death. These and virtually all other carcinomas share a common lethal feature. With very few exceptions, metastatic disease from a carcinoma is fatal. Moreover, even for those cancer patients who initially survive their primary cancers, common experience has shown that their lives are dramatically altered. Many cancer patients experience strong anxieties driven by the awareness of the potential for recurrence or treatment failure. Many cancer patients experience physical debilitations following treatment. Many cancer patients experience a recurrence. Generally speaking, the fundamental problem in the management of the deadliest cancers is the lack of effective and non-toxic systemic therapies. Molecular medicine, still very much in its infancy, promises to redefine the ways in which these cancers are managed. Unquestionably, there is an intensive worldwide effort aimed at the development of novel molecular approaches to cancer diagnosis and treatment. For example, there is a great interest in identifying truly tumor-specific genes and proteins that could be used as diagnostic and prognostic markers and/or therapeutic targets or agents. Research efforts in these areas are encouraging, and the increasing availability of useful molecular technologies has accelerated the acquisition of meaningful knowledge about cancer. Nevertheless, progress is slow and generally uneven. As discussed below, the management of prostate cancer serves as a good example of the limited extent to which molecular biology has translated mto real progress m the clinic. With limited exceptions, the situation is more or less the same for the other ma j or carcmomas mentioned above. Worldwide, prostate cancer is the fourth most prevalent cancer m men. In North America and Northern Europe, it is by far the most common male cancer and is the second leading cause of cancer death m men In the United States alone, well over 40,000 men die annually of this disease - second only to lung cancer Despite the magmtude of these figures, there is still no effective treatment for metastatic prostate cancer. Surgical prostatectomy, radiation therapy, hormone ablation therapy, and chemotherapy remam fixed as the mam treatment modahties. Unfortunately, these treatments are ineffective for many and are often associated with significant undesirable consequences. On the diagnostic front, the lack of a prostate tumor marker that can accurately detect early-stage, localized tumors remains a significant limitation in the management of this disease. Although the serum PSA assay has been a very useful tool, its specificity and general utility is widely regarded as lacking m several important respects, as further discussed below. Most prostate cancers initially occur m the peripheral zone of the prostate gland, away from the urethra. Tumors within this zone may not produce any symptoms and, as a result, most men with early-stage prostate cancer will not present clinical symptoms of the disease until significant progression has occurred. Tumor progression into the transition zone of the prostate may lead to urethral obstruction, thus producing the first symptoms of the disease. However, these clinical symptoms are indistinguishable from the common non-mahgnant condition of benign prostatic hyperplasia (BPH). Early detection and diagnosis of prostate cancer currendy relies on digital rectal examinations (DRE), prostate specific antigen (PSA) measurements, transrectal ultrasonography (TRUS), and transrectal needle biopsy (TRNB) At present, serum PSA measurement in combmation with DRE represent the leading tool used to detect and diagnose prostate cancer. Both have major limitations which have fueled intensive research mto finding better diagnostic markers of this disease. Similarly, there is no available marker that can predict the emergence of the typically fatal metastatic stage of prostate cancer. Diagnosis of metastatic stage is presendy achieved by open surgical or laparoscopic pelvic lymphadenectomy, whole body radionuchde scans, skeletal radiography, and/or bone lesion biopsy analysis Clearly, better imaging and other less invasive diagnostic methods offer the promise of easing the difficulty those procedures place on a patient, as well as improving diagnostic accuracy and opening therapeutic options. A similar problem is the lack of an effective prognostic marker for determining which cancers are indolent and which ones are or will be aggressive. PSA, for example, fails to discriminate accurately between mdolent and aggressive cancers. Until there are prostate tumor markers capable of rehably identifymg early-stage disease, predicting susceptibility to metastasis, and precisely imaging tumors, the management of prostate cancer will continue to be extremely difficult PSA is the most widely used tumor marker for screening, diagnosis, and monitoring prostate cancer today. In particular, several l munoassays for the detection of serum PSA are in widespread clinical use. Recendy, a reverse transcnptase-polymerase chain reaction (RT-PCR) assay for PSA mRNA in serum has been developed. However, PSA is not a disease-specific marker, as elevated levels of PSA are detectable in a large percentage of patients with BPH and prostatitis (25-86%) (Gao et al , 1997, Prostate 31: 264-281), as well as m other nonmahgnant disorders and in some normal men, a factor which significandy limits the diagnostic specificity of this marker. For example, elevations in serum PSA of between 4 to 10 ng/ml are observed m BPH, and even higher values are observed in prostatitis, particularly acute prostatitis. BPH is an extremely common condition m men. Further confusing the situation is the fact that serum PSA elevations may be observed without any indication of disease from DRE, and visa-versa. Moreover, it is now recognized that PSA is not prostate-specific (Gao et al., supra, for review). Various methods designed to improve the specificity of PSA-based detection have been described, such as measurmg PSA density and the ratio of free vs. complexed PSA. However, none of these methodologies have been able to reproducibly distinguish benign from malignant prostate disease In addition, PSA diagnostics have sensitivities of between 57-79% (Cupp & Osterling, 1993, Mayo Clin Proc 68:297-306), and thus miss identifying prostate cancer in a significant population of men with the disease. There are some known markers which are expressed predominandy in prostate, such as prostate specific membrane antigen (PSM), a hydrolase with 85% identity to a rat neuropeptidase (Carter et al., 1996, Proc. Natl. Acad. Sci. USA 93: 749; Bzdega et al., 1997, J. Neurochem. 69: 2270). However, the expression of PSM in small intestine and brain (Israeli et al., 1994, Cancer Res. 54: 1807), as well its potential role in neuropeptide catabolism in brain, raises concern of potential neurotoxicity with anti-PSM therapies. Preliminary results using an Indium-I ll labeled, anti-PSM monoclonal antibody to image recurrent prostate cancer show some promise (Sodee et al., 1996, Clin Nuc Med 21: 759- 766). More recendy identified prostate cancer markers include PCTA-1 (Su et al., 1996, Proc. Nad. Acad. Sci. USA 93: 7252) and prostate stem cell antigen (PSCA) (Reiter et al., 1998, Proc. Nad. Acad. Sci. USA 95: 1735). PCTA-1, a novel galectin, is largely secreted into the media of expressing cells and may hold promise as a diagnostic serum marker for prostate cancer (Su et al., 1996). PSCA, a GPI-linked cell surface molecule, was cloned from LAPC-4 cDNA and is unique in that it is expressed primarily in basal cells of normal prostate tissue and in cancer epithelia (Reiter et al., 1998). Vaccines for prostate cancer are also being actively explored with a variety of antigens, including PSM and PSA. While previously identified markers such as PSA, PSM, PCTA and PSCA have facilitated efforts to diagnose and treat prostate cancer, there is need for the identification of additional markers and therapeutic targets for prostate and related cancers in order to further improve diagnosis and therapy. SUMMARY OF THE INVENTION The present invention relates to a gene and protein designated 36P6D5. In normal individuals, 36P6D5 protein appears to be predominandy expressed in pancreas, with lower levels of expression detected in prostate and small intestine. The 36P6D5 gene is also expressed in several human cancer xenografts and cell lines derived from prostate, breast, ovarian and colon cancers, in some cases at high levels. Over-expression of 36P6D5, relative to normal, is observed in prostate cancer xenografts initially derived from a prostate cancer lymph node metastasis and passaged intratibially and subcutaneously in SCID mice. Extremely high level expression of 36P6D5 is detected m the breast cancer cell line DU4475, a cell line that was initially derived from a mammary gland carcinoma (Langlois et al., 1979, Cancer Res. 39: 2604). The 36P6D5 gene is also expressed in tumor patient samples derived from bladder, kidney, colon and lung cancers, m some cases at high levels. A full length 36P6D5 cDNA of 931 bp (SEQ ID NO: 1) provided herein encodes a 235 amino acid open reading frame (SEQ ID NO: 2) with significant homology to the 2-19 protem precursor (Genbank P98173) as well as a gene previously cloned from human osteoblasts (Q92520). The predicted 235 amino acid 36P6D5 protem also contams an N-terminal signal sequence, indicating that the 36P6D5 protem is secreted. The 36P6D5 gene therefore encodes a secreted tumor antigen which may be useful as a diagnostic, staging and/or prognostic marker for, and/or may serve as a target for various approaches to the treatment of, prostate, breast, colon, pancreatic, and ovarian cancers expressmg 36P6D5. The predicted molecular weight of the 36P6D5 protem is approximately 26 kD and its' pi is 8 97. Expression analysis demonstrates high levels of 36P6D5 expression m several prostate and other cancer cell hnes as well as prostate cancer patient samples and tumor xenografts. The expression profile of 36P6D5 in normal adult tissues, combmed with the over-expression observed in cancer cells such as bladder, colon, kidney, breast, lung, ovary and prostate cancer cell lines and/or cancer patient samples, provides evidence that 36P6D5 is aberrandy expressed m at least some cancers, and can serve as a useful diagnostic and/or therapeutic target for such cancers. The mvention provides polynucleotides corresponding or complementary to all or part of the 36P6D5 genes, mRNAs, and/or coding sequences, preferably m isolated form, including polynucleotides encoding 36P6D5 protems and fragments thereof, DNA, RNA, DNA/RNA hybrid, and related molecules, polynucleotides or oligonucleotides complementary to the 36P6D5 genes or mRNA sequences or parts thereof, and polynucleotides or oligonucleotides that hybridize to the 36P6D5 genes, mRNAs, or to 36P6D5-encoding polynucleotides. Also provided are means for isolating cDNAs and the genes encoding 36P6D5. Recombinant DNA molecules containing 36P6D5 polynucleotides, cells transformed or transduced with such molecules, and host-vector systems for the expression of 36P6D5 gene products are also provided. The mvention further provides 36P6D5 protems and polypeptide fragments thereof. The mvention further provides antibodies that bmd to 36P6D5 protems and polypeptide fragments thereof, mcludmg polyclonal and monoclonal antibodies, murine and other mammalian antibodies, chimeric antibodies, humanized and fully human antibodies, and antibodies labeled with a detectable marker. The mvention further provides methods for detecting the presence and status of 36P6D5 polynucleotides and protems m various biological samples, as well as methods for identifying cells that express 36P6D5 A typical embodiment of this mvention provides methods for monitoring 36P6D5 gene products m a tissue sample having or suspected of having some form of growth dysregulation such as cancer. The mvention further provides various therapeutic compositions and strategies for treating cancers that express 36P6D5 such as prostate cancers, mcludmg therapies aimed at inhibiting the transcription, translation, processmg or function of 36P6D5 as well as cancer vaccines BRIEF DESCRIPTION OF THE FIGURES FIGS. 1A-1B. Nucleotide (SEQ ID NO: 1) and deduced ammo acid (SEQ ID NO: 2) sequences of 36P6D5 cDNA. The start methionine and consensus Kozak sequence are indicated m bold and the putative N-terminal signal sequence is underlined. FIGS. 2A-2B. Ammo acid sequence alignment of the 36P6D5 ORF with 2-19 protem precursor (2A) (SEQ ID NO: 15) and GS3786 protem (osteoblast protem) (2B) (SEQ ID NO: 16). Percent sequence identities are indicated on the figure. FIG. 3. Northern blot analysis of human 36P6D5 expression in various normal tissues showing predominant expression in pancreas and low level expression in prostate and small intestine. FIGS. 4A-4B. Northern blot analysis of human 36P6D5 mRNA expression in a panel of prostate cancer xenografts and various other human cancer cell hnes. FIGS. 5A-5B Secretion of 36P6D5 protem from transfected 293T cells and detection with antι-36P6D5 polyclonal antibody. 293T cells were transiendy transfected with either pCDNA 3.1 MYC/HIS 36P6D5, pTag5 36P6D5, m which the natural signal sequence of 36P6D5 is replaced with an immunoglobulin signal sequence, or pAPTag5 36P6D5 which encodes a fusion protem composed of 36P6D5 and alkaline phosphatase (also containing the Ig signal sequence). Conditioned media or whole cell lysates were subjected to Western blotting with either rabbit anti-His pAb (Santa Cruz, Biotechnology, Inc., 1:2,500 dilution, left panel) or with affinity purified rabbit anti- 36P6D5 pAb (1 ug/ml, right panel). Anti-His and anti-36P6D5 pAb reactive bands were visualized by incubation of the blots with anti-rabbit-HRP conjugated secondary antibody followed by enhanced chemilurninescence detection. FIG. 6. Expression of 36P6D5 in cancer patient tumors. RT-PCR analysis of 36P6D5 mRNA expression in bladder cancer, kidney cancer, colon cancer, and lung cancer patient tumors. FIG. 7. 36P6D5 expression in bladder cancer and their matched normal tissues was tested by Northern blot analysis. For this figure, 10μg of total RNA were loaded for each sample. Overexpression of 36P6D5 expression was detected in 3 out of 4 cancers tested (lanes 3,5,7 and 8). No expression was seen in bladder tissue isolated from a normal individual (lane 1). FIG. 8. Binding of 36P6D5 to LAPC9 AD. A single cell suspension of LAPC9 AD xenograft cells were allowed to adhere overnight to a 6 well plate. The cells were incubated in the presence of control or 36P6D5-AP fusion protein. The alkaline phosphate substrate, BM purple, was used for detection. FIGS. 9A-9B. Human cancer cells express and secrete 36P6D5 protein. Conditioned media and/or cell lysates from a variety of cancer cell lines representing cancers derived from prostate (LAPC4 xenograft), colon (Colo 205, CaCo-1), breast (Du4475), and pancreatic (Capan-1) tissues, as well as PC3 prostate cancer cells engineered to overexpress 36P6D5 protein, were subjected to Western analysis using an anti-36P6D5 murine pAb. The specific anti-36P6D5 immunoreactive bands representing endogenous 36P6D5 protein are indicated with arrows and run approximately between 35 and 40 kD. The molecular weight of 36P6D5 calculated from the amino acid sequence is 26 kD suggesting that endogenous 36P6D5 protein is post-translationally modified, possibly by glycosylation. FIG 10. A sensitive and specific capture ELISA detects 36P6D5 protein in supernatants of human cancer cell lines. A capture ELISA was developed using protein G purified murine anti-36P6D5 pAb as capture Ab and a biotinylated form of the same pAb as detection Ab. Shown is the standard curve generated using the Tag5-36P6D5 protein and specific detection and quantitation of 36P6D5 present in supernatants derived from PC-3-Neo transfected cells (O.D. =0.023, 36P6D5 protein concentration in ng/ml=N.D.), PC-3 cells overexpressing 36P6D5 (O.D.=0.186, 36P6D5 protein concentration in ng/ml=1.48) and endogenous 36P6D5 protein secreted by Du4475 breast cancer cells (O.D. =0.085, 36P6D5 protein concentration in ng/ml=0.50). FIGS. 11A-11B. Detection of 36P6D5 expression in human cancers. Cell lysates from Colon, breast and kidney cancer tissues (Ca), as well as their normal matched adjacent tissues (N) were subjected to Western analysis using an anti-36P6D antibody. The specific anti-36P6D5 immunoreactive bands represent a monomeric form of the 36P6D5 protein, which runs approximately between 35 and 40 kD, and multimeric forms of the protein, which run approximately at 90 and 120 kD. DETAILED DESCRIPTION OF THE INVENTION Unless otherwise defined, all terms of art, notations and other scientific terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this invention pertains. In some cases, terms with commonly understood meanings are defined herein for clarity and/or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art. The techniques and procedures described or referenced herein are generally well understood and commonly employed using conventional methodology by those skilled in the art, such as, for example, the widely utilized molecular cloning methodologies described in Sambrook et al., Molecular Cloning: A Laboratory Manual 2nd. edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. As appropriate, procedures involving the use of commercially available kits and reagents are generally carried out in accordance with manufacturer defined protocols and/or parameters unless otherwise noted. As used herein, the terms "advanced prostate cancer", "locally advanced prostate cancer", "advanced disease" and "locally advanced disease" mean prostate cancers which have extended through the prostate capsule, and are meant to include stage C disease under the American Urological Association (AUA) system, stage Cl - C2 disease under the Whitmore-Jewett system, and stage T3 - T4 and N+ disease under the TNM (tumor, node, metastasis) system. In general, surgery is not recommended for patients with locally advanced disease, and these patients have substantially less favorable outcomes compared to patients havmg clinically localized (organ-confined) prostate cancer Locally advanced disease is clinically identified by palpable evidence of induration beyond the lateral border of the prostate, or asymmetry or induration above the prostate base. Locally advanced prostate cancer is presendy diagnosed pathologically following radical prostatectomy if the tumor invades or penetrates the prostatic capsule, extends mto the surgical margm, or mvades the seminal vesicles As used herein, the terms "metastatic prostate cancer" and "metastatic disease" mean prostate cancers which have spread to regional lymph nodes or to distant sites, and are meant to mclude stage D disease under the AUA system and stage TxNxM+ under the TNM system As is the case with locally advanced prostate cancer, surgery is generally not indicated for patients with metastatic disease, and hormonal (androgen ablation) therapy is the preferred treatment modality. Patients with metastatic prostate cancer eventually develop an androgen-refractory state within 12 to 18 months of treatment initiation, and approximately half of these patients die within 6 months thereafter The most common site for prostate cancer metastasis is bone. Prostate cancer bone metastases are, on balance, characteristically osteoblastic rather than osteolytic (ι.e., resulting in net bone formation). Bone metastases are found most frequendy m the sp e, followed by the femur, pelvis, rib cage, skull and humerus Other common sites for metastasis mclude lymph nodes, lung, hver and bram Metastatic prostate cancer is typically diagnosed by open or laparoscopic pelvic lymphadenectomy, whole body radionuchde scans, skeletal radiography, and/or bone lesion biopsy As used herem, the term "polynucleotide" means a polymeric form of nucleotides of at least about 10 bases or base pairs in length, either ribonucleotides or deoxynucleotides or a modified form of either type of nucleotide, and is meant to mclude smgle and double stranded forms of DNA. As used herem, the term "polypeptide" means a polymer of at least about 6 ammo acids Throughout the specification, standard three letter or smgle letter designations for amino acids are used As used herem, the terms "hybridize", "hybridizing", "hybridizes" and the like, used in the context of polynucleotides, are meant to refer to conventional hybridization conditions, preferably such as hybridization in 50% formamide/6XSSC/0.1% SDS/100 μg/ml ssDNA, in which temperatures for hybridization are above 37 degrees C and temperatures for washing in 0.1X SSC/0.1% SDS are above 55 degrees C, and most preferably to stringent hybridization conditions. "Stringency" of hybridization reactions is readily determinable by one of ordinary skill in the art, and generally is an empirical calculation dependent upon probe length, washing temperature, and salt concentration. In general, longer probes require higher temperatures for proper annealing, while shorter probe ' s need lower temperatures. Hybridization generally depends on the ability of denatured DNA to reanneal when complementary strands are present in an environment below their melting temperature. The higher the degree of desired homology between the probe and hybridizable sequence, the higher the relative temperature that can be used. As a result, it follows that higher relative temperatures would tend to make the reaction conditions more stringent, while lower temperatures less so. For additional details and explanation of stringency of hybridization reactions, see Ausubel et al., Current Protocols in Molecular Biology, Wiley Interscience Publishers, (1995). "Stringent conditions" or "high stringency conditions", as defined herein, may be identified by those that: (1) employ low ionic strength and high temperature for washing, for example 0.015 M sodium chloride/0.0015 M sodium citrate/0.1% sodium dodecyl sulfate at 50°C; (2) employ during hybridization a denaturing agent, such as formamide, for example, 50% (v/v) formamide with 0.1% bovine serum albumin/0.1% Ficoll/0.1% polyvinylpyrrohdone/50mM sodium phosphate buffer at pH 6.5 with 750 mM sodium chloride, 75 mM sodium citrate at 42°C; or (3) employ 50% formamide, 5 x SSC (0.75 M NaCl, 0.075 M sodium citrate), 50 mM sodium phosphate (pH 6.8), 0.1% sodium pyrophosphate, 5 x Denhardt's solution, sonicated salmon sperm DNA (50 μg/ml), 0.1% SDS, and 10% dextran sulfate at 42°C, with washes at 42°C in 0.2 x SSC (sodium chloride/sodium, citrate) and 50% formamide at 55°C, followed by a high-stringency wash consisting of 0.1 x SSC containing EDTA at 55°C. "Moderately stringent conditions" may be identified as described by Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, New York: Cold Spring Harbor Press, and include the use of washing solution and hybridization conditions (e.g., temperature, ionic strength and %SDS) less stringent than those described above. An example of moderately stringent conditions is overnight incubation at 37°C in a solution comprising: 20% formamide, 5 x SSC (150 mM NaCl, 15 mM trisodium citrate), 50 mM sodium phosphate (pH 7.6), 5 x Denhardt's solution, 10% dextran sulfate, and 20 mg/mL denatured sheared salmon sperm DNA, followed by washing the filters in 1 x SSC at about 37-50°C. The skilled artisan will recognize how to adjust the temperature, ionic strength, etc. as necessary to accommodate factors such as probe length and the like. In the context of amino acid sequence comparisons, the term "identity" is used to express the percentage of amino acid residues at the same relative positions that are the same. Also in this context, the term "homology" is used to express the percentage of amino acid residues at the same relative positions that are either identical or are similar, using the conserved amino acid criteria of BLAST analysis, as is generally understood in the art. For example, % identity values may be generated by WU-BLAST-2 (Altschul et al., 1996, Methods in Enzymology 266:460-480; http://blast.wusd/edu/blast/README.html). Further details regarding amino acid substitutions, which are considered conservative under such criteria, are provided below. Additional definitions are provided throughout the subsections that follow. MOLECULAR BIOLOGY OF AND USES FOR 36P6D5 As is further described in the Examples below, the 36P6D5 gene and protein have been characterized using a number of analytical approaches. For example, analyses of nucleotide coding and amino acid sequences were conducted in order to identify potentially related molecules, as well as recognizable structural domains, topological features, and other elements within the 36P6D5 mRNA and protein structure. Northern blot analyses of 36P6D5 mRNA expression were conducted in order to estabhsh the range of normal and cancerous tissues expressing 36P6D5 message. The 36P6D5 protein is predicted to be initially translated into a 235 amino acid precursor containing a signal sequence which, during post-translational processing, is cleaved to yield a mature 211 or 212 amino acid secreted protein (FIG. 1). The 36P6D5 protein has a predicted molecular weight=25.9 and pl=8.97. 36P6D5 is predicted to be a membrane associated protein, with the first 28 amino acids being intracellular. Based on the Signal Peptide algorithm, the intracellular portion of the protein seems to be cleaved off between aa 29 and 30, releasing the rest of the molecule as a soluble protein. The 36P6D5 gene is normally expressed predominandy in pancreas (FIG. 3), but is also expressed or over-expressed in several human cancers, including cancers of the prostate, breast, pancreas, colon, lung, bladder, kidney and ovary (FIG. 4, 6 and 7). The 36P6D5 protein structure shows significant homology to two previously described protein sequences, 2-19 protein precursor (Genbank P98173) (SEQ ID NO: 15) and an osteoblast protein designated GS3786 (Q92520) (SEQ ID NO: 16) (FIG. 2). 36P6D5 has similarities to a predicted osteoblast protein, NP-055703.1, with 36% identity over its entire sequence, with most of the 54% homology occurring between aa 74 and aa 235. It is also weakly similar to protein GS3786. The fact that 36P6D5 has similarities to bone derived proteins is not surprising as it was discovered using SSH comparing LAPC4AD(IT) and LAPC4AD(SQ) RNA. Given its homology to the osteoblast protein, it is possible that the 36P6D5 protein may function as a secreted factor that stimulates the proliferation of cancer cells (such as the 36P5D6 cancer cells shown in figures 4, 6 and 7) in bone. As disclosed herein, 36P6D5 exhibits specific properties that are analogous to those found in a family of genes whose polynucleotides, polypeptides and anti- polypeptide antibodies are used in well known diagnostic assays directed to exarnining conditions associated with dysregulated cell growth such as cancer, in particular prostate cancer (see e.g. both its highly specific pattern of tissue expression as well as its overexpression in prostate cancers as described for example in Example 3). The best known member of this class is PSA, the archetypal marker that has been used by medical practitioners for years to identify and monitor the presence of prostate cancer (see e.g. Merrill et al., J. Urol. 163(2): 503-5120 (2000); Polascik et al., J. Urol. Aug;162(2):293-306 (1999) and Fortier et al., J. Nat. Cancer Inst. 91 (19): 1635-1640(1999)). A variety of other diagnostic markers are also used in this context including p53 and K-ras (see e.g. Tulchinsky et al., Int J Mol Med 1999 Jul;4(l):99-102 and Minimoto et al., Cancer Detect Prev 2000;24(1):1-12). Consequendy, this disclosure of the 36P6D5 polynucleotides and polypeptides (as well as the 36P6D5 polynucleotide probes and anti-36P6D5 antibodies used to identify the presence of these molecules) and their properties allows skilled artisans to utilize these molecules in methods that are analogous to those used, for example, in a variety of diagnostic assays directed to examining conditions associated with cancer. Typical embodiments of diagnostic methods which utilize the 36P6D5 polynucleotides, polypeptides and antibodies described herein are analogous to those methods from well estabhshed diagnostic assays which employ PSA polynucleotides, polypeptides and antibodies. For example, just as PSA polynucleotides are used as probes (for example in Northern analysis, see e.g. Sharief et al., Biochem. Mol. Biol. Int. 33(3):567-74(1994)) and primers (for example in PCR analysis, see e.g. Okegawa et al, J. Urol. 163(4): 1189-1190 (2000)) to observe the presence and/or the level of PSA mRNAs in methods of monitoring PSA overexpression or the metastasis of prostate cancers, the 36P6D5 polynucleotides described herein can be utilized in the same way to detect 36P6D5 overexpression or the metastasis of prostate and other cancers expressing this gene. Alternatively, just as PSA polypeptides are used to generate antibodies specific for PSA which can then be used to observe the presence and/or the level of PSA proteins in methods of monitoring PSA protein overexpression (see e.g. Stephan et al, Urology 55(4):560-3 (2000)) or the metastasis of prostate cells (see e.g. Alanen et al., Pathol. Res. Pract. 192(3):233-7 (1996)), the 36P6D5 polypeptides described herein can be utilized to generate antibodies for use in detecting 36P6D5 overexpression or the metastasis of prostate cells and cells of other cancers expressing this gene. Specifically, because metastases involves the movement of cancer cells from an organ of origin (such as the bladder, kidney or prostate gland etc.) to a different area of the body (such as a lymph node), assays which examine a biological sample for the presence of cells expressing 36P6D5 polynucleotides and/or polypeptides can be used to provide evidence of metastasis, for example, when a biological sample from tissue that does not normally contain 36P6D5 expressing cells (lymph node) is found to contain 36P6D5 expressing cells. Alternatively 36P6D5 polynucleotides and/or polypeptides can be used to provide evidence of cancer, for example, when a cells in biological sample that do not normally express 36P6D5 or express 36P6D5 at a different level (such as kidney, bladder, lung and prostate cells etc.) are found to express 36P6D5 or have an increased expression of 36P6D5. In such assays, artisans may further wish to generate supplementary evidence of metastasis by testing the biological sample for the presence of a second tissue restricted marker (in addition to 36P6D5) such as PSA, PSCA etc. (see e.g. Alanen et al , Pathol. Res. Pract 192(3): 233-237 (1996)) Just as PSA polynucleotide fragments and polynucleotide variants are employed by skilled artisans for use in methods of monitoring this molecule, 36P6D5 polynucleotide fragments and polynucleotide variants can also be used m an analogous manner. In particular, typical PSA polynucleotides used in methods of monitoring this molecule are probes or primers which consist of fragments of the PSA cDNA sequence. Illustrating this, primers used to PCR amplify a PSA polynucleotide must mclude less than the whole PSA sequence to function in the polymerase cham reaction. In the context of such PCR reactions, skilled artisans generally create a variety of different polynucleotide fragments that can be used as primers in order to amplify different portions of a polynucleotide of interest or to optimize amplification reactions (see e.g. Caetano-Anolles, G Biotechniques 25(3): 472-476, 478-480 (1998); Robertson et al., Methods Mol. Biol. 98:121-154 (1998)). An additional illustration of the utility of such fragments is provided in Example 3, where a 36P6D5 polynucleotide fragment is used as a probe to show the overexpression of 36P6D5 mRNAs in cancer cells. In addition, in order to facilitate their use by medical practitioners, variant polynucleotide sequences are typically used as primers and probes for the corresponding mRNAs m PCR and Northern analyses (see e.g. Sawai et al., Fetal Diagn. Ther. 1996 Nov-Dec,ll(6):407-13 and Current Protocols In Molecular Biology, Volume 2, Umt 2, Frederick M. Ausubul et al. eds., 1995)). Polynucleotide fragments and variants are typically useful in this context as long as they have the common attribute or characteristic of being capable of bmding to a target polynucleotide sequence (e.g. the 36P6D5 polynucleotide shown m SEQ ID NO: 1) under conditions of relatively high stringency. Just as PSA polypeptide fragments and polypeptide variants are employed by skilled artisans for use m methods of monitoring this molecule, 36P6D5 polypeptide fragments and polypeptide variants can also be used in an analogous manner. In particular, typical PSA polypeptides used m methods of monitoring this molecule are fragments of the PSA protem which contam an epitope that can be recognized by an antibody which will specifically bmd to the PSA protem. This practice of using polypeptide fragments or polypeptide variants used to generate antibodies (such as anti- PSA antibodies) is typical in the art with a wide variety of systems such as fusion protems being used by practitioners (see e.g. Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubul et al. eds., 1995). In this context, each of the variety of epitopes in a protein of interest functions to provide the architecture upon which the antibody is generated. Typically, skilled artisans generally create a variety of different polypeptide fragments that can be used in order to generate antibodies specific for different portions of a polypeptide of interest (see e.g. U.S. Patent No. 5,840,501 and U.S. Patent No. 5,939,533). For example it may be preferable to utilize a polypeptide comprising one of the 36P6D5 biological motifs discussed below. Polypeptide fragments and variants are typically useful in this context as long as they have the common attribute or characteristic of having an epitope capable of generating an antibody specific for a target polypeptide sequence (e.g. the 36P6D5 polypeptide shown in SEQ ID NO: 2). As shown herein, the 36P6D5 polynucleotides and polypeptides (as well as the 36P6D5 polynucleotide probes and anti-36P6D5 antibodies used to identify the presence of these molecules) exhibit specific properties that make them useful in diagnosing cancers of the prostate. The described diagnostic assays that measures the presence of 36P6D5 gene products, in order to evaluate the presence or onset of the particular disease conditions described herein such as prostate cancer are particularly useful in identifying potential candidates for preventive measures or further monitoring, as has been done so successfully with PSA. Moreover, these materials satisfy a need in the art for molecules having similar characteristics to PSA in situations where, for example, a definite diagnosis of metastasis of prostatic origin cannot be made on the basis of a testing for PSA alone (see e.g. Alanen et al., Pathol. Res. Pract. 192(3): 233-237 (1996)), and consequendy, materials such as 36P6D5 polynucleotides and polypeptides (as well as the 36P6D5 polynucleotide probes and anti-36P6D5 antibodies used to identify the presence of these molecules) must be employed to confirm metastases of prostatic origin. Finally, in addition to their use in diagnostic assays, the 36P6D5 polynucleotides disclosed herein have a number of other specific utilities such as their use in the identification of oncogenetic associated chromosomal abnormalities in 21q22.2-22.3. Moreover, in addition to their use in diagnostic assays, the 36P6D5 polypeptides and polynucleotides disclosed herein have other utilities such as their use in the forensic analysis of tissues of unknown origin (see e.g. Takahama K Forensic Sci Int 1996 Jun 28 . 80(1-2). 63-9). As discussed m detail below, 36P6D5 function can be assessed in mammalian cells usmg a variety of techniques that are well known m the art. For mammalian expression, 36P6D5 can be cloned mto several vectors, mcludmg pcDNA 3.1 myc-His- tag (Invitrogen) and the retroviral vector pSRαtkneo (Muller et al., 1991, MCB 11.1785). Using these expression vectors, 36P6D5 can be expressed m several cell hnes, mcludmg PC-3, NIH 3T3, LNCaP and 293T Expression of 36P6D5 can be momtored usmg northern blot analysis. The mammalian cell hnes expressmg 36P6D5 can be tested m several in vitro and in vivo assays, mcludmg cell prohferation m tissue culture, activation of apoptotic signals, tumor formation in SCID mice, and m vitro mvasion usmg a membrane mvasion culture system (MICS) (Welch et al. ,Int. J. Cancer 43- 449-457). The 36P6D5 cell phenotype can be compared to the phenotype of cells that lack expression of 36P6D5. 36P6D5 POLYNUCLEOTIDES One aspect of the mvention provides polynucleotides corresponding or complementary to all or part of a 36P6D5 gene, mRNA, and/or coding sequence, preferably in isolated form, including polynucleotides encoding a 36P6D5 protem and fragments thereof, DNA, RNA, DNA/RNA hybrid, and related molecules, polynucleotides or oligonucleotides complementary to a 36P6D5 gene or mRNA sequence or a part thereof, and polynucleotides or oligonucleotides that hybridize to a 36P6D5 gene, mRNA, or to a 36P6D5 encodmg polynucleotide (collectively, "36P6D5 polynucleotides"). As used herem, the 36P6D5 gene and protein is meant to mclude the 36P6D5 genes and proteins specifically described herein and the genes and protems corresponding to other 36P6D5 protems and structurally similar variants of the foregomg. Such other 36P6D5 protems and variants will generally have coding sequences that are highly homologous to the 36P6D5 coding sequence, and preferably will share at least about 50% amino acid identity and at least about 60% ammo acid homology (usmg BLAST criteria), more preferably sharmg 70% or greater homology (usmg BLAST criteria). A 36P6D5 polynucleotide may comprise a polynucleotide having the nucleotide sequence of human 36P6D5 as shown m FIG. 1 (SEQ ID NO: 1), wherem T can also be U; a polynucleotide which encodes all or part of the 36P6D5 protem; a sequence complementary to the foregomg; or a polynucleotide fragment of any of the foregomg. Another embodiment comprises a polynucleotide having the sequence as shown m FIG. 1 (SEQ ID NO: 1), from nucleotide residue number 59 through nucleotide residue number 763 or 766, wherem T can also be U Another embodiment comprises a polynucleotide havmg the sequence as shown m FIG. 1 (SEQ ID NO: 1), from nucleotide residue number 131 through nucleotide residue number 763 or 766, wherem T can also be U. Another embodiment comprises a polynucleotide encoding a 36P6D5 polypeptide whose sequence is encoded by the cDNA contamed m the plasmid as deposited on April 9, 1999 with American Type Culture Collection, 10801 University Boulevard, Manassas, Virginia 20110-2209, USA (ATCC) as Accession No. 207197. Another embodiment comprises a polynucleotide which is capable of hybridizing under strmgent hybridization conditions to the human 36P6D5 cDNA shown m FIG. 1 (SEQ ID NO: 1). Typical embodiments of the mvention disclosed herem mclude 36P6D5 polynucleotides containing specific portions of the 36P6D5 mRNA sequence (and those which are complementary to such sequences) such as those that encode the protem and fragments thereof. For example, representative embodiments of the mvention disclosed herem mclude: polynucleotides encodmg about ammo acid 1 to about ammo acid 10 of the 36P6D5 protem shown m SEQ ID NO. 2, polynucleotides encodmg about ammo acid 20 to about ammo acid 30 of the 36P6D5 protem shown m SEQ ID NO: 2, polynucleotides encodmg about ammo acid 30 to about ammo acid 40 of the 36P6D5 protem shown m SEQ ID NO: 2, polynucleotides encodmg about amino acid 40 to about ammo acid 50 of the 36P6D5 protem shown in SEQ ID NO: 2, polynucleotides encodmg about ammo acid 50 to about amino acid 60 of the 36P6D5 protem shown in SEQ ID NO: 2, polynucleotides encodmg about ammo acid 60 to about ammo acid 70 of the 36P6D5 protem shown m SEQ ID NO: 2, polynucleotides encoding about ammo acid 70 to about ammo acid 80 of the 36P6D5 protem shown in SEQ ID NO: 2, polynucleotides encodmg about ammo acid 80 to about ammo acid 90 of the 36P6D5 protein shown m SEQ ID NO: 2 and polynucleotides encoding about ammo acid 90 to about amino acid 100 of the 36P6D5 protein shown in SEQ ID NO: 2, etc. Following this scheme, polynucleotides encoding portions of the amino acid sequence of amino acids 100-235 of the 36P6D5 protein are typical embodiments of the invention. Polynucleotides encoding larger portions of the 36P6D5 protein are also contemplated. For example polynucleotides encoding from about amino acid 1 (or 20 or 30 or 40 etc.) to about amino acid 20, (or 30, or 40 or 50 etc.) of the 36P6D5 protein shown in SEQ ID NO: 2 may be generated by a variety of techniques well known in the art. Additional illustrative embodiments of 36P6D5 polynucleotides include embodiments consisting of a polynucleotide having the sequence as shown in FIG. 1 (SEQ ID NO: 1) from about nucleotide residue number 1 through about nucleotide residue number 250, from about nucleotide residue number 250 through about nucleotide residue number 500 and from about nucleotide residue number 500 through about nucleotide residue number 750 and from about nucleotide residue number 750 through about nucleotide residue number 913. These polynucleotide fragments can include any portion of the 36P6D5 sequence as shown in FIG. 1 (SEQ ID NO: 1), for example a polynucleotide having the 235 amino acid ORF within the polynucleotide sequence as shown in FIG. 1 (SEQ ID NO: 1), e.g. from about nucleotide residue number 59 through about nucleotide residue number 763. Additional illustrative embodiments of the invention disclosed herein include 36P6D5 polynucleotide fragments encoding one or more of the biological motifs contained within the 36P6D5 protein sequence. Typical polynucleotide fragments of the invention include those that encode one or more of the 36P6D5 N-glycosylation sites, casein kinase II phosphorylation sites, the protein kinase c phosphorylation sites, the amino acid permeases signature or n-myristoylation sites as disclosed in greater detail in the text discussing the 36P6D5 protein and polypeptides below. The polynucleotides of the preceding paragraphs have a number of different specific uses. For example, because the human 36P6D5 gene maps to chromosome 21q22.2-22.3, polynucleotides encoding different regions of the 36P6D5 protein can be used to characterize cytogenetic abnormalities on chromosome 21, bands q22.2-22.3 that have been identified as being associated with various cancers. In particular, a variety of chromosomal abnormalities in 21q22.2-22.3have been identified as frequent cytogenetic abnormalities in a number of different cancers (see, e.g., Babu et al., Cancer Genet Cytogenet. 1989 Mar;38(l) 127-9 and Ho et al. Blood 1996 Jun 15;87(12):5218-24). Consequendy, polynucleotides encoding specific regions of the 36P6D5 protem provide new tools that can be used to delineate with a greater precision than previously possible, the specific nature of the cytogenetic abnormalities m this region of chromosome 21 that may contribute to the malignant phenotype. In this context, these polynucleotides satisfy a need m the art for expanding the sensitivity of chromosomal screenmg in order to identify more subde and less common chromosomal abnormalities (see, e.g, Evans et al, 1994, Am. J. Obstet. Gynecol. 171 (4):1055-1057). Alternatively, as 36P6D5 is shown to be highly expressed m prostate cancers (see e g. FIG. 4), these polynucleotides may be used m methods assessmg the status of 36P6D5 gene products m normal versus cancerous tissues. Typically, polynucleotides encodmg specific regions of the 36P6D5 protem may be used to assess the presence of perturbations (such as deletions, insertions, pomt mutations etc.) in specific regions (such as regions containing the RNA bmding sequences) of the 36P6D5 gene products. Exemplary assays mclude both RT-PCR assays as well as single-strand conformation polymorphism (SSCP) analysis (see, e.g, Marrogi et al, 1999, J. Cutan. Pathol. 26(8): 369- 378), both of which utilize polynucleotides encodmg specific regions of a protem to examine these regions within the protem. Other specifically contemplated embodiments of the mvention disclosed herem are genomic DNA, cDNAs, πbozymes, and antisense molecules, as well as nucleic acid molecules based on an alternative backbone or mcludmg alternative bases, whether derived from natural sources or synthesized. For example, antisense molecules can be RNAs or other molecules, including peptide nucleic acids (PNAs) or non-nucleic acid molecules such as phosphorothioate derivatives, that specifically bmd DNA or RNA in a base pair- dependent manner. A skilled artisan can readily obtain these classes of nucleic aαd molecules usmg the 36P6D5 polynucleotides and polynucleotide sequences disclosed herem. Antisense technology entails the administration of exogenous oligonucleotides that bmd to a target polynucleotide located within the cells. The term "antisense" refers to the fact that such oligonucleotides are complementary to their intracellular targets, e.g, 36P6D5. See for example, Jack Cohen, 1988, OLIGODEOXYNUCLEOTIDES, Antisense Inhibitors of Gene Expression, CRC Press, and Synthesis 1:1-5 (1988). The 36P6D5 antisense ohgonucleotides of the present mvention mclude derivatives such as S- ohgonucleotides (phosphorothioate derivatives or S-ohgos, see, Jack Cohen, supra), which exhibit enhanced cancer cell growth inhibitory action S-ohgos (nucleoside phosphorothioates) are lsoelectronic analogs of an oligonucleotide (O-ohgo) in which a nonbridging oxygen atom of the phosphate group is replaced by a sulfur atom. The S- ohgos of the present mvention may be prepared by treatment of the corresponding O- ohgos with 3H-l,2-benzodιthιol-3-one-l,l-dιoxide, which is a sulfur transfer reagent. See Iyer, R. P et al, 1990, J Org. Chem. 55:4693-4698; and Iyer, R. P. et al, 1990, J. Am. Chem Soc 112:1253-1254, the disclosures of which are fully incorporated by reference herem. Additional 36P6D5 antisense ohgonucleotides of the present mvention mclude morphohno antisense ohgonucleotides known m the art (see e g. Partridge et al, 1996, Antisense & Nucleic Acid Drug Development 6. 169-175). The 36P6D5 antisense ohgonucleotides of the present mvention typically may be RNA or DNA that is complementary to and stably hybridizes with the first 100 N- terminal codons or last 100 C-terminal codons of the 36P6D5 genomic sequence or the corresponding mRNA. While absolute complementarity is not required, high degrees of complementarity are preferred. Use of an oligonucleotide complementary to this region allows for the selective hybridization to 36P6D5 mRNA and not to mRNA specifying other regulatory subumts of protem kmase. Preferably, the 36P6D5 antisense ohgonucleotides of the present mvention are a 15 to 30-mer fragment of the antisense DNA molecule havmg a sequence that hybridizes to 36P6D5 mRNA. Optionally, 36P6D5 antisense oligonucleotide is a 30-mer oligonucleotide that is complementary to a region in the first 10 N-terminal codons and last 10 C-terminal codons of 36P6D5 Alternatively, the antisense molecules are modified to employ ribozymes in the inhibition of 36P6D5 expression (L A. Couture & D. T. Stmchcomb, 1996, Trends Genet. 12: 510-515). Further specific embodiments of this aspect of the mvention mclude primers and primer pairs, which allow the specific amplification of the polynucleotides of the mvention or of any specific parts thereof, and probes that selectively or specifically hybridize to nucleic acid molecules of the mvention or to any part thereof. Probes may be labeled with a detectable marker, such as, for example, a radioisotope, fluorescent compound, bioluminescent compound, a chemiluminescent compound, metal chelator or enzyme. Such probes and primers can be used to detect the presence of a 36P6D5 polynucleotide in a sample and as a means for detecting a cell expressing a 36P6D5 protein. Examples of such probes include polynucleotides comprising all or part of the human 36P6D5 cDNA sequences shown in SEQ ID NO: 1. Examples of primer pairs capable of specifically amplifying 36P6D5 mRNAs are also described in the Examples that follow. As will be understood by the skilled artisan, a great many different primers and probes may be prepared based on the sequences provided herein and used effectively to amplify and/or detect a 36P6D5 mRNA. As used herein, a polynucleotide is said to be "isolated" when it is substantially separated from contaminant polynucleotides that correspond or are complementary to genes other than the 36P6D5 gene or that encode polypeptides other than 36P6D5 gene product or fragments thereof. A skilled artisan can readily employ nucleic acid isolation procedures to obtain an isolated 36P6D5 polynucleotide. The 36P6D5 polynucleotides of the invention are useful for a variety of purposes, including but not limited to their use as probes and primers for the amplification and/or detection of the 36P6D5 gene(s), mRNA(s), or fragments thereof; as reagents for the diagnosis and/or prognosis of prostate cancer and other cancers; as coding sequences capable of directing the expression of 36P6D5 polypeptides; as tools for modulating or inhibiting the expression of the 36P6D5 gene(s) and/or translation of the 36P6D5 transcript(s); and as therapeutic agents. ISOLATION OF 36P6D5-ENCODING NUCLEIC ACID MOLECULES The 36P6D5 cDNA sequences described herein enable the isolation of other polynucleotides encoding 36P6D5 gene product(s), as well as the isolation of polynucleotides encoding 36P6D5 gene product homologs, alternatively spliced isoforms, allelic variants, and mutant forms of the 36P6D5 gene product. Various molecular cloning methods that can be employed to isolate full length cDNAs encoding a 36P6D5 gene are well known (See, e.g, Sambrook, J. et al, 1989, Molecular Cloning: A Laboratory Manual, 2d ed. Cold Spring Harbor Press, New York; Ausubel et al, eds, 1995, Current Protocols in Molecular Biology, Wiley and Sons). For example, lambda phage cloning methodologies may be conveniendy employed, using commercially available cloning systems (e.g. Lambda ZAP Express, Stratagene). Phage clones containing 36P6D5 gene cDNAs may be identified by probing with a labeled 36P6D5 cDNA or a fragment thereof For example, in one embodiment, the 36P6D5 cDNA (SEQ ID NO 1) or a portion thereof can be synthesized and used as a probe to retrieve overlapping and full length cDNAs corresponding to a 36P6D5 gene. The 36P6D5 gene itself may be isolated by screenmg genomic DNA hbranes, bacterial artificial chromosome hbranes (BACs), yeast artificial chromosome hbranes (YACs), and the like, with 36P6D5 DNA probes or pnmers. RECOMBINANT DNA MOLECULES AND HOST-VECTOR SYSTEMS The mvention also provides recombinant DNA or RNA molecules containing a 36P6D5 polynucleotide, mcludmg but not limited to phages, plasmids, phagemids, cosmids, YACs, BACs, as well as various viral and non-viral vectors well known m the art, and cells transformed or transfected with such recombinant DNA or RNA molecules. As used herem, a recombmant DNA or RNA molecule is a DNA or RNA molecule that has been subjected to molecular manipulation in vitro. Methods for generating such molecules are well known (see, e.g, Sambrook et al, 1989, supra) The mvention further provides a host-vector system compnsmg a recombinant DNA molecule containing a 36P6D5 polynucleotide within a suitable prokaryotic or eukaryotic host cell. Examples of suitable eukaryotic host cells mclude a yeast cell, a plant cell, or an animal cell, such as a mammahan cell or an insect cell (e g , a baculovirus- mfectible cell such as an Sf9 or HighFive cell). Examples of suitable mammahan cells mclude various prostate cancer cell lines such as PrEC, LNCaP and TsuPrl, other transfectable or transducible prostate cancer cell hnes, as well as a number of mammahan cells routinely used for the expression of recombmant protems (e.g, COS, CHO, 293, 293T cells). More particularly, a polynucleotide comprising the coding sequence of 36P6D5 may be used to generate 36P6D5 protems or fragments thereof usmg any number of host-vector systems routinely used and widely known in the art. A wide range of host-vector systems suitable for the expression of 36P6D5 protems or fragments thereof are available (see, e g, Sambrook et al, 1989, supra; Current Protocols m Molecular Biology, 1995, supra). Preferred vectors for mammalian expression mclude but are not limited to pcDNA 3.1 myc-His-tag (Invitrogen) and the retroviral vector pSRαtkneo (Muller et al, 1991, MCB 11:1785). Usmg these expression vectors, 36P6D5 may be preferably expressed m several prostate cancer and non-prostate cell hnes, mcludmg for example 293, 293T, rat-1, NIH 3T3 and TsuPrl. The host-vector systems of the invention are useful for the production of a 36P6D5 protem or fragment thereof. Such host-vector systems may be employed to study the functional properties of 36P6D5 and 36P6D5 mutations. Recombmant human 36P6D5 protem may be produced by mammahan cells transfected with a construct encoding 36P6D5. In an illustrative embodiment described in the Examples, 293T cells can be transfected with an expression plasmid encoding 36P6D5, the 36P6D5 protem is expressed in the 293T cells, and the recombmant 36P6D5 protem can be isolated usmg standard purification methods (e.g., affinity purification usmg anti-36P6D5 antibodies). In another embodiment, also described m the Examples herein, the 36P6D5 coding sequence is subcloned mto the retroviral vector pSRαMSVtkneo and used to infect various mammalian cell hnes, such as NIH 3T3, TsuPrl, 293 and rat-1 m order to estabhsh 36P6D5 expressmg cell hnes. Vanous other expression systems well known in the art may .also be employed. Expression constructs encoding a leader peptide jomed m frame to the 36P6D5 coding sequence may be used for the generation of a secreted form of recombinant 36P6D5 protem. Protems encoded by the 36P6D5 genes, or by fragments thereof, will have a variety of uses, mcludmg but not limited to generating antibodies and in methods for identifymg ligands and other agents and cellular constituents that bmd to a 36P6D5 gene product. Antibodies raised agamst a 36P6D5 protem (like 36P6D5 polynucleotides) or fragment thereof may be useful in diagnostic and prognostic assays, and imaging methodologies m the management of human cancers characterized by expression of 36P6D5 protem, mcludmg but not limited to cancers of the kidney lung, colon, prostate, bram, bladder, pancreas, ovaries, lung, and breast (see e.g. Figs. 4, 6 and 7). Such antibodies may be expressed lntracellularly and used m methods of treating patients with such cancers Vanous immunological assays useful for the detection of 36P6D5 protems are contemplated, mcludmg but not limited to FACS analysis, vanous types of radioirnmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme-linked immunofluorescent assays (ELIFA), lmmunocytochemical methods, and the like. Such antibodies may be labeled and used as immunological imaging reagents capable of detecting 36P6D5 expressmg cells (e g, m radioscintigraphic imaging methods). 36P6D5 protems may also be particularly useful m generating cancer vaccines, as further described below. 36P6D. 1 . POLYPEPTIDES Another aspect of the present mvention provides 36P6D5 protems and polypeptide fragments thereof. The 36P6D5 protems of the mvention mclude those specifically identified herem, as well as allehc vanants, conservative substitution vanants and homologs that can be isolated/generated and charactenzed without undue experimentation following the methods outlined below. Fusion protems that combme parts of different 36P6D5 protems or fragments thereof, as well as fusion protems of a 36P6D5 protem and a heterologous polypeptide are also mcluded. Such 36P6D5 protems will be collectively referred to as the 36P6D5 protems, the protems of the mvention, or 36P6D5. As used herem, the term "36P6D5 polypeptide" refers to a polypeptide fragment or a 36P6D5 protem of at least 6 ammo acids, preferably at least 15 ammo acids. Specific embodiments of 36P6D5 protems comprise a polypeptide having the ammo acid sequence of human 36P6D5 as shown in SEQ ID NO: 2. Alternatively, embodiments of 36P6D5 protems compnse variant polypeptides havmg alterations in the ammo acid sequence of human 36P6D5 as shown m SEQ ID NO: 2. In general, naturally occurring allehc variants of human 36P6D5 will share a high degree of structural identity and homology (e.g, 90% or more identity). Typically, allehc variants of the 36P6D5 protems will contam conservative amino acid substitutions within the 36P6D5 sequences descnbed herem or will contain a substitution of an ammo acid from a corresponding position in a 36P6D5 homologue. One class of 36P6D5 allehc vanants will be protems that share a high degree of homology with at least a small region of a particular 36P6D5 amino acid sequence, but will further contam a radical departure from the sequence, such as a non-conservative substitution, truncation, insertion or frame shift. Conservative amino acid substitutions can frequently be made m a protem without altermg either the conformation or the function of the protein. Such changes include substituting any of isoleucine (I), vahne (V), and leucme (L) for any other of these hydrophobic amino acids; aspartic acid (D) for glutarmc acid (E) and vice versa; glutamine (Q) for asparagme (N) and vice versa; and serme (S) for threonine (T) and vice versa. Other substitutions can also be considered conservative, depending on the environment of the particular ammo acid and its role in the three-dimensional structure of the protem For example, glycme (G) and alanine (A) can frequendy be mterchangeable, as can alanme (A) and valine (V) Methionine (M), which is relatively hydrophobic, can frequendy be mterchanged with leucme and isoleucine, and sometimes with valine. Lysine (EC) and arginine (R) are frequendy mterchangeable m locations m which the significant feature of the ammo acid residue is its charge and the differing pK's of these two amino acid residues are not significant. Still other changes can be considered "conservative" m particular environments. Embodiments of the mvention disclosed herem include a wide variety of art accepted variants of 36P6D5 protems such as polypeptides havmg ammo acid insertions, deletions and substitutions. 36P6D5 variants can be made using methods known in the art such as site-directed mutagenesis, alanme scannmg, and PCR mutagenesis. Site- directed mutagenesis (Carter et al, 1986, Nucl. Acids Res. 13:4331; Zoller et al, 1987, Nucl Acids Res. 10:6487), cassette mutagenesis (Wells et al, 1985, Gene 34:315), restriction selection mutagenesis (Wells et al, 1986, Philos. Trans. R. Soc. London Ser. A, 317-415) or other known techmques can be performed on the cloned DNA to produce the 36P6D5 variant DNA. Scannmg ammo acid analysis can also be employed to identify one or more ammo acids along a contiguous sequence. Among the preferred scanmng amino acids are relatively small, neutral ammo acids. Such ammo acids mclude alanme, glycme, serme, and cysteme. Alanme is typically a preferred scannmg ammo acid among this group because it eliminates the side-cham beyond the beta-carbon and is less likely to alter the main-chain conformation of the variant Alanine is also typically preferred because it is the most common ammo acid Further, it is frequendy found m both buned and exposed positions (Creighton, The Proteins, (W.H. Freeman & Co, N.Y.), Chothia, 1976, J. Mol. Biol, 150.1). If alanme substitution does not yield adequate amounts of variant, an lsosteric ammo acid can be used. As defined herem, 36P6D5 variants have the distinguishing attribute of havmg at least one epitope m common with a 36P6D5 protem havmg the amino acid sequence of SEQ ID NO: 2, such that an antibody that specifically binds to a 36P6D5 variant will also specifically bmd to the 36P6D5 protem havmg the amino acid sequence of SEQ ID NO: 2. A polypeptide ceases to be a variant of the protem shown m SEQ ID NO: 2 when it no longer contams an epitope capable of being recognized by an antibody that specifically binds to a 36P6D5 protem. Those skilled in the art understand that antibodies that recognize protems bmd to epitopes of varying size, and a grouping of the order of about six ammo acids, contiguous or not, is regarded as a typical number of ammo acids m a minimal epitope. See e.g. Hebbes et al, Mol Immunol (1989) 26(9):865-73; Schwartz et al, J Immunol (1985) 135(4):2598-608. As there are approximately 20 ammo acids that can be mcluded at a given position within the minimal 6 ammo acid epitope, an approximation of the odds of such an epitope occurrmg by chance are about 20 6 or about 1 in 64 million Another specific class of 36P6D5 protem variants shares 90% or more identity with the amino acid sequence of SEQ ID NO: 2 Another specific class of 36P6D5 protem variants comprises one or more of the 36P6D5 biological motifs described below. As discussed above, embodiments of the claimed mvention include polypeptides containing less than the 235 ammo acid sequence of the 36P6D5 protem shown in SEQ ID NO: 2 (and the polynucleotides encoding such polypeptides). For example, representative embodiments of the mvention disclosed herem mclude polypeptides consisting of about amino acid 1 to about amino acid 10 of the 36P6D5 protem shown m SEQ ID NO: 2, polypeptides consisting of about ammo acid 20 to about ammo acid 30 of the 36P6D5 protem shown m SEQ ID NO. 2, polypeptides consisting of about amino acid 30 to about ammo acid 40 of the 36P6D5 protem shown m SEQ ID NO. 2, polypeptides consisting of about ammo acid 40 to about ammo acid 50 of the 36P6D5 protem shown in SEQ ID NO: 2, polypeptides consisting of about ammo acid 50 to about ammo acid 60 of the 36P6D5 protem shown m SEQ ID NO: 2, polypeptides consisting of about ammo acid 60 to about ammo acid 70 of the 36P6D5 protem shown m SEQ ID NO- 2, polypeptides consisting of about ammo acid 70 to about ammo acid 80 of the 36P6D5 protein shown in SEQ ID NO- 2, polypeptides consisting of about ammo acid 80 to about ammo acid 90 of the 36P6D5 protem shown m SEQ ID NO: 2 and polypeptides consisting of about amino acid 90 to about amino acid 100 of the 36P6D5 protem shown in SEQ ID NO: 2, etc. Following this scheme, polypeptides consisting of portions of the ammo acid sequence of ammo acids 100-235 of the 36P6D5 protem are typical embodiments of the mvention Polypeptides consisting of larger portions of the 36P6D5 protem are also contemplated. For example polypeptides consisting of about ammo acid 1 (or 20 or 30 or 40 etc.) to about amino acid 20, (or 30, or 40 or 50 etc.) of the 36P6D5 protem shown in SEQ ID NO: 2 may be generated by a variety of techniques well known m the art Additional illustrative embodiments of the mvention disclosed herein mclude 36P6D5 polypeptides containing the ammo acid residues of one or more of the biological motifs contamed withm the 36P6D5 polypeptide sequence as shown in SEQ ID NO: 2. In one embodiment, typical polypeptides of the mvention can contam one or more of the 36P6D5 N-glycosylation sites such as NVTA at residues 120-123 and/or NHSD at residues 208-211 (SEQ ID NO: 2). In another embodiment, typical polypeptides of the mvention can contam one or more of the 36P6D5 protem kinase C phosphorylation sites such as SIR at residues 43-45 and/or STR at residues 160-162 (SEQ ID NO: 2) In another embodiment, typical polypeptides of the invention can contam one or more of the 36P6D5 casern kinase II phosphorylation sites such as SIGE at residues 46-49 and/or TYDD at residues 155-158 (SEQ ID NO: 2). In another embodiment, typical polypeptides of the mvention can contam one or more of the N- mynstoylation sites such as GGGRSK at residues 81-86, GINIAI at residues 108-113 and/or GNVTAT at residues 119-124 (SEQ ID NO: 2). In another embodiment, typical polypeptides of the mvention can contam the amino acid permease signature AGGLLKWFWFASLCAWYSGYLLAELIPDAP at residues 5-36 (SEQ ID NO: 2). In another embodiment, typical polypeptides of the mvention can contam the signal sequence shown m Figure 1. In yet another embodiment, typical polypeptides of the mvention can contam one or more immunogenic epitopes identified by a process described herein such as those shown m Table 1. Related embodiments of these inventions mclude polypeptides containing combinations of the different motifs discussed above with preferable embodiments bemg those which contam no insertions, deletions or substitutions either within the motifs or the mtervenmg sequences of these polypeptides. In addition, embodiments which include a number of either N-terminal and/or C-terminal ammo acid residues on either side of these motifs may be desirable (to, for example, include a greater portion of the polypeptide architecture m which the motif is located) Typically the number of N-terminal and/or C-terminal ammo acid residues on either side of a motif is between about 5 to about 50 ammo acid residues. Illustrative examples of such embodiments includes a polypeptide havmg one or more motifs selected from the group consisting of SIR and/or SIGE and/or NHSD (SEQ ID NO: 2). Alternatively polypeptides having other combinations of the biological motifs disclosed herein are also contemplated such as a polypeptide having SIR and any one of the other biological motifs such as SIGE or a polypeptide having TYDD and any one of the other biological motifs such as GGGRSK etc. (SEQ ID NO: 2). Polypeptides consisting of one or more of the 36P6D5 motifs discussed above are useful in elucidating the specific characteristics of a malignant phenotype in view of the observation that the 36P6D5 motifs discussed above are associated with growth dysregulation and because 36P6D5 is overexpressed in cancers (FIGS. 4, 6 and 7). Casein kinase II and protein kinase C for example are enzymes known to be associated with the development of the malignant phenotype (see e.g. Chen et al, 1998, Lab Invest, 78(2):165-174; Gaiddon et al, 1995, Endocrinology 136(10):4331-4338; Hall et al, 1996, Nucleic Acids Research 24(6):1119-1126; Peterzicl et al, 1999, Oncogene 18(46):6322- 6329; and O'Brian, 1998, Oncol. Rep. 5(2): 305-309). Moreover, both glycosylation and myristoylation are protein modifications also associated with cancer and cancer progression (see e.g. Dennis et al, 1999, Biochim. Biophys. Acta 1473(l):21-34; Raju et al, 1997, Exp. CeU Res. 235(1):145-154). The polypeptides of the preceding paragraphs have a number of different specific uses. As 36P6D5 is shown to be expressed in a variety of cancers including kidney, prostate, bladder, ovarian, breast, pancreas, colon and lung cancer cell lines and/or patient samples (see e.g. FIGS. 4, 6 and 7), these polypeptides may be used in methods assessing the status of 36P6D5 gene products in normal versus cancerous tissues and elucidating the malignant phenotype. Typically, polypeptides encoding specific regions of the 36P6D5 protein may be used to assess the presence of perturbations (such as deletions, insertions, point mutations etc.) in specific regions of the 36P6D5 gene products (such as regions containing the RNA binding motifs). Exemplary assays can utilize antibodies targeting a 36P6D5 polypeptide containing the amino acid residues of one or more of the biological motifs contained within the 36P6D5 polypeptide sequence in order to evaluate the characteristics of this region in normal versus cancerous tissues. Alternatively, 36P6D5 polypeptides containing the amino acid residues of one or more of the biological motifs contained within the 36P6D5 polypeptide sequence can be used to screen for factors that interact with that region of 36P6D5. As discussed above, redundancy in the genetic code permits variation in 36P6D5 gene sequences. In particular, one skilled in the art will recognize specific codon preferences by a specific host species and can adapt the disclosed sequence as preferred for a desired host. For example, preferred codon sequences typically have rare codons (i.e, codons having a usage frequency of less than about 20% in known sequences of the desired host) replaced with higher frequency codons. Codon preferences for a specific organism may be calculated, for example, by utilizing codon usage tables available on the Internet at the following address: http://www.dna.affrc.go.jp/~nakamura/codon.html. Nucleotide sequences that have been optimized for a particular host species by replacing any codons having a usage frequency of less than about 20% are referred to herein as "codon optimized sequences." Additional sequence modifications are known to enhance protein expression in a cellular host. These include elimination of sequences encoding spurious polyadenylation signals, exon/intron sphce site signals, transposon-like repeats, and/or other such well- characterized sequences that may be deleterious to gene expression. The GC content of the sequence may be adjusted to levels average for a given cellular host, as calculated by reference to known genes expressed in the host cell. Where possible, the sequence may also be modified to avoid predicted hairpin secondary mRNA structures. Other useful modifications include the addition of a translational initiation consensus sequence at the start of the open reading frame, as described in Kozak, 1989, Mol. Cell Biol, 9:5073- 5080. Nucleotide sequences that have been optimized for expression in a given host species by elimination of spurious polyadenylation sequences, elimination of exon/intron splicing signals, elimination of transposon-like repeats and/or optimization of GC content in addition to codon optimization are referred to herein as an "expression enhanced sequence." 36P6D5 proteins may be embodied in many forms, preferably in isolated form. As used herein, a protein is said to be "isolated" when physical, mechanical or chemical methods are employed to remove the 36P6D5 protein from cellular constituents that are normally associated with the protein. A skilled artisan can readily employ standard purification methods to obtain an isolated 36P6D5 protein. A purified 36P6D5 protein molecule will be substantially free of other proteins or molecules that impair the binding of 36P6D5 to antibody or other ligand. The nature and degree of isolation and punfication will depend on the mtended use Embodiments of a 36P6D5 protem mclude a purified 36P6D5 protem and a functional, soluble 36P6D5 protem In one form, such functional, soluble 36P6D5 protems or fragments thereof retam the ability to bmd antibody or other ligand The mvention also provides 36P6D5 polypeptides comprising biologically active fragments of the 36P6D5 ammo acid sequence, such as a polypeptide corresponding to part of the ammo acid sequence for 36P6D5 as shown in SEQ ID NO 2 Such polypeptides of the mvention exhibit properties of the 36P6D5 protein, such as the ability to ehcit the generation of antibodies that specifically bmd an epitope associated with the 36P6D5 protem 36P6D5 polypeptides can be generated usmg standard peptide synthesis technology or usmg chemical cleavage methods well known m the art based on the ammo acid sequences of the human 36P6D5 protems disclosed herem Alternatively, recombmant methods can be used to generate nucleic acid molecules that encode a polypeptide fragment of a 36P6D5 protem In this regard, the 36P6D5-encodιng nucleic acid molecules descnbed herem provide means for generating defined fragments of 36P6D5 protems 36P6D5 polypeptides are particularly useful m generating and characterizing domam specific antibodies (e g , antibodies recognizing an extracellular or intracellular epitope of a 36P6D5 protem), m identifymg agents or cellular factors that bmd to 36P6D5 or a particular structural domam thereof, and m various therapeutic contexts, mcludmg but not limited to cancer vaccmes 36P6D5 polypeptides containing particularly interesting structures can be predicted and/or identified usmg vanous analytical techniques well known in the art, mcludmg, for example, the methods of Chou-Fasman, Garnier-Robson, Kyte-Doohtde, Eisenberg, ECarplus-Schultz or Jameson-Wolf analysis, or on the basis of lmmunogenicity Fragments containing such structures are particularly useful in generating subunit specific anti-36P6D5 antibodies or in identifymg cellular factors that bmd to 36P6D5 In an embodiment described in the examples that follow, 36P6D5 can be conveniendy expressed m cells (such as 293T cells) transfected with a commercially available expression vector such as a CMV driven expression vector encodmg 36P6D5 with a C-terminal 6XHιs and MYC tag (ρcDNA3 1/mycHIS, Invitrogen or Tag5, GenHunter Corporation, Nashville TN) The Tag5 vector provides an IgGK secretion signal that can be used to facilitate the production of a secreted 36P6D5 protem m transfected cells The secreted HIS-tagged 36P6D5 m the culture media may be purified usmg a nickel column usmg standard techniques. Modifications of 36P6D5 such as covalent modifications are mcluded within the scope of this invention. One type of covalent modification mcludes reacting targeted ammo acid residues of a 36P6D5 polypeptide with an organic deπvatizmg agent that is capable of reacting with selected side chams or the N- or C- terminal residues of the 36P6D5. Another type of covalent modification of the 36P6D5 polypeptide mcluded within the scope of this mvention comprises altermg the native glycosylation pattern of the polypeptide. "Altermg the native glycosylation pattern" is mtended for purposes herem to mean deleting one or more carbohydrate moieties found m native sequence 36P6D5 (either by removing the underlymg glycosylation site or by deleting the glycosylation by chemical and/or enzymatic means), and/or adding one or more glycosylation sites that are not present m the native sequence 36P6D5. In addition, the phrase mcludes quahtative changes m the glycosylation of the native protems, mvolving a change in the nature and proportions of the various carbohydrate moieties present Another type of covalent modification of 36P6D5 compnses linking the 36P6D5 polypeptide to one of a variety of nonprotemaceous polymers, e g, polyethylene glycol (PEG), polypropylene glycol, or polyoxyalkylenes, m the manner set forth m U.S. Patent Nos. 4,640,835; 4,496,689; 4,301,144; 4,670,417; 4,791,192 or 4,179,337. The 36P6D5 of the present mvention may also be modified in a way to form a chtmenc molecule compnsmg 36P6D5 fused to another, heterologous polypeptide or ammo acid sequence. In one embodiment, such a chimeric molecule comprises a fusion of the 36P6D5 with a polyhistidine epitope tag, which provides an epitope to which immobilized mckel can selectively bind. The epitope tag is generally placed at the amino- or carboxyl- terminus of the 36P6D5. In an alternative embodiment, the chimeric molecule may comprise a fusion of the 36P6D5 with an immunoglobulin or a particular region of an immunoglobulin. For a bivalent form of the chimeric molecule (also referred to as an "lmmunoadhesin"), such a fusion could be to the Fc region of an IgG molecule. The Ig fusions preferably mclude the substitution of a soluble (transmembrane domain deleted or inactivated) form of a 36P6D5 polypeptide m place of at least one variable region within an Ig molecule. In a particularly preferred embodiment, the immunoglobulin fusion includes the hinge, CH2 and CH3, or the hinge, CHI, CH2 and CH3 regions of an IgGl molecule. For the production of immunoglobulin fusions see also US Patent No. 5,428,130 issued June 27, 1995. 36P6D5 ANTIBODIES The term "antibody" is used in the broadest sense and specifically covers single anti- 36P6D5 monoclonal antibodies (including agonist, antagonist and neutralizing antibodies) and anti-36P6D5 antibody compositions with polyepitopic specificity. The term "monoclonal antibody" (mAb) as used herein refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e. the antibodies comprising the individual population are identical except for possible naturally-occurring mutations that may be present in minor amounts. Another aspect of the invention provides antibodies that bind to 36P6D5 proteins and polypeptides. The most preferred antibodies will specifically bind to a 36P6D5 protein and will not bind (or will bind weakly) to non-36P6D5 proteins and polypeptides. Anti- 36P6D5 antibodies that are particularly contemplated include monoclonal and polyclonal antibodies as well as fragments containing the antigen binding domain and/or one or more complementarity deteimining regions of these antibodies. As used herein, an antibody fragment is defined as at least a portion of the variable region of the inirnunoglobulin molecule that binds to its target, i.e, the antigen binding region. 36P6D5 antibodies of the invention may be particularly useful in prostate cancer diagnostic and prognostic assays, and imaging methodologies. Intracellularly expressed antibodies (e.g, single chain antibodies) may be therapeutically useful in treating cancers in which the expression of 36P6D5 is involved, such as for example advanced and metastatic prostate cancers. Such antibodies may be useful in the treatment, diagnosis, and/or prognosis of other cancers, to the extent 36P6D5 is also expressed or overexpressed in other types of cancers such as prostate, kidney, bladder, ovarian, breast, pancreas, colon and lung cancers. 36P6D5 antibodies may also be used therapeutically by, for example, modulating or inhibiting the biological activity of a 36P6D5 protein or targeting and destroying cancer cells expressing a 36P6D5 protein or 36P6D5 binding partoer. Because 36P6D5 is a secreted protein, antibodies may be therapeutically useful for blocking 36P6D5's ability to bind to its receptor or interact with other proteins through which it exerts its biological activity. The invention also provides various immunological assays useful for the binding to, detection and quantification of 36P6D5 and mutant 36P6D5 proteins and polypeptides. Such methods and assays generally comprise one or more 36P6D5 antibodies capable of recognizing and binding a 36P6D5 or mutant 36P6D5 protein, as appropriate, and may be performed within various immunological assay formats well known in the art, including but not limited to various types of radioimmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme-linked immunofluorescent assays (ELIFA), and the like. In addition, " immunological imaging methods capable of detecting prostate cancer and other cancers expressing 36P6D5 are also provided by the invention, including but limited to radioscintigraphic imaging methods using labeled 36P6D5 antibodies. Such assays may be clinically useful in the detection, monitoring, and prognosis of 36P6D5 expressing cancers such as prostate, breast, pancreas, colon and ovarian cancer cell lines. 36P6D5 antibodies may also be used in methods for purifying 36P6D5 and mutant 36P6D5 proteins and polypeptides and for isolating 36P6D5 homologues and related molecules. For example, in one embodiment, the method of purifying a 36P6D5 protein comprises incubating a 36P6D5 antibody, which has been coupled to a solid matrix, with a lysate or other solution containing 36P6D5 under conditions that permit the 36P6D5 antibody to bind to 36P6D5; washing the solid matrix to eliminate impurities; and eluting the 36P6D5 from the coupled antibody. Other uses of the 36P6D5 antibodies of the invention include generating anti-idiotypic antibodies that mimic the 36P6D5 protein. Various methods for the preparation of antibodies are well known in the art. For example, antibodies may be prepared by immunizing a suitable mammahan host using a 36P6D5 protein, peptide, or fragment, in isolated or immunoconjugated form (Harlow, and Lane, eds, 1988, Antibodies: A Laboratory Manual, CSH Press; Harlow, 1989, Antibodies, Cold Spring Harbor Press, NY). In addition, fusion proteins of 36P6D5 may also be used, such as a 36P6D5 GST-fusion protein. In a particular embodiment, a GST fusion protein comprising all or most of the open reading frame amino acid sequence of SEQ ID NO: 2 may be produced and used as an immunogen to generate appropriate antibodies. In another embodiment, a 36P6D5 peptide may be synthesized and used as an immunogen. In addition, naked DNA immunization techniques known in the art may be used (with or without purified 36P6D5 protein or 36P6D5 expressing cells) to generate an immune response to the encoded immunogen (for review, see Donnelly et al, 1997, Ann. Rev. Immunol. 15:617-648). The amino acid sequence of the 36P6D5 as shown in SEQ ID NO: 2 may be used to select specific regions of the 36P6D5 protein for generating antibodies. For example, hydrophobicity and hydrophihcity analyses of the 36P6D5 amino acid sequence may be used to identify hydrophilic regions in the 36P6D5 structure. Regions of the 36P6D5 protein that show immunogenic structure, as well as other regions and domains, can readily be identified using various other methods known in the art, such as Chou-Fasman, Garnier- Robson, Kyte-Doolittle, Eisenberg, Karplus-Schultz or Jameson- Wolf analysis. Illustrating this, the binding of peptides from 36P6D5 proteins to the human MHC class I molecule HLA-A2 are predicted and shown in Table 1 below. Specifically, the complete amino acid sequences of 36P6D5 proteins was entered into the HLA Peptide Motif Search algorithm found in the Bioinformatics and Molecular Analysis Section (BIMAS) Web site (http://bimas.dcrt.nih.gov/). The HLA Peptide Motif Search algorithm was developed by Dr. Ken Parker based on binding of specific peptide sequences in the groove of HLA Class I molecules and specifically HLA-A2 (see e.g. Falk et al. Nature 351: 290-6 (1991); Hunt et al. Science 255:1261-3 (1992); Parker et al, J. Immunol. 149:3580-7 (1992); Parker et al, J. Immunol. 152:163-75 (1994)). This algorithm allows location and ranking of 8-mer, 9-mer, and 10-mer peptides from a complete protein sequence for predicted binding to HLA-A2 as well as other HLA Class I molecules. Most HLA-A2 binding peptides are 9-mers favorably containing a leucine (L) at position 2 and a vahne (V) or leucine (L) at position 9 (Parker et al, J. Immunol. 149:3580-7 (1992)). The results of 36P6D5 predicted binding peptides are shown in Table 1 below. In Table 1, the top 10 ranking candidates for each family member are shown along with their location, the amino acid sequence of each specific peptide, and an estimated binding score. The binding score corresponds to the estimated half-time of dissociation of complexes containing the peptide at 37°C at pH 6.5. Peptides with the highest binding score are predicted to be the most tighdy bound to HLA Class I on the cell surface and thus represent the best immunogenic targets for T-cell recognition. Actual binding of peptides to HLA-A2 can be evaluated by stabilization of HLA-A2 expression on the antigen-processing defective cell line T2 (see e.g. Xue et al. Prostate 30:73-8 (1997) and Peshwa et al. Prostate 36:129-38 (1998)). Immunogenicity of specific peptides can be evaluated in vitro by stimulation of CD8+ cytotoxic T lymphocytes (CTL) in the presence of dendritic cells. Methods for preparing a protein or polypeptide for use as an immunogen and for preparing immunogenic conjugates of a protein with a carrier such as BSA, KLH, or other carrier proteins are well known in the art. In some circumstances, direct conjugation using, for example, carbodiimide reagents may be used; in other instances linking reagents such as those supphed by Pierce Chemical Co, Rockford, IL, may be effective. Administration of a 36P6D5 immunogen is conducted generally by injection over a suitable time period and with use of a suitable adjuvant, as is generally understood in the art. During the immunization schedule, titers of antibodies can be taken to determine adequacy of antibody formation. 36P6D5 monoclonal antibodies are preferred and may be produced by various means well known in the art. For example, immortalized cell lines that secrete a desired monoclonal antibody may be prepared using the standard hybridoma technology of Kohler and Milstein or modifications that immortalize producing B cells, as is generally known. The immortalized cell lines secreting the desired antibodies are screened by immunoassay in which the antigen is the 36P6D5 protein or a 36P6D5 fragment. When the appropriate immortalized cell culture secreting the desired antibody is identified, the cells may be expanded and antibodies produced either from in vitro cultures or from ascites fluid. The antibodies or fragments may also be produced, using current technology, by recombinant means. Regions that bind specifically to the desired regions of the 36P6D5 protein can also be produced in the context of chimeric or CDR grafted antibodies of multiple species origin. Humanized or human 36P6D5 antibodies may also be produced and are preferred for use in therapeutic contexts. Methods for humanizing murine and other non-human antibodies by substituting one or more of the non-human antibody CDRs for corresponding human antibody sequences are well known (see for example, Jones et al, 1986, Nature 321:522-525; Riechmann et al, 1988, Nature 332:323-327; Verhoeyen et al, 1988, Science 239:1534-1536). See also, Carter et al, 1993, Proc. Nad. Acad. Sci. USA 89:4285 and Sims et al, 1993, J. Immunol. 151:2296. Methods for producing fully human monoclonal antibodies mclude phage display and transgenic methods (for review, see Vaughan et al, 1998, Nature Biotechnology 16:535-539). Fully human 36P6D5 monoclonal antibodies may be generated usmg clonmg technologies employmg large human Ig gene combmatonal hbranes (ι.e, phage display) (Gnffiths and Hoogenboom, Buildmg an m vitro immune system: human antibodies from phage display hbranes. In: Clark, M, ed, 1993, Protem Engineering of Antibody Molecules for Prophylactic and Therapeutic Applications in Man, Nottingham Academic, pp 45-64; Burton and Barbas, Human Antibodies from combinational hbranes. Id, pp 65-82). Fully human 36P6D5 monoclonal antibodies may also be produced usmg transgenic mice engineered to contam human lrnmunoglobu n gene loci as descnbed m PCT Patent Application W098/24893, Kucherlapati and Jakobovits et al, pubhshed December 3, 1997 (see also, Jakobovits, 1998, Exp. Opm. Invest. Drugs 7 (4): 607-614). This method avoids the m vitro manipulation required with phage display technology and efficiendy produces high affinity authentic human antibodies. Reactivity of 36P6D5 antibodies with a 36P6D5 protem may be estabhshed by a number of well known means, mcludmg western blot, lmmunoprecipitation, ELISA, and FACS analyses usmg, as appropriate, 36P6D5 protems, peptides, 36P6D5-expressιng cells or extracts thereof. A 36P6D5 antibody or fragment thereof of the mvention may be labeled with a detectable marker or conjugated to a second molecule. Suitable detectable markers mclude, but are not limited to, a radioisotope, a fluorescent compound, a bioluminescent compound, chemiluminescent compound, a metal chelator or an enzyme. A second molecule for con j ugation to the 36P6D5 antibody can be selected m accordance with the mtended use. For example, for therapeutic use, the second molecule can be a toxin or therapeutic agent. Further, bi-specific antibodies specific for two or more 36P6D5 epitopes may be generated usmg methods generally known in the art. Homodtmenc antibodies may also be generated by cross-linking techniques known in the art (e g, Wolff et al, 1993, Cancer Res. 53: 2560-2565). 36P6D5 TRANSGENIC ANIMALS Nucleic acids that encode 36P6D5 or its modified forms can also be used to generate either transgenic animals or "knock out" animals which, in turn, are useful m the development and screening of therapeutically useful reagents. A transgenic animal (e.g., a mouse or rat) is an animal having cells that contain a transgene, which transgene was introduced into the animal or an ancestor of the animal at a prenatal, e.g, an embryonic stage. A transgene is a DNA that is integrated into the genome of a cell from which a transgenic animal develops. In one embodiment, cDNA encoding 36P6D5 can be used to clone genomic DNA encoding 36P6D5 in accordance with estabhshed techniques and the genomic sequences used to generate transgenic animals that contain cells that express DNA encoding 36P6D5. Methods for generating transgenic animals, particularly animals such as mice or rats, have become conventional in the art and are described, for example, in U.S. Patent Nos. 4,736,866 and 4,870,009. Typically, particular cells would be targeted for 36P6D5 transgene incorporation with tissue-specific enhancers. Transgenic animals that include a copy of a transgene encoding 36P6D5 introduced into the germ line of the animal at an embryonic stage can be used to examine the effect of increased expression of DNA encoding 36P6D5. Such animals can be used as tester animals for reagents thought to confer protection from, for example, pathological conditions associated with its overexpression. In accordance with this facet of the invention, an animal is treated with the reagent and a reduced incidence of the pathological condition, compared to untreated animals bearing the transgene, would indicate a potential therapeutic intervention for the pathological condition. Alternatively, non-human homologues of 36P6D5 can be used to construct a 36P6D5 "knock out" animal that has a defective or altered gene encoding 36P6D5 as a result of homologous recombination between the endogenous gene encoding 36P6D5 and altered genomic DNA encoding 36P6D5 introduced into an embryonic cell of the animal. For example, cDNA encoding 36P6D5 can be used to clone genomic DNA encoding 36P6D5 in accordance with estabhshed techniques. A portion of the genomic DNA encoding 36P6D5 can be deleted or replaced with another gene, such as a gene encoding a selectable marker that can be used to monitor integration. Typically, several kilobases of unaltered flanking DNA (both at the 5' and 3' ends) are included in the vector (see e.g, Thomas and Capecchi, 1987, Cell 51:503) for a description of homologous recombination vectors]. The vector is introduced into an embryonic stem cell line (e.g, by electroporation) and cells in which the introduced DNA has homologously recombined with the endogenous DNA are selected (see e.g, Li et al, 1992, CeU 69:915). The selected ceUs are then injected into a blastocyst of an animal (e.g, a mouse or rat) to form aggregation chimeras (see e.g, Bradley, in Robertson, ed, 1987, Teratocarcinomas and Embryonic Stem CeUs: A Practical Approach, (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 to create a "knock out" animal. Progeny harboring the homologously recombined DNA in their germ ceUs can be identified by standard techniques and used to breed animals in which aU ceUs of the animal contain the homologously recombined DNA. Knockout animals can be characterized for instance, for their ability to defend against certain pathological conditions and for their development of pathological conditions due to absence of the 36P6D5 polypeptide. METHODS FOR THE DETECTION OF 36P6D5 Another aspect of the present invention relates to methods for detecting 36P6D5 polynucleotides and 36P6D5 proteins and variants thereof, as weU as methods for identifying a ceU that expresses 36P6D5. The expression profile of 36P6D5 makes it a potential diagnostic marker for local and/or metastasized disease. Northern blot analysis suggests that different tissues express different isoforms of 36P6D5. The 36P6D5 isoforms in prostate cancer appear to be different from the isoform expressed in normal prostate. In this context, the status of 36P6D5 gene products may provide information useful for predicting a variety of factors including susceptibility to advanced stage disease, rate of progression, and/ or tumor aggressiveness. As discussed in detail below, the status of 36P6D5 gene products in patient samples may be analyzed by a variety protocols that are weU known in the art including irnmunohistochemical analysis, the variety of Northern blotting techniques including in situ hybridization, RT-PCR analysis (for example on laser capture micro-dissected samples), western blot analysis and tissue array analysis. More particularly, the invention provides assays for the detection of 36P6D5 polynucleotides in a biological sample, such as serum, bone, prostate, and other tissues, urine, semen, ceU preparations, and the like. Detectable 36P6D5 polynucleotides include, for example, a 36P6D5 gene or fragments thereof, 36P6D5 mRNA, alternative sphce variant 36P6D5 mRNAs, and recombinant DNA or RNA molecules containing a 36P6D5 polynucleotide. A number of methods for amplifying and/or detecting the presence of 36P6D5 polynucleotides are weU known in the art and may be employed in the practice of this aspect of the invention. In one embodiment, a method for detecting a 36P6D5 mRNA in a biological sample comprises producing cDNA from the sample by reverse transcription using at least one primer; amphfying the cDNA so produced using a 36P6D5 polynucleotides as sense and antisense primers to amplify 36P6D5 cDNAs therein; and detecting the presence of the amplified 36P6D5 cDNA. OptionaUy, the sequence of the amplified 36P6D5 cDNA can be determined. In another embodiment, a method of detecting a 36P6D5 gene in a biological sample comprises first isolating genomic DNA from the sample; amphfying the isolated genomic DNA using 36P6D5 polynucleotides as sense and antisense primers to amplify the 36P6D5 gene therein; and detecting the presence of the amplified 36P6D5 gene. Any number of appropriate sense and antisense probe combinations may be designed from the nucleotide sequences provided for the 36P6D5 (SEQ ID NO: 1) and used for this purpose. The invention also provides assays for detecting the presence of a 36P6D5 protein in a tissue of other biological sample such as serum, bone, prostate, and other tissues, urine, ceU preparations, and the like. Methods for detecting a 36P6D5 protein are also weU known and include, for example, irnrnunoprecipitation, immunohistochemical analysis, Western Blot analysis, molecular binding assays, ELISA, ELIFA and the like. For example, in one embodiment, a method of detecting the presence of a 36P6D5 protein in a biological sample comprises first contacting the sample with a 36P6D5 antibody, a 36P6D5- reactive fragment thereof, or a recombinant protein containing an antigen binding region of a 36P6D5 antibody; and then detecting the binding of 36P6D5 protein in the sample thereto. Methods for identifying a ceU that expresses 36P6D5 are also provided. In one embodiment, an assay for identifying a ceU that expresses a 36P6D5 gene comprises detecting the presence of 36P6D5 mRNA in the ceU. Methods for the detection of particular mRNAs in ceUs are well known and include, for example, hybridization assays using complementary DNA probes (such as in situ hybridization using labeled 36P6D5 riboprobes, Northern blot and related techniques) and various nucleic acid amphfication assays (such as RT-PCR using complementary primers specific for 36P6D5, and other amphfication type detection methods, such as, for example, branched DNA, SISBA, TMA and the like). Alternatively, an assay for identifymg a ceU that expresses a 36P6D5 gene compnses detecting the presence of 36P6D5 protem m the ceU or secreted by the cell. Vanous methods for the detection of protems are weU known m the art and may be employed for the detection of 36P6D5 protems and 36P6D5 expressmg ceUs. 36P6D5 expression analysis may also be useful as a tool for identifymg and evaluating agents that modulate 36P6D5 gene expression. For example, 36P6D5 expression is significandy upregulated in prostate cancer, and may also be expressed m other cancers. Identification of a molecule or biological agent that could inhibit 36P6D5 expression or over-expression in cancer ceUs may be of therapeutic value. Such an agent may be identified by usmg a screen that quantifies 36P6D5 expression by RT-PCR, nucleic acid hybridization or antibody bmding. ASSAYS FOR CIRCULATING AND EXCRETED 36P6D5 Mature 36P6D5 protem has an N-terminal signal sequence m the cDNA encoded ORF. Because 36P6D5 is a secreted protem expressed m cancers of the prostate, kidney, bladder, breast, colon, ovary, pancreas, and possibly other cancers, tumors expressmg 36P6D5 would be expected to secrete 36P6D5 mto the vasculature, and/or excreted mto urme or semen, where the protem may be detected and quantified usmg assays and techmques weU known m the molecular diagnostic field. Detecting and quantifying the levels of circulating or excreted 36P6D5 is expected to have a number of uses m the diagnosis, staging, and prognosis of cancers expressmg 36P6D5, including but not limited to cancers of the prostate, kidney, bladder, breast, colon, ovary and pancreas. A number of different technical approaches for the detection and quantification of protems in serum, urme or semen are weU known in the art. Because 36P6D5 is a secreted protem expressed m cancers of the prostate, kidney, bladder, breast, colon, ovary, pancreas, and possibly other cancers, assays for detecting and quantifying 36P6D5 in blood or serum are expected to be useful for the detection, diagnosis, prognosis, and/ or staging of a 36P6D5 expressmg tumor m an individual. For example, 36P6D5 expression in normal tissues is found predominandy m pancreas (FIG. 3), with lower levels of expression detected m prostate and smaU mtestme. However, high level expression is detected m xenografts denved from prostate cancer as weU as ceU hnes denved from cancers of the breast, colon, pancreas and ovary (FIG. 4). Accordingly, detection of serum 36P6D5 may provide an indication of the presence of a prostate, breast, colon, ovarian or pancreatic tumor. Diagnosis of cancer may be made on the basis of this information and/or other information. In respect of prostate cancer, for example, such other information may include serum PSA measurements, DRE and/or ultrasonography. Further, the level of 36P6D5 detected in the serum may provide information useful in staging or prognosis. For example, as supported by the data presented in Figure 9 and 10, as cell populations expand and growth through the stroma and microvasculature, higher levels of 36P6D5 are expected to be observed in serum. In this context, very high levels of 36P6D5 protein in serum may suggest larger and/or more aggressive tumors. In addition, peripheral blood and bone marrow may be convenientiy assayed for the presence of 36P6D5 protein and/or 36P6D5 expressing cancer ceUs, including but not limited to prostate, bladder, colon, pancreatic, kidney and ovarian cancers, using RT-PCR to detect 36P6D5 expression. The presence of RT-PCR amplifiable 36P6D5 mRNA provides an indication of the presence of the cancer. RT-PCR detection assays for tumor ceUs in peripheral blood are currendy being evaluated for use in the diagnosis and management of a number of human solid tumors. In the prostate cancer field, these include RT-PCR assays for the detection of ceUs expressing PSA and PSM (Verkaik et al, 1997, Urol. Res. 25: 373- 384; Ghossein et al, 1995, J. Clin. Oncol. 13: 1195-2000; Heston et al, 1995, Clin. Chem. 41: 1687-1688). RT-PCR assays are weU known in the art. In one embodiment, a capture ELISA is used to detect and quantify 36P6D5 in serum, urine or semen. A capture ELISA for 36P6D5 comprises, generaUy, at least two monoclonal antibodies of different isotypes that recognize distinct epitopes of the 36P6D5 protein, or one anti-36P6D5 monoclonal antibody and a specific polyclonal serum derived from a different species (e.g, rabbit, goat, sheep, hamster, etc.). In this assay, one reagent serves as the capture (or coating) antibody and the other as the detection antibody. As shown in Table 2, clinical serum samples from and pancreatic cancer patients, and normal male donors were screened for 36P6D5 protein using a capture ELISA as described above and in Figure 10. Supernatants from PC-3-36P6D5 and Du4475 ceUs, and from PC-3-neo ceUs, served as positive and negative controls, respectively for 36P6D5 protein detection. ND: not detected or below detection sensitivity. 36P6D5 protein was detected in 7/10 colon cancer patients and 6/10 pancreatic cancer patients, one of which had relatively high levels (29.70 ng/ml), but only in 1 /6 normal male donors. In a related embodiment, FACS analysis is used for the detection of ceUs expressing 36P6D5 protein, for example those that have escaped the local site of disease and have migrated to other sites such as the lymphatic system. As discussed in detail below, levels of 36P6D5 including 36P6D5 serum levels may be used to provide an indication of the presence, extent and aggressiveness of a 36P6D5 expressing tumor. As noted, above 36P6D5 shares a number of characteristics with PSA which is the most important, accurate, and chnicaUy useful biochemical marker in the prostate. Any process that disrupts the normal architecture of the prostate aUows diffusion of PSA into the stroma and microvasculature. Consequendy, chnicaUy important increases in serum prostate-specific antigen levels are seen with prostatic cancers. In particular, the greater number of malignant ceUs and the stromal disruption associated with cancer account for the increased serum prostate-specific antigen level. In this context, serum prostate-specific antigen levels correlate positively with clinical stage, tumor volume, histologic grade, and the presence of capsular perforation and seminal vesicle invasion. See e.g. Bostwick, D.G. Am. J. Clin. Pathol. 102 (4 Suppl 1): S31-S37 (1994). Using PSA as an analogous molecule, is likely that because 36P6D5 is also a secreted molecule that exhibits a restricted pattern of tissue expression (including the prostate), the increasing load of malignant ceUs and the stromal disruption that occurs with cancer wiU make the serum 36P6D5 antigen levels correlate positively with one or more chnicaUy relevant factors such as clinical stage, tumor volume, histologic grade, and the presence of capsular perforation and seminal vesicle invasion. Serum 36P6D5 measurements over time would be expected to provide further information, wherein an increase in 36P6D5 would be expected to reflect progression and the rate of the increase would be expected to correlate with aggressiveness. Similarly, a decline in serum 36P6D5 would be expected to reflect a slower growing or regressing tumor. The identification of 36P6D5 in serum may be useful to detect tumor initiation and early stage disease. In patients who have undergone surgery or therapy, serum 36P6D5 levels would be useful for monitoring treatment response and potential recurrence. MONITORING THE STATUS OF 36P6D5 AND ITS PRODUCTS Assays that evaluate the status of the 36P6D5 gene and 36P6D5 gene products m an individual may provide information on the growth or oncogenic potential of a biological sample from this individual. For example, because 36P6D5 mRNA is so highly expressed m prostate cancers as compared to normal prostate tissue, assays that evaluate the relative levels of 36P6D5 mRNA transcnpts or protems m a biological sample may be used to diagnose a disease associated with 36P6D5 dysregulation such as cancer and may provide prognostic information useful m defining appropriate therapeutic options Because 36P6D5 is expressed, for example, m vanous prostate cancer xenograft tissues and cancer ceU lines, and cancer patient samples, the expression status of 36P6D5 can provide information useful for determining information mcludmg the presence, stage and location of displasic, precancerous and cancerous ceUs, predicting susceptibility to vanous stages of disease, and/or for gauging tumor aggressiveness. Moreover, the expression profile makes it a potential imaging reagent for metastasized disease. Consequendy, an important aspect of the mvention is directed to the vanous molecular prognostic and diagnostic methods for examining the status of 36P6D5 m biological samples such as those from individuals suffering from, or suspected of suffering from a pathology characterized by dysregulated ceUular growth such as cancer. Oncogenesis is known to be a multistep process where ceUular growth becomes progressively dysregulated and ceUs progress from a normal physiological state to precancerous and then cancerous states (see e.g. Alers et al. Lab Invest 77(5): 437-438 (1997) and Isaacs et al. Cancer Surv. 23. 19-32 (1995)). In this context, examining a biological sample for evidence of dysregulated ceU growth (such as aberrant 36P6D5 expression in prostate cancers) can aUow the early detection of such aberrant ceUular physiology before a pathology such as cancer has progressed to a stage at wl ich therapeutic options are more limited. In such examinations, the status of 36P6D5 m a biological sample of interest (such as one suspected of havmg dysregulated ceU growth) can be compared, for example, to the status of 36P6D5 m a corresponding normal sample (e.g. a sample from that individual (or alternatively another individual) that is not effected by a pathology, for example one not suspected of having dysregulated ceU growth) with alterations m the status of 36P6D5 in the biological sample of interest (as compared to the normal sample) providing evidence of dysregulated ceUular growth In addition to usmg a biological sample that is not effected by a pathology as a normal sample, one can also use a predetermined normative value such as a predetermined normal level of mRNA expression (see e.g. Grever et al , J Comp. Neurol 1996 Dec 9;376(2):306-14 and U S. patent No. 5,837,501) to compare 36P6D5 m normal versus suspect samples. The term "status" m this context is used according to its art accepted meaning and refers to the condition or state of a gene and its products. As specificaUy descnbed herem, the status of 36P6D5 can be evaluated by a number of parameters known m the art. TypicaUy an alteration m the status of 36P6D5 comprises a change m the location of 36P6D5 expressmg ceUs and/or an mcrease m 36P6D5 mRNA and/or protem expression. TypicaUy, skilled artisans use a number of parameters to evaluate the condition or state of a gene and its products. These mclude, but are not limited to the location of expressed gene products (mcludmg the location of 36P6D5 expressing ceUs) as weU as the, level, and biological activity of expressed gene products (such as 36P6D5 mRNA polynucleotides and polypeptides). Alterations in the status of 36P6D5 can be evaluated by a wide variety of methodologies weU known m the art, typicaUy those discussed below. TypicaUy an alteration m the status of 36P6D5 comprises a change in the location of 36P6D5 and/or 36P6D5 expressmg ceUs and/or an mcrease in 36P6D5 mRNA and/or protem expression. As discussed m detail herem, m order to identify a condition or phenomenon associated with dysregulated ceU growth, the status of 36P6D5 m a biological sample may be evaluated by a number of methods utilized by skilled artisans mcludmg, but not limited to genomic Southern analysis (to examine, for example perturbations in the 36P6D5 gene), northerns and/or PCR analysis of 36P6D5 mRNA (to examme, for example alterations m the polynucleotide sequences or expression levels of 36P6D5 mRNAs), and western and/or immunohistochemical analysis (to examme, for example alterations in polypeptide sequences, alterations m polypeptide localization within a sample, alterations in expression levels of 36P6D5 protems and/or associations of 36P6D5 protems with polypeptide bmdmg partners). Detectable 36P6D5 polynucleotides mclude, for example, a 36P6D5 gene or fragments thereof, 36P6D5 mRNA, alternative sphce variants 36P6D5 mRNAs, and recombinant DNA or RNA molecules containing a 36P6D5 polynucleotide. The expression profile of 36P6D5 makes it a potential diagnostic marker for local and/or metastasized disease. In particular, the status of 36P6D5 may provide information useful for predicting susceptibility to particular disease stages, progression, and/or tumor aggressiveness. The invention provides methods and assays for deterrriining 36P6D5 status and diagnosing cancers that express 36P6D5, such as cancers of the prostate, bladder, bladder, kidney, ovaries, breast, pancreas, colon and lung. 36P6D5 status in patient samples may be analyzed by a number of means weU known in the art, including without limitation, immunohistochemical analysis, in situ hybridization, RT-PCR analysis on laser capture micro-dissected samples, western blot analysis of clinical samples and ceU lines, and tissue array analysis. Typical protocols for evaluating the status of the 36P6D5 gene and gene products can be found, for example in Ausubul et al. eds, 1995, Current Protocols In Molecular Biology, Units 2 [Northern Blotting], 4 [Southern Blotting], 15 [Immunoblotting] and 18 [PCR Analysis] . As described above, the status of 36P6D5 in a biological sample can be examined by a number of weU known procedures in the art. For example, the status of 36P6D5 in a biological sample taken from a specific location in the body can be examined by evaluating the sample for the presence or absence of 36P6D5 expressing ceUs (e.g. those that express 36P6D5 mRNAs or proteins). This examination can provide evidence of dysregulated ceUular growth for example, when 36P6D5 expressing ceUs are found in a biological sample that does not normaUy contain such ceUs (such as a lymph node). Such alterations in the status of 36P6D5 in a biological sample are often associated with dysregulated ceUular growth. SpecificaUy, one indicator of dysregulated ceUular growth is the metastases of cancer ceUs from an organ of origin (such as the bladder, kidney or prostate gland) to a different area of the body (such as a lymph node). In this context, evidence of dysregulated ceUular growth is important for example because occult lymph node metastases can be detected in a substantial proportion of patients with prostate cancer, and such metastases are associated with known predictors of disease progression (see e.g. J Urol 1995 Aug;154(2 Pt l):474-8). In one aspect, the invention provides methods for monitoring 36P6D5 gene products by determining the status of 36P6D5 gene products expressed by ceUs in a test tissue sample from an individual suspected of havmg a disease associated with dysregulated ceU growth (such as hyperplasia or cancer) and then comparmg the status so determined to the status of 36P6D5 gene products in a corresponding normal sample, the presence of aberrant 36P6D5 gene products m the test sample relative to the normal sample providing an indication of the presence of dysregulated ceU growth within the ceUs of the individual. In another aspect, the mvention provides assays useful m determining the presence of cancer in an individual, comprising detecting a significant increase m 36P6D5 mRNA or protein expression m a test ceU or tissue sample relative to expression levels m the corresponding normal ceU or tissue. The presence of 36P6D5 mRNA may, for example, be evaluated in tissue samples mcludmg but not limited to prostate, kidney, bladder, ovarian, breast, pancreas, colon and lung issues (see e.g. FIGS. 4, 6 and 7). The presence of significant 36P6D5 expression m any of these tissues may be useful to mdicate the emergence, presence and/or severity of these cancers, smce the correspondmg normal tissues do not express 36P6D5 mRNA or express it at lower levels. In a related embodiment, 36P6D5 status may be determined at the protem level rather than at the nucleic acid level. For example, such a method or assay would compnse determining the level of 36P6D5 protem expressed by ceUs m a test tissue sample and comparmg the level so determined to the level of 36P6D5 expressed m a corresponding normal sample. In one embodiment, the presence of 36P6D5 protein is evaluated, for example, usmg immunohistochemical methods. 36P6D5 antibodies or bmdmg partners capable of detecting 36P6D5 protem expression may be used m a vanety of assay formats weU known m the art for this purpose. In other related embodiments, one can evaluate the integrity 36P6D5 nucleotide and ammo acid sequences in a biological sample m order to identify perturbations m the structure of these molecules such as insertions, deletions, substitutions and the like. Such embodiments are useful because perturbations m the nucleotide and ammo aαd sequences are observed m a large number of protems associated with a growth dysregulated phenotype (see, e.g, Marrogi et al, 1999, J. Cutan. Pathol. 26(8):369-378). In this context, a wide vanety of assays for observing perturbations m nucleotide and ammo acid sequences are weU known in the art. For example, the size and structure of nucleic acid or ammo acid sequences of 36P6D5 gene products may be observed by the Northern, Southern, Western, PCR and DNA sequencing protocols discussed herem. In addition, other methods for observing perturbations in nucleotide and ammo acid sequences such as smgle strand conformation polymorphism analysis are weU known m the art (see, e.g, U.S Patent Nos. 5,382,510 and 5,952,170). In another embodiment, one can examine the methylation status of the 36P6D5 gene m a biological sample. Aberrant demethylation and/or hypermethylation of CpG islands m gene 5' regulatory regions frequendy occurs in immortalized and transformed ceUs and can result in altered expression of vanous genes. For example, promoter hypermethylation of the pi-class glutathione S-transferase (a protem expressed m normal prostate but not expressed m >90% of prostate carcinomas) appears to permanendy sdence transcription of this gene and is the most frequendy detected genomic alteration m prostate carcmomas (De Marzo et al. Am. J. Pathol. 155(6): 1985-1992 (1999)). In addition, this alteration is present m at least 70% of cases of high-grade prostatic intraepithehal neoplasia (PIN) (Brooks et al, Cancer Epidemiol. Biomarkers Prev, 1998, 7:531-536). In another example, expression of the LAGE-I tumor specific gene (which is not expressed in normal prostate but is expressed m 25-50% of prostate cancers) is mduced by deoxy-azacytidine m lymphoblastoid ceUs, suggesting that tumoral expression is due to demethylation (Lethe et al. Int. J. Cancer 76(6): 903-908 (1998)). In this context, a vanety of assays for exammmg methylation status of a gene are weU known m the art. For example, one can utilize in Southern hybndtzation approaches methylation- sensitive restnction enzymes which can not cleave sequences that contam methylated CpG sites m order to assess the overaU methylation status of CpG islands. In addition, MSP (methylation specific PCR) can rapidly profile the methylation status of aU the CpG sites present in a CpG island of a given gene. This procedure mvolves initial modification of DNA by sodium bisulfite (which wiU convert aU unmethylated cytosmes to uracil) foUowed by amphfication usmg primers specific for methylated versus unmethylated DNA. Protocols involving methylation mterference can also be found for example m Current Protocols In Molecular Biology, Units 12, Fredenck M. Ausubul et al. eds, 1995. Gene amphfication provides an additional method of assessmg the status of 36P6D5, a locus that maps to 21q22.2-22 3, a region shown to be perturbed m a variety of cancers. Gene amphfication may be measured m a sample direcdy, for example, by conventional Southern blotting, Northern blotting to quantitate the transcription of mRNA (Thomas, 1980, Proc. Nad Acad. Sci. USA, 77:5201-5205), dot blotting (DNA analysis), or in situ hybridization, usmg an appropriately labeled probe, based on the sequences provided herem. Alternatively, antibodies may be employed that can recognize specific duplexes, mcludmg DNA duplexes, RNA duplexes, and DNA-RNA hybrid duplexes or DNA-protein duplexes. The antibodies m turn may be labeled and the assay may be carried out where the duplex is bound to a surface, so that upon the formation of duplex on the surface, the presence of antibody bound to the duplex can be detected. In addition to the tissues discussed above, biopsied tissue or penpheral blood or bone marrow may be conveniendy assayed for the presence of cancer ceUs, mcludmg but not limited to prostate, kidney, bladder, ovarian, breast, pancreas, colon and lung cancers usmg for example, Northern, dot blot or RT-PCR analysis to detect 36P6D5 expression (see e.g. FIGS 4, 6 and 7) The presence of RT-PCR amphfiable 36P6D5 mRNA provides an mchcation of the presence of the cancer. RT-PCR detection assays for tumor ceUs m penpheral blood are currendy bemg evaluated for use in the diagnosis and management of a number of human sohd tumors. In the prostate cancer field, these mclude RT-PCR assays for the detection of ceUs expressmg PSA and PSM (Verkaik et al, 1997, Urol. Res. 25:373- 384; Ghossem et al, 1995, J. Clin. Oncol 13:1195-2000; Heston et al, 1995, Clin. Chem. 41:1687-1688). RT-PCR assays are weU known in the art A related aspect of the mvention is directed to predicting susceptibihty to developmg cancer in an individual. In one embodiment, a method for predicting susceptibihty to cancer compnses detecting 36P6D5 mRNA or 36P6D5 protem m a tissue sample, its presence indicating susceptibihty to cancer, wherem the degree of 36P6D5 mRNA expression present is proportional to the degree of susceptibihty. In a speαfic embodiment, the presence of 36P6D5 m prostate tissue is examined, with the presence of 36P6D5 m the sample providing an indication of prostate cancer susceptibihty (or the emergence or existence of a prostate tumor) In another specific embodiment, the presence of 36P6D5 in tissue is examined, with the presence of 36P6D5 m the sample providing an mchcation of cancer susceptibihty (or the emergence or existence of a tumor). In a closely related embodiment, one can evaluate the integnty 36P6D5 nucleotide and ammo acid sequences m a biological sample m order to identify perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like, with the presence of one or more perturbations m 36P6D5 gene products m the sample providing an mchcation of cancer susceptibihty (or the emergence or existence of a tumor). Yet another related aspect of the mvention is directed to methods for gauging tumor aggressiveness. In one embodiment, a method for gauging aggressiveness of a tumor compnses determirung the level of 36P6D5 mRNA or 36P6D5 protein expressed by ceUs m a sample of the tumor, comparmg the level so determined to the level of 36P6D5 mRNA or 36P6D5 protem expressed in a corresponding normal tissue taken from the same individual or a normal tissue reference sample, wherem the degree of 36P6D5 mRNA or 36P6D5 protem expression m the tumor sample relative to the normal sample indicates the degree of aggressiveness. In a specific embodiment, aggressiveness of a tumor is evaluated by determining the extent to which 36P6D5 is expressed m the tumor ceUs, with higher expression levels indicating more aggressive tumors. In a closely related embodiment, one can evaluate the integnty of 36P6D5 nucleotide and ammo acid sequences in a biological sample m order to identify perturbations m the structure of these molecules such as insertions, deletions, substitutions and the like, with the presence of one or more perturbations indicating more aggressive tumors. The mvention additionaUy provides methods of examining a biological sample for evidence of dysregulated ceUular growth. In one embodiment, the method compnses comparing the status of 36P6D5 m the biological sample to the status of 36P6D5 m a correspondmg normal sample, wherem alterations in the status of 36P6D5 m the biological sample are associated with dysregulated ceUular growth The status of 36P6D5 m the biological sample can be evaluated by, for example, exammmg levels of 36P6D5 mRNA expression or levels of 36P6D5 protem expression. In one embodiment, an alteration in the status of 36P6D5 is identified by the presence of 36P6D5 expressmg ceUs m a biological sample from a tissue m which 36P6D5 expressmg ceUs are normaUy absent. In another aspect, the mvention provides assays useful in determirung the presence of cancer m an individual, compnsmg detecting a significant mcrease m 36P6D5 mRNA or protem expression m a test ceU or tissue sample relative to expression levels m the correspondmg normal ceU or tissue. The presence of 36P6D5 mRNA may, for example, be evaluated m tissue samples mcludmg but not limited to colon, lung, prostate, pancreas, bladder, breast, ovary, cervix, testis, head and neck, brain, stomach, bone, etc. The presence of significant 36P6D5 expression in any of these tissues may be useful to indicate the emergence, presence and/or severity of these cancers or a metastasis of cancer originating in another tissue, since the corresponding normal tissues do not express 36P6D5 mRNA or express it at lower levels. Yet another related aspect of the invention is directed to methods for observing the progression of a malignancy in an individual over time. In one embodiment, methods for observing the progression of a malignancy in an individual over time comprise deterrriining the level of 36P6D5 mRNA or 36P6D5 protein expressed by ceUs in a sample of the tumor, comparing the level so determined to the level of 36P6D5 mRNA or 36P6D5 protein expressed in an equivalent tissue sample taken from the same individual at a different time, wherein the degree of 36P6D5 mRNA or 36P6D5 protein expression in the tumor sample over time provides information on the progression of the cancer. In a specific embodiment, the progression of a cancer is evaluated by determiriing the extent to which 36P6D5 expression in the tumor ceUs alters over time, with higher expression levels indicating a progression of the cancer. In a closely related embodiment, one can evaluate the integrity 36P6D5 nucleotide and amino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like, with the presence of one or more perturbations indicating a progression of the cancer. The above diagnostic approaches may be combined with any one of a wide variety of prognostic and diagnostic protocols known in the art. For example, another embodiment of the invention disclosed herein is directed to methods for observing a coincidence between the expression of 36P6D5 gene and 36P6D5 gene products (or perturbations in 36P6D5 gene and 36P6D5 gene products) and a factor that is associated with malignancy as a means of diagnosing and prognosticating the status of a tissue sample. In this context, a wide variety of factors associated with malignancy may be utilized such as the expression of genes otherwise associated with malignancy (including PSA, PSCA and PSM expression) as weU as gross cytological observations (see e.g. Bocking et al, 1984, Anal. Quant. Cytol. 6(2):74-88; Eptsein, 1995, Hum. Pathol. 26(2):223-9; Thorson et al, 1998, Mod. Pathol. 11 (6):543-51; Baisden et al, 1999, Am. J. Surg. Pathol. 23(8):918-24). Methods for observing a coincidence between the expression of 36P6D5 gene and 36P6D5 gene products (or perturbations in 36P6D5 gene and 36P6D5 gene products) and an additional factor that is associated with malignancy are useful, for example, because the presence of a set or consteUation of specific factors that coincide provides information crucial for diagnosing and prognosticating the status of a tissue sample. In a typical embodiment, methods for observing a coincidence between the expression of 36P6D5 gene and 36P6D5 gene products (or perturbations in 36P6D5 gene and 36P6D5 gene products) and a factor that is associated with malignancy entaUs detecting the overexpression of 36P6D5 mRNA or protein in a tissue sample, detecting the overexpression of PSA mRNA or protein in a tissue sample, and observing a coincidence of 36P6D5 mRNA or protein and PSA mRNA or protein overexpression. In a specific embodiment, the expression of 36P6D5 and PSA mRNA in prostate tissue is examined. In a preferred embodiment, the coincidence of 36P6D5 and PSA mRNA overexpression in the sample provides an indication of prostate cancer, prostate cancer susceptibihty or the emergence or existence of a prostate tumor. Methods for detecting and quantifying the expression of 36P6D5 mRNA or protein are described herein and use of standard nucleic acid and protein detection and quantification technologies is weU known in the art. Standard methods for the detection and quantification of 36P6D5 mRNA include in situ hybridization using labeled 36P6D5 riboprobes, Northern blot and related techniques using 36P6D5 polynucleotide probes, RT- PCR analysis using primers specific for 36P6D5, and other amphfication type detection methods, such as, for example, branched DNA, SISBA, TMA and the like. In a specific embodiment, semi-quantitative RT-PCR may be used to detect and quantify 36P6D5 mRNA expression as described in the Examples that foUow. Any number of primers capable of amphfying 36P6D5 may be used for this purpose, including but not limited to the various primer sets specificaUy described herein. Standard methods for the detection and quantification of protein may be used for this purpose. In a specific embodiment, polyclonal or monoclonal antibodies specificaUy reactive with the wild-type 36P6D5 protein may be used in an in tnunohistochernical assay of biopsied tissue. IDENTIFYING MOLECULES THAT INTERACT WITH 36P6D5 The 36P6D5 protein sequences disclosed herein aUow the skiUed artisan to identify proteins, smaU molecules and other agents that interact with 36P6D5 and pathways activated by 36P6D5 via any one of a variety of art accepted protocols For example one can utilize one of the variety of so-caUed interaction trap systems (also referred to as the "two-hybrid assay") In such systems, molecules that mteract reconstitute a transcription factor and direct expression of a reporter gene, the expression of which is then assayed. Typical systems identify protein-protein interactions in vivo through reconstitution of a eukaryotic transcriptional activator and are disclosed for example m U S. Patent Nos. 5,955,280, 5,925,523, 5,846,722 and 6,004,746. Alternatively one can identify molecules that mteract with 36P6D5 protem sequences by screening peptide hbranes In such methods, peptides that bmd to selected receptor molecules such as 36P6D5 are identified by screening hbranes that encode a random or controUed coUection of amino acids. Peptides encoded by the hbranes are expressed as fusion protems of bactenophage coat protems, and bactenophage particles are then screened agamst the receptors of interest. Peptides havmg a wide variety of uses, such as therapeutic or diagnostic reagents, may thus be identified without any prior information on the structure of the expected hgand or receptor molecule. Typical peptide hbranes and screening methods that can be used to identify molecules that interact with 36P6D5 protem sequences are disclosed for example m U.S. Patent Nos 5,723,286 and 5,733,731. Alternatively, ceU hnes expressmg 36P6D5 can be used to identify protem-protem interactions mediated by 36P6D5. This possibility can be examined usmg lmmunoprecipitation techmques as shown by others (Hamilton BJ, et al. Biochem. Biophys. Res. Commun. 1999, 261.646-51). TypicaUy 36P6D5 protem can be immunoprecipitated from 36P6D5 expressmg prostate cancer ceU hnes usmg anti- 36P6D5 antiboches. Alternatively, antibodies agamst His-tag can be used m a ceU line engmeered to express 36P6D5 (vectors mentioned above). The immunoprecipitated complex can be examined for protem association by procedures such as western blotting, 35 S-methionine labehng of protems, protem microsequencing, silver staining and two dimensional gel electrophoresis. SmaU molecules that interact with 36P6D5 can be identified through related embodiments of such screening assays. For example, smaU molecules can be identified that mterfere with protein function, mcludmg molecules that interfere with 36P6D5's ability to mediate phosphorylation and de-phosphorylation, second messenger signaling and tumorigenesis. Typical methods are discussed for example in U.S. Patent No. 5,928,868 and include methods for forming hybrid hgands in which at least one hgand is a smaU molecule. In an iUustrative embodiment, the hybrid hgand is introduced into ceUs that in turn contain a first and a second expression vector. Each expression vector includes DNA for expressing a hybrid protein that encodes a target protein linked to a coding sequence for a transcriptional module. The ceUs further contains a reporter gene, the expression of which is conditioned on the proximity of the first and second hybrid proteins to each other, an event that occurs only if the hybrid hgand binds to target sites on both hybrid proteins. Those ceUs that express the reporter gene are selected and the unknown smaU molecule or the unknown hybrid protein is identified. A typical embodiment of this invention consists of a method of screening for a molecule that interacts with a 36P6D5 amino acid sequence shown in FIG. 1 (SEQ ID NO: 2), comprising the steps of contacting a population of molecules with the 36P6D5 amino acid sequence, aUowing the population of molecules and the 36P6D5 amino acid sequence to interact under conditions that facilitate an interaction, determining the presence of a molecule that interacts with the 36P6D5 amino acid sequence and then separating molecules that do not interact with the 36P6D5 amino acid sequence from molecules that do interact with the 36P6D5 amino acid sequence. In a specific embodiment, the method further includes purifying a molecule that interacts with the 36P6D5 amino acid sequence. In a preferred embodiment, the 36P6D5 amino acid sequence is contacted with a library of peptides. USING 36P6D5 TO MODULATE CELLULAR MICROENVIRONMENTS A variety of secreted proteins have been described in prostate cancer, a number of which have been shown to participate in the process of tumor formation and progression (Inoue K. Clin Cancer Res. 2000;6:2104-19, Dow JK, deVere White RW. Urology. 2000;55:800-6 ). In the process of tumor progression, cancer ceUs to secrete and express molecules that aUow them to grow in both the microenvironment of the local prostate as weU as the bone microenvironment. A unique feature of prostate cancer is that in the process of tumor progression, cancer ceUs become metastatic to bone and recent studies suggest that this predilection to metastasize to the bone is based on the ability of prostate cancer ceUs to secrete and express molecules that aUow them to grow m the bone microenvironment (Koeneman KS, Yeung F, Chung LW. Prostate 1999: 39:246). In this context, the data presented herem (see e.g Figures 8 and 9) suggests that 36P6D5 plays a role (1) in targeting prostate ceUs to the bone, (2) aUowmg the growth of prostate ceUs m the bone microenvironment, (3) mducmg the differentiation of prostate tumor ceUs or bone marrow ceUs to osteoblasts or (4) supporting the interaction of bone stroma with prostate cancer ceUs thereby creating a favorable environment for the growth of cancer ceUs. Consequendy, this molecule can be used m methods for conditioning media and/or rnimicking the microenvironment m which prostate cancer ceUs can metastasize. In order to test the possibility that 36P6D5 mteracts with ceUs normaUy located in the prostate and bone microenvironments, the 36P6D5 protem was expressed as a recombinant protem (pTag5 36P6D5). Purified recombιnant-36P6D5 was then mcubated with a variety of relevant ceU types, mcludmg prostate epithelial ceUs, prostate tumor ceU lines, prostate stromal ceUs, osteosarcoma and bone stromal ceUs. Bmdmg of 36P6D5 to intact ceUs is detected by FACS analysis and by calorimetric assay. Our studies indicated that, when the recombinant 36P6D5 AP-fusion protem is mcubated m the presence of prostate cancer ceUs derived from LAPC4 and LAPC9 xenografts, it binds to LAPC9 and LAPC4 xenograft ceUs. Bmdmg of 36P6D5 to the ceU surface was detected usmg calorimetric change m AP substrate (Figure 8). In contrast, no color conversion was observed when ceUs were mcubated with the appropriate control. This analysis is valuable as it identifies a ceU population that binds and may respond to 36P6D5. In addition, the identification of a target ceU population may provide a means of isolating and identifymg 36P6D5 receptors. Tins information can be used m a variety of therapeutic application and smaU molecule design. Usmg the data presented herem (see e g. Figure 8), one can employ methods to modulate cancer ceU phenotypes and dissect the different stages of metastasis by reproducmg the microenvironment of the local prostate in which cancer ceUs oπgmate as weU metastatic ceUular microenvironment, thereby generating a cancer model in which artisans can assess novel therapeutic and diagnostic compositions and methods. An iUustrative method consists of modulating the microenvironment of a ceU by exposmg the ceU to a 36P6D5 polypeptide so that the polypeptide bmds to the ceU, thereby modulating the microenvironment of the ceU. A related method m this context consists of modulating the microenvironment of a ceU by exposing the ceU to a molecule that interacts with a 36P6D5 polypeptide (such as an anti-36P6D5 antibody) that inhibits or facilitates the binding of the polypeptide to the ceU, thereby modulating the microenvironment of the ceU. Such methods for generating or modulating a specific microenvironmental milieu satisfy a need in the art to generate a variety diverse microenvironments based on observations that cancer ceUs (including prostate cancer ceUs) are differentiaUy regulated depending upon the factors present in the ceU microenvironment (see e.g. Levesque et al. Endocrinology 139(5): 2375-2381 (1998). Consequendy the identification 36P6D5 proteins as molecules which are both secreted by and bind to ceUs in this microenvironment aUows the skilled artisan to use this information to include and/or manipulate 36P6D in contexts that more faithfuUy reproduce and modulate the events occurring in the progression of cancers. A number of experiments can designed to investigate how 36P6D5 may contribute to the growth of prostate cancer ceUs. In a first typical set of experiments, prostate cancer epithelial ceUs are incubated in the presence or absence of recombinant 36P6D5, and evaluated for prohferation using a weU-documented calorimetric assay. In paraUel, PC3 ceUs engineered to stably express 36P6D5 are evaluated for ceU growth potential. In a second typical set of experiments, tagged prostate cancer ceUs, such as PC3 ceUs engineered to express the Green Fluorescence Protein (GFP), are grown in the presence of bone stromal ceUs. The ceUs are incubated in the presence or absence of recombinant 36P6D5, and evaluated for ceU growth by measuring increase in GFP. Using the disclosure provided herein, it is possible to examine the role of 36P6D5 in bone metastasis. In order to deterrnine whether 36P6D5 induces prostate ceUs to become osteomimetic, primary prostate ceUs as weU as ceU lines can be grown in the presence or absence of recombinant purified 36P6D5. CeUs can be then examined for the expression of early and late markers of bone maturation, including osteonectin, osteopontin, alkaline phosphatase and osteocalcin. One can also determine whether 36P6D5 is inducing the expression of growth factors supportive of prostate ceU growth in a traditionaUy protective microenvironment such as the bone. PCR and ELISA techniques can be used to investigate the expression and secretion of FGF, HGF and IGF in ceUs grown in the presence or absence of recombinant purified 36P6D5. Similar experiments can be performed using bone marrow ceUs to determine whether 36P6D5 induces the differentiation of chondrocyte progenitors to mature osteocytes. These experiments may be valuable in demonstrating the role of 36P6D5 m supporting the creation of an environment favorable for prostate cancer growth in bone, and identifymg targets for therapeutic intervention. Usmg the disclosure provided herem, it is possible to examine the role of 36P6D5 m CeU-CeU Interaction. It is possible that 36P6D5 plays a role m recruiting prostate ceUs to the bone by enhancing prostate ceU interaction with stromal ceUs or osteocytes. GFP expressmg prostate cancer ceUs can be grown in the presence or absence of recombmant 36P6D5 protem. GPF ceUs can be mcubated with control or 36P6D5 treated stromal ceUs and osteocytes for various amounts of time. Non-adherent ceUs can be removed and adhesion to stroma and osteocytes can be evaluated by measuring the amount of GFP in the culture. This data wiU be critical in considering inhibitors of factors which modulate the microenvironment of the local prostate m which cancer ceUs ongmate and grow as the colonization of metastatic sites by cancer ceUs THERAPEUTIC METHODS AND COMPOSITIONS The identification of 36P6D5 as a gene that is highly expressed m cancers of the prostate (and possibly other cancers), opens a number of therapeutic approaches to the treatment of such cancers As discussed above, it is possible that 36P6D5 is secreted from cancer ceUs and m this way modulates prohferation signals. Its potential role as a transcription factor and its high expression in prostate cancer makes it a potential target for smaU molecule-mediated therapy. Accordingly, therapeutic approaches aimed at mhibitmg the activity of the 36P6D5 protem are expected to be useful for patients suffering from prostate cancer and other cancers expressmg 36P6D5. These therapeutic approaches aimed at mhibitmg the activity of the 36P6D5 protem generaUy faU mto two classes. One class comprises various methods for inhibiting the bmdmg or association of the 36P6D5 protein with its binding partoer or with other protems. Another class compnses a variety of methods for mhibitmg the transcnption of the 36P6D5 gene or translation of 36P6D5 mRNA. 36P6D5 as a Target for Antibody-Based Therapy The structural features of 36P6D5 indicate that this molecule is an attractive target for antibody-based therapeutic strategies. A number of typical antibody strategies are known m the art for targeting both extraceUular and intraceUular molecules (see e.g. complement and ADCC mediated killing as weU as the use of intrabodies discussed below). Because 36P6D5 is expressed by cancer ceUs of various lineages and not by corresponding normal ceUs, systemic administration of 36P6D5-ιmmunoreactive compositions would be expected to exhibit exceUent sensitivity without toxic, nonspecific and/or non-target effects caused by bmding of the lmmunothcrapeutic molecule to non-target organs and tissues Antiboches specificaUy reactive with domains of 36P6D5 can be useful to treat 36P6D5-expressιng cancers systemicaUy, either as conjugates with a toxin or therapeutic agent, or as naked antibodies capable of inhibiting ceU prohferation or function. 36P6D5 antiboches can be mtroduced mto a patient such that the antibody bmds to 36P6D5 and modulates or perturbs a function such as an interaction with a binding partner and consequendy mediates the growth inhibition and/or destruction of the ceUs and the tumor and/or inhibits the growth of the ceUs or the tumor. Mechanisms by which such antibodies exert a therapeutic effect may include complement-mechated cytolysis, antibody-dependent ceUular cytotoxicity, modulating the physiological function of 36P6D5, mhibitmg hgand bmdmg or signal transduction pathways, modulating tumor ceU differentiation, altermg tumor angiogenesis factor profiles, and/or by mducmg apoptosis. 36P6D5 antibodies can be conjugated to toxic or therapeutic agents and used to dehver the toxic or therapeutic agent direcdy to 36P6D5-beaπng tumor ceUs. Examples of toxic agents mclude, but are not limited to, calchemicin, maytansmoids, radioisotopes such as 131 I, ytnum, and bismuth Cancer lmmunotherapy usmg anti-36P6D5 antibodies may foUow the teachings generated from various approaches that have been successfuUy employed m the treatment of other types of cancer, including but not limited to colon cancer (Arlen et al, 1998, Cπt. Rev Immunol 18.133-138), multiple myeloma (Ozaki et al, 1997, Blood 90:3179-3186; Tsunenan et al, 1997, Blood 90.2437-2444), gastric cancer (Kasprzyk et al, 1992, Cancer Res. 52:2771-2776), B-ceU lymphoma (Funakoshi et al, 1996, J. Immunother. Emphasis Tumor Immunol 19:93-101), leukemia (Zhong et al, 1996, Leuk. Res. 20:581-589), colorectal cancer (Moun et al, 1994, Cancer Res. 54:6160-6166, Velders et al, 1995, Cancer Res. 55-4398-4403), and breast cancer (Shepard et al, 1991, J. Chn. Immunol. 11 117-127). Some therapeutic approaches involve con j ugation of naked antibody to a toxin, such as the conjugation of 131 I to anti-CD20 antibodies (e.g, Rituxan 1M , IDEC Pharmaceuticals Corp.), while others involve co-achninistration of antibodies and other therapeutic agents, such as Herceptin IM (trastuzumab) with pachtaxel (Genentech, Inc.). For treatment of prostate cancer, for example, 36P6D5 antiboches can be administered in conjunction with radiation, chemotherapy or hormone ablation. Although 36P6D5 antibody therapy may be useful for aU stages of cancer, antibody therapy may be particularly appropriate in advanced or metastatic cancers. Treatment with the antibody therapy of the invention may be indicated for patients who have received previously one or more chemotherapy, whUe combining the antibody therapy of the invention with a chemotherapeutic or radiation regimen may be preferred for patients who have not received chemotherapeutic treatment. AdditionaUy, antibody therapy may enable the use of reduced dosages of concomitant chemotherapy, particularly for patients who do not tolerate the toxicity of the chemotherapeutic agent very weU. It may be desirable for some cancer patients to be evaluated for the presence and level of 36P6D5 expression, preferably using immunohistochemical assessments of tumor tissue, quantitative 36P6D5 imaging, or other techniques capable of reliably indicating the presence and degree of 36P6D5 expression. Irnmunohistochemical analysis of tumor biopsies or surgical specimens may be preferred for this purpose. Methods for irnmunohistochemical analysis of tumor tissues are weU known in the art. Anti-36P6D5 monoclonal antibodies useful in treating prostate and other cancers include those that are capable of initiating a potent immune response against the tumor and those that are capable of direct cytotoxicity. In this regard, anti-36P6D5 monoclonal antibodies (mAbs) may ehcit tumor ceU lysis by either complement-mediated or antibody-dependent ceU cytotoxicity (ADCC) mechanisms, both of which require an intact Fc portion of the immunoglobulin molecule for interaction with effector ceU Fc receptor sites or complement proteins. In addition, anti-36P6D5 mAbs that exert a direct biological effect on tumor growth are useful in the practice of the invention. Potential mechanisms by which such direcdy cytotoxic mAbs may act include inhibition of ceU growth, modulation of ceUular differentiation, modulation of tumor angiogenesis factor profiles, and the induction of apoptosis. The mechanism by which a particular anti-36P6D5 mAb exerts an anti-tumor effect may be evaluated usmg any number of m vitro assays designed to determine ADCC, ADMMC, complement-mechated ceU lysis, and so forth, as is generaUy known in the art The use of murine or other non-human monoclonal antiboches, or human/mouse chtmenc mAbs may mduce moderate to strong immune responses m some patients. In some cases, this wiU result m clearance of the antibody from circulation and reduced efficacy. In the most severe cases, such an immune response may lead to the extensive formation of immune complexes which, potentiaUy, can cause renal failure. Accordingly, preferred monoclonal antiboches used in the practice of the therapeutic methods of the mvention are those that are either fully human or humanized and that bind specificaUy to the target 36P6D5 antigen with high affinity but exhibit low or no antigenicity m the patient Therapeutic methods of the mvention contemplate the administration of smgle anti-36P6D5 mAbs as weU as combinations, or cocktails, of different mAbs. Such mAb cocktads may have certam advantages masmuch as they contam mAbs that target different epitopes, exploit different effector mechanisms or combine direcdy cytotoxic mAbs with mAbs that rely on immune effector functionality. Such mAbs m combmation may exhibit synergistic therapeutic effects. In addition, the administration of anti-36P6D5 mAbs may be combmed with other therapeutic agents, including but not limited to various chemotherapeutic agents, androgen-blockers, and immune modulators (e.g, IL-2, GM-CSF). The anti-36P6D5 mAbs may be administered m their "naked" or unconjugated form, or may have therapeutic agents conjugated to them The anti-36P6D5 antibody formulations may be administered via any route capable of delivering the antibodies to the tumor site PotentiaUy effective routes of administration mclude, but are not limited to, intravenous, intraperitoneal, intramuscular, lntratumor, intradermal, and the like. Treatment wiU generaUy mvolve the repeated administration of the anti-36P6D5 antibody preparation via an acceptable route of administration such as intravenous injection (IV), typicaUy at a dose in the range of about 0.1 to about 10 mg/kg body weight Doses in the range of 10-500 mg mAb per week may be effective and weU tolerated. Based on clinical experience with the Herceptin mAb m the treatment of metastatic breast cancer, an initial loading dose of approximately 4 mg/kg patient body weight IV foUowed by weekly doses of about 2 mg/kg LV of the anti- 36P6D5 mAb preparation may represent an acceptable dosing regimen. Preferably, the mitial loadmg dose is administered as a 90 minute or longer infusion. The periodic maintenance dose may be administered as a 30 minute or longer infusion, provided the mitial dose was weU tolerated. However, as one of skiU m the art wiU understand, various factors wiU influence the ideal dose regimen m a particular case. Such factors may mclude, for example, the bmdmg affinity and half hfe of the Ab or mAbs used, the degree of 36P6D5 expression in the patient, the extent of circulating shed 36P6D5 antigen, the desired steady-state antibody concentration level, frequency of treatment, and the influence of chemotherapeutic agents used m combination with the treatment method of the mvention. OptimaUy, patients should be evaluated for the level of circulating shed 36P6D5 antigen in serum m order to assist in the determination of the most effective dosmg regimen and related factors. Such evaluations may also be used for monitoring purposes throughout therapy, and may be useful to gauge therapeutic success in combmation with evaluating other parameters (such as serum PSA levels m prostate cancer therapy). Inhibition of 36P6D5 Protein Function The mvention mcludes various methods and compositions for inhibiting the binding of 36P6D5 to its bmding partner or hgand, or its association with other proteιn(s) as weU as methods for mhibitmg 36P6D5 function. Inhibition of 36P6D5 With IntraceUular Antibodies In one approach, recombmant vectors encodmg single cham antibodies that specificaUy bmd to 36P6D5 may be mtroduced mto 36P6D5 expressmg ceUs via gene transfer technologies, wherem the encoded smgle cham anti-36P6D5 antibody is expressed mtraceUularly, binds to 36P6D5 protem, and thereby inhibits its function. Methods for engineering such IntraceUular smgle cham antibodies are weU known. Such IntraceUular antibodies, also known as "intrabodies", may be specificaUy targeted to a particular compartment within the ceU, providing control over where the inhibitory activity of the treatment wiU be focused This technology has been successfully apphed m the art (for review, see Richardson and Marasco, 1995, TIBTECH vol. 13). Intrabodies have been shown to virtuaUy eliminate the expression of otherwise abundant ceU surface receptors. See, for example, Richardson et al, 1995, Proc Nad. Acad. Sci. USA 92: 3137-3141; Beerh et al, 1994, J. Biol. Chem. 289. 23931-23936; Deshane et al, 1994, Gene Ther. 1: 332-337. Smgle cham antiboches comprise the variable domains of the heavy and light chain j omed by a flexible linker polypeptide, and are expressed as a smgle polypeptide. OptionaUy, smgle cham antibodies may be expressed as a smgle cham variable region fragment j omed to the light cham constant region. WeU known IntraceUular trafficking signals may be engmeered into recombinant polynucleotide vectors encoding such smgle cham antibodies m order to precisely target the expressed mtrabody to the desired IntraceUular compartment. For example, mtraboches targeted to the endoplasmic reticulum (ER) may be engmeered to incorporate a leader peptide and, optionaUy, a C- terminal ER retention signal, such as the KDEL ammo acid motif. Intrabodies intended to exert activity m the nucleus may be engmeered to mclude a nuclear localization signal. Lipid moieties may be j omed to mtraboches m order to tether the mtrabody to the cytosohc side of the plasma membrane Intrabodies may also be targeted to exert function m the cytosol. For example, cytosohc mtraboches may be used to sequester factors within the cytosol, thereby preventing them from bemg transported to their natural ceUular destination. In one embodiment, mtraboches may be used to capture 36P6D5 m the nucleus, thereby preventing its activity within the nucleus. Nuclear targeting signals may be engmeered mto such 36P6D5 mtraboches m order to achieve the desired targeting. Such 36P6D5 mtraboches may be designed to bmd specificaUy to a particular 36P6D5 domam. In another embodiment, cytosohc mtraboches that specificaUy bind to the 36P6D5 protem may be used to prevent 36P6D5 from gaining access to the nucleus, thereby preventing it from exerting any biological activity within the nucleus (e.g., preventing 36P6D5 from forming transcription complexes with other factors). In order to specificaUy direct the expression of such mtraboches to particular tumor ceUs, the transcription of the mtrabody may be placed under the regulatory control of an appropriate tumor-specific promoter and/or enhancer. In order to target mtrabody expression specificaUy to prostate, for example, the PSA promoter and/or promoter/enhancer may be utilized (See, for example, U S Patent No. 5,919,652). Inhibition of 36P6D5 With Recombmant Protems In another approach, recombmant molecules that are capable of bmchng to 36P6D5 thereby preventing 36P6D5 from accessing/binding to its bmding partoer(s) or associating with other protem(s) are used to inhibit 36P6D5 function. Such recombinant molecules may, for example, contam the reactive part(s) of a 36P6D5 specific antibody molecule. In a particular embodiment, the 36P6D5 bmdmg domam of a 36P6D5 bmdmg partoer may be engineered mto a dimenc fusion protem compnsmg two 36P6D5 hgand bmdmg domains linked to the Fc portion of a human IgG, such as human IgGl Such IgG portion may contain, for example, the C H 2 and C H 3 domains and the hinge region, but not the C H 1 domam. Such dimenc fusion protems may be administered m soluble form to patients suffering from a cancer associated with the expression of 36P6D5, mcludmg but not limited to prostate, bladder, ovarian, breast, pancreas, colon and lung cancers, where the dimenc fusion protem specificaUy bmds to 36P6D5 thereby blocking 36P6D5 interaction with a bmding partner. Such dimenc fusion protems may be further combined mto multimenc protems usmg known antibody linking technologies. Inhibition of 36P6D5 Transcription or Translation Within another class of therapeutic approaches, the mvention provides various methods and compositions for inhibiting the transcription of the 36P6D5 gene Similarly, the mvention also provides methods and compositions for inhibiting the translation of 36P6D5 mRNA mto protem. In one approach, a method of mhibitmg the transcription of the 36P6D5 gene comprises contacting the 36P6D5 gene with a 36P6D5 antisense polynucleotide In another approach, a method of mhibitmg 36P6D5 mRNA translation compnses contacting the 36P6D5 mRNA with an antisense polynucleotide In another approach, a 36P6D5 specific ribozyme may be used to cleave the 36P6D5 message, thereby inhibiting translation. Such antisense and nbozyme based methods may also be directed to the regulatory regions of the 36P6D5 gene, such as the 36P6D5 start site, promoter and/or enhancer elements. SimUarly, proteins capable of inhibiting a 36P6D5 gene transcription factor may be used to inhibit 36P6D5 mRNA transcription. The various polynucleotides and compositions useful in the aforementioned methods have been described above. In anther approach, one can inhibit the translation of the 36P6D6 gene using morpholino antisense technology. The use of antisense and ribozyme molecules to inhibit transcription and translation is weU known in the art. Other factors that inhibit the transcription of 36P6D5 through interfering with 36P6D5 transcriptional activation may also be useful for the treatment of cancers expressing 36P6D5. Similarly, factors that are capable of interfering with 36P6D5 processing may be useful for the treatment of cancers expressing 36P6D5. Cancer treatment methods utilizing such factors are also within the scope of the invention. General Considerations for Therapeutic Strategies Gene transfer and gene therapy technologies may be used for delivering therapeutic polynucleotide molecules to tumor ceUs synthesizing 36P6D5 (ie, antisense, ribozyme, polynucleotides encoding intrabodies and other 36P6D5 inhibitory molecules). A number of gene therapy approaches are known in the art. Recombinant vectors encoding 36P6D5 antisense polynucleotides, ribozymes, factors capable of interfering with 36P6D5 transcription, and so forth, may be dehvered to target tumor ceUs using such gene therapy approaches. The above therapeutic approaches may be combined with any one of a wide variety of chemotherapy or radiation therapy regimens. These therapeutic approaches may also enable the use of reduced dosages of chemotherapy and/or less frequent administration, particularly in patients that do not tolerate the toxicity of the chemotherapeutic agent weU. The anti-tumor activity of a particular composition (e.g, antisense, ribozyme, intrabody), or a combination of such compositions, may be evaluated using various in vitro and in vivo assay systems. In vitro assays for evaluating therapeutic potential include ceU growth assays, soft agar assays and other assays indicative of tumor promoting activity, binding assays capable of dctemiining the extent to which a therapeutic composition wiU inhibit the binding of 36P6D5 to a binding partner, etc. In vivo, the effect of a 36P6D5 therapeutic composition may be evaluated in a suitable animal model. For example, xenogenic prostate cancer models wherein human prostate cancer explants or passaged xenograft tissues are mtroduced mto immune compromised animals, such as nude or SCID mice, are appropnate m relation to prostate cancer and have been descnbed (Klein et al, 1997, Nature Medicine 3:402-408). For example, PCT Patent Application WO98/16628, Sawyers et al, pubhshed April 23, 1998, descnbes vanous xenograft models of human prostate cancer capable of recapitulating the development of primary tumors, micrometastasis, and the formation of osteoblastic metastases characteristic of late stage disease Efficacy may be predicted usmg assays that measure inhibition of tumor formation, tumor regression or metastasis, and the like. See, also, the Examples below In vivo assays that qualify the promotion of apoptosis may also be useful in evaluating potential therapeutic compositions. In one embodiment, xenografts from bearmg mice treated with the therapeutic composition may be examined for the presence of apoptotic foci and compared to untreated control xenograft-beaπng mice. The extent to which apoptotic foci are found m the tumors of the treated mice provides an indication of the therapeutic efficacy of the composition. The therapeutic compositions used m the practice of the foregoing methods may be formulated mto pharmaceutical compositions compnsmg a earner suitable for the desired delivery method. Suitable earners mclude any material that when combmed with the therapeutic composition retains the anti-tumor function of the therapeutic composition and is non-reactive with the patient's immune system. Examples mclude, but are not limited to, any of a number of standard pharmaceutical carriers such as sterile phosphate buffered saline solutions, bactenostatic water, and the like (see, generaUy, Remington's Pharmaceutical Sciences 16 th Ed , A. Osal, Ed, 1980). Therapeutic formulations may be solubihzed and administered via any route capable of dehvermg the therapeutic composition to the tumor site. PotentiaUy effective routes of administration include, but are not limited to, intravenous, parenteral, mtrapentoneal, intramuscular, lntratumor, intradermal, intraorgan, orthotopic, and the like. A preferred formulation for intravenous injection comprises the therapeutic composition m a solution of preserved bactenostatic water, stenle unpreserved water, and/or diluted in polyvmylchloride or polyethylene bags contammg 0.9% sterile Sochum Chloride for Injection, USP. Therapeutic protem preparations may be lyophthzed and stored as stenle powders, preferably under vacuum, and then reconstituted m bacteriostatic water containing, for example, benzyl alcohol preservative, or m sterile water prior to in j ection. Dosages and administration protocols for the treatment of cancers usmg the foregomg methods wdl vary with the method and the target cancer and wiU generaUy depend on a number of other factors appreciated in the art. CANCER VACCINES As noted above, the expression profile of 36P6D5 shows that it is highly expressed m advanced and metastasized prostate cancer. This expression pattern is reminiscent of the Cancer-Testis (CT) antigens or MAGEs, which are testis-specific genes that are up-regulated in melanomas and other cancers (Van den Eynde and Boon, Int J Chn Lab Res. 27:81-86, 1997). Due to their tissue-specific expression and high expression levels m cancer, the MAGEs are currendy bemg investigated as targets for cancer vaccmes (Durrant, Anticancer Drugs 8 727-733, 1997; Reynolds et al, Int J Cancer 72:972-976, 1997). The mvention further provides cancer vaccmes compnsmg a 36P6D5 protein or fragment thereof, as weU as DNA based vaccmes. In view of the expression of 36P6D5 cancer vaccmes are expected to be effective at specificaUy preventing and/or treating 36P6D5 expressmg cancers without creating non-specific effects on non-target tissues. The use of a tumor antigen m a vaccme for generating humoral and ceU-mediated immunity for use in anti-cancer therapy is weU known m the art and has been employed in prostate cancer usmg human PSMA and rodent PAP immunogens (Hodge et al, 1995, Int. J. Cancer 63:231-237; Fong et al , 1997, J. Immunol. 159:3113-3117) Such methods can be readily practiced by employmg a 36P6D5 protem, or fragment thereof, or a 36P6D5-encoding nucleic acid molecule and recombinant vectors capable of expressmg and appropriately presenting the 36P6D5 immunogen. An iUustrative example of a typical technique consists of a method of generating an immune response (e.g. a humoral response) in a mammal compnsmg the steps exposmg the mammal's immune system to an immunoreactive epitope (e.g an epitope of the 36P6D5 protein shown m SEQ ID NO: 2) so that the mammal generates an immune response that is specific for that epitope is generated (e.g. antibodies that specificaUy recognize that epitope). For example, viral gene delivery systems may be used to dehver a 36P6D5-encoding nucleic acid molecule. Various viral gene delivery systems that can be used in the practice of this aspect of the invention include, but are not limited to, vaccinia, fowlpox, canarypox, adenovirus, influenza, pohovirus, adeno-associated virus, lentivirus, and sindbus virus (Restifo, 1996, Curr. Opin. Immunol. 8:658-663). Non-viral delivery systems may also be employed by using naked DNA encoding a 36P6D5 protein or fragment thereof introduced into the patient (e.g, intramuscularly) to induce an anti-tumor response. In one embodiment, the full-length human 36P6D5 cDNA may be employed. In another embodiment, 36P6D5 nucleic acid molecules encoding specific cytotoxic T lymphocyte (CTL) epitopes may be employed. CTL epitopes can be determined using specific algorithms (e.g, Epimer, Brown University) to identify peptides within a 36P6D5 protein that are capable of optimaUy binding to specified HLA aUeles. Various ex vivo strategies may also be employed. One approach involves the use of dendritic ceUs to present 36P6D5 antigen to a patient's immune system. Dendritic ceUs express MHC class I and II, B7 co-stimulator, and IL-12, and are thus highly specialized antigen presenting ceUs. In prostate cancer, autologous dendritic ceUs pulsed with peptides of the prostate-specific membrane antigen (PSMA) are being used in a Phase I clinical trial to stimulate prostate cancer patients' immune systems (Tjoa et al, 1996, Prostate 28:65-69; Murphy et al, 1996, Prostate 29:371-380). Dendritic ceUs can be used to present 36P6D5 peptides to T ceUs in the context of MHC class I and II molecules. In one embodiment, autologous dendritic ceUs are pulsed with 36P6D5 peptides capable of binding to MHC molecules. In another embodiment, dendritic ceUs are pulsed with the complete 36P6D5 protein. Yet another embodiment involves engineering the overexpression of the 36P6D5 gene in dendritic ceUs using various implementing vectors known in the art, such as adenovirus (Arthur et al, 1997, Cancer Gene Ther. 4:17-25), retrovirus (Henderson et al, 1996, Cancer Res. 56:3763-3770), lentivirus, adeno- associated virus, DNA transfection (Ribas et al, 1997, Cancer Res. 57:2865-2869), and tumor-derived RNA transfection (Ashley et al, 1997, J. Exp. Med. 186:1177-1182). CeUs expressing 36P6D5 may also be engineered to express immune modulators, such as GM-CSF, and used as immunizing agents. Anti-idiotypic anti-36P6D5 antibodies can also be used in anti-cancer therapy as a vaccine for inducing an immune response to ceUs expressing a 36P6D5 protein. SpecificaUy, the generation of anti-idiotypic antibodies is weU known in the art and can reachly be adapted to generate anti-idiotypic anti-36P6D5 antibodies that mirnic an epitope on a 36P6D5 protein (see, for example, Wagner et al, 1997, Hybridoma 16: 33-40; Foon et al, 1995, J. Clin. Invest. 96:334-342; Herlyn et al, 1996, Cancer Immunol. Immunother. 43:65-76). Such an anti-idiotypic antibody can be used in cancer vaccine strategies. Genetic immunization methods may be employed to generate prophylactic or therapeutic humoral and ceUular immune responses directed against cancer ceUs expressing 36P6D5. Constructs comprising DNA encoding a 36P6D5 protem/immunogen and appropriate regulatory sequences may be injected direcdy into muscle or skin of an individual, such that the ceUs of the muscle or skin take-up the construct and express the encoded 36P6D5 protem/immunogen. Expression of the 36P6D5 protein immunogen results in the generation of prophylactic or therapeutic humoral and ceUular immunity against bone, colon, pancreatic prostate, kidney, bladder and ovarian cancers. Various prophylactic and therapeutic genetic immunization techniques known in the art may be used (for review, see information and references pubhshed at Internet address www.genweb . com) . DIAGNOSTIC COMPOSITIONS AND KITS For use in the diagnostic and therapeutic applications described or suggested above, kits are also provided by the invention. Such kits may comprise a carrier means being compartmentalized to receive in close confinement one or more container means such as vials, tubes, and the like, each of the container means comprising one of the separate elements to be used in the method. For example, one of the container means may comprise a probe that is or can be detectably labeled. Such probe may be an antibody or polynucleotide specific for a 36P6D5 protein or a 36P6D5 gene or message, respectively. Where the kit utilizes nucleic acid hybridization to detect the target nucleic acid, the kit may also have containers containing nucleotide(s) for amplification of the target nucleic acid sequence and/or a container comprising a reporter-means, such as a biotin-binding protein, such as avidin or streptavidin, bound to a reporter molecule, such as an enzymatic, florescent, or radioisotope label. The kit of the invention wiU typicaUy comprise the container described above and one or more other containers comprising materials desirable from a commercial and user standpomt, mcludmg buffers, diluents, filters, needles, syringes, and package mserts with mstructions for use. A label may be present on the on the contamer to mdicate that the composition is used for a specific therapy or non-therapeutic application, and may also mdicate directions for either in vivo or in vitro use, such as those descnbed above. Accordingly, the mvention also provides diagnostic compositions compnsmg 36P6D5-related molecules. Such molecules mclude the vanous 36P6D5 polynucleotides, primers, probes, protems, fragments, antibodies descnbed herem. The molecules mcluded m the diagnostic composition may optionaUy be labeled with a detectable marker. 36P6D5 diagnostic compositions may further compnse appropnate buffers, diluents, and other ingredients as desired EXAMPLES Various aspects of the mvention are further described and lUustrated by way of the several examples which foUow, none of which are mtended to limit the scope of the mvention. EXAMPLE 1: SSH-GENERATED ISOLATION OF cDNA FRAGMENT OF THE 36P6D5 GENE MATERIALS AND METHODS LAPC Xenografts: LAPC xenografts were obtained from Dr. Charles Sawyers (UCLA) and generated as described (EClein et al, 1997, Nature Med. 3: 402-408). Androgen dependent LAPC-4 xenografts (LAPC-4 AD) were grown subcutaneously m male SCID mice and were passaged as smaU tissue chunks in recipient males. LAPC-4 AD xenografts were grown mtratibiaUy as foUows. LAPC-4 AD xenograft tumor tissue grown subcutaneously was minced mto 1-2 mm 3 sections while the tissue was bathed in IX Iscoves medium, minced tissue was then centrifuged at 1.3K rpm for 4 minutes, the supernatant was resuspended m 10 ml ice cold IX Iscoves medium and centnfuged at 1.3K rpm for 4 minutes. The peUet was then resuspended m IX Iscoves with 1% pronase E and mcubated for 20 minutes at room temperature with mild rocking agitation foUowed by incubation on ice for 2-4 minutes. Filtrate was centrifuged at 1.3K rmp for 4 minutes, and the pronase was removed from the aspirated peUet by resuspendmg m 10 ml Iscoves and re-centrifuging. Clumps of ceUs were then plated in PrEGM medium and grown overnight. The ceUs were then harvested, filtered, washed 2X RPMI, and counted. Approximately 50,000 ceUs were mixed with and equal volume of ice-cold Matrigel on ice, and surgicaUy mjected mto the proximal tibial metaphyses of SCID mice via a 27 gauge needle. After 10-12 weeks, LAPC-4 tumors growmg in bone marrow were recovered. Cell Lines: Human ceU hnes (e.g., HeLa) were obtamed from the ATCC and were maintained in DMEM with 5% fetal calf serum. RNA Isolation: Tumor tissue and ceU lines were homogenized m Tnzol reagent (Life Technologies, Gibco BRL) usmg 10 ml/ g tissue or 10 ml/ 10 8 ceUs to isolate total RNA. Poly A RNA was purified from total RNA usmg Qiagen's Ohgotex mRNA Mini and Midi kits. Total and mRNA were quantified by spectrophotometric analysis (O.D. 260/280 nm) and analyzed by gel electrophoresis. Oligonucleotides : The foUowmg HPLC purified ohgonucleotides were used. DPNCDN (cDNA synthesis primer): 5'TTTTGATCAAGCTT 30 3' (SEQ ID NO: 3) Adaptor 1: 5'CTAATACGACTCACTATAGGGCTCGAGCGGCCGCCCGGGCAG3' (SEQ ID NO: 4) 3'GGCCCGTCCTAG5' (SEQ ID NO: 5) Adaptor 2: 5'GTAATACGACTCACTATAGGGCAGCGTGGTCGCGGCCGAG3' (SEQ ID NO: 6) 3'CGGCTCCTAG5' (SEQ ID NO: 7) PCR primer 1 : 5'CTAATACGACTCACTATAGGGC3' (SEQ ID NO: 8) Nested primer (NP)1: 5 CGAGCGGCCGCCCGGGCAGGA3' (SEQ ID NO: 9) Nested primer (NP)2: 5ΑGCGTGGTCGCGGCCGAGGA3' (SEQ ID NO: 10) Suppression Subtractive Hybridization: Suppression Subtractive Hybridization (SSH) was used to identify cDNAs corresponding to genes which may be differentiaUy expressed in prostate cancer. The SSH reaction utihzed cDNA from LAPC-4 AD xenografts growing in two different environments, namely the subcutaneous ("LAPC-4 AD SQ") and intratibial ("LAPC-4 AD IT") growth environments, wherein the LAPC-4 AD IT xenograft was used as the source of the "tester" cDNA, whUe the LAPC-4 AD SQ xenograft was used as the source of the "driver" cDNA. Double stranded cDNAs corresponding to tester and driver cDNAs were synthesized from 2 μg of poly(A) + RNA isolated from the relevant xenograft tissue, as described above, using CLONTECH's PCR-Select cDNA Subtraction Kit and 1 ng of oligonucleotide DPNCDN as primer. First- and second-strand synthesis were carried out as described in the Kit's user manual protocol (CLONTECH Protocol No. PTl 117- 1, Catalog No. Kl 804-1). The resulting cDNA was digested with Dpn II for 3 hrs. at 37°C. Digested cDNA was extracted with phenol/ chloroform (1:1) and ethanol precipitated. Driver cDNA was generated by combining Dpn II digested cDNA from the human ceU lines HeLa, 293, A431, Colo205, and mouse hver. Tester cDNA was generated by diluting 1 μl of Dpn II digested cDNA from the relevant xenograft source (see above) (400 ng) in 5 μl of water. The diluted cDNA (2 μl, 160 ng) was then hgated to 2 μl of Adaptor 1 and Adaptor 2 (10 μM), in separate ligation reactions, in a total volume of 10 μl at 16°C overnight, using 400 u of T4 DNA hgase (CLONTECH). Ligation was terminated with 1 μl of 0.2 M EDTA and heating at 72°C for 5 min. The first hybridization was performed by adding 1.5 μl (600 ng) of driver cDNA to each of two tubes containing 1.5 μl (20 ng) Adaptor 1- and Adaptor 2- hgated tester cDNA. In a final volume of 4 μl, the samples were overlaid with mineral oil, denatured in an MJ Research thermal cycler at 98°C for 1.5 minutes, and then were aUowed to hybridize for 8 hrs at 68°C. The two hybridizations were then mixed together with an additional 1 μl of fresh denatured driver cDNA and were aUowed to hybridize overnight at 68°C. The second hybridization was then diluted in 200 μl of 20 mM Hepes, pH 8.3, 50 mM NaCl, 0.2 mM EDTA, heated at 70°C for 7 min. and stored at -20°C. PCR Amplification. Cloning and Sequencing of Gene Fragments Generated from SSH: To amplify gene fragments resulting from SSH reactions, two PCR amplifications were performed. In the primary PCR reaction 1 μl of the diluted final hybridization mix was added to 1 μl of PCR primer 1 (10 μM), 0.5 μl dNTP mix (10 μM), 2.5 μl 10 x reaction buffer (CLONTECH) and 0.5 μl 50 x Advantage cDNA polymerase Mix (CLONTECH) in a final volume of 25 μl. PCR 1 was conducted using the foUowing conditions: 75°C for 5 min, 94°C for 25 sec, then 27 cycles of 94°C for 10 sec, 66°C for 30 sec, 72°C for 1.5 min. Five separate primary PCR reactions were performed for each experiment. The products were pooled and chluted 1:10 with water. For the secondary PCR reaction, 1 μl from the pooled and chluted primary PCR reaction was added to the same reaction mix as used for PCR 1, except that primers NP1 and NP2 (10 μM) were used instead of PCR primer 1. PCR 2 was performed using 10-12 cycles of 94°C for 10 sec, 68°C for 30 sec, 72°C for 1.5 minutes. The PCR products were analyzed using 2% agarose gel electrophoresis. The PCR products were inserted into pCR2.1 using the T/A vector cloning kit (Invitrogen). Transformed E. coh were subjected to blue/white and ampicillin selection. White colonies were picked and arrayed into 96 weU plates and were grown in liquid culture overnight. To identify inserts, PCR amphfication was performed on 1 μl of bacterial culture using the conditions of PCR1 and NP1 and NP2 as primers. PCR products were analyzed using 2% agarose gel electrophoresis. Bacterial clones were stored in 20% glycerol in a 96 weU format. Plasmid DNA was prepared, sequenced, and subjected to nucleic acid homology searches of the GenBank, dBest, and NCI-CGAP databases. RT-PCR Expression Analysis: First strand cDNAs were generated from 1 μg of mRNA with ohgo (dT)12-18 priming using the Gibco-BRL Superscript Preamplification system. The manufacturers protocol was used and included an incubation for 50 min at 42°C with reverse transcriptase foUowed by RNAse H treatment at 37°C for 20 min. After completing the reaction, the volume was increased to 200 μl with water prior to normalization. First strand cDNAs from 16 different normal human tissues were obtained from Clontech. Normalization of the first strand cDNAs from multiple tissues was performed by using the primers 5'atatcgccgcgctcgtcgtcgacaa3' (SEQ ID NO: 11) and 5'agccacacgcagctcattgtagaagg 3' (SEQ ID NO: 12) to amplify β-actin. First strand cDNA (5 μl) was amplified in a total volume of 50 μl containing 0.4 μM primers, 0.2 μM each dNTPs, 1XPCR buffer (Clontech, 10 mM Tris-HCL, 1.5 mM MgCl 2 , 50 mM KC1, ρH8.3) and IX Klentaq DNA polymerase (Clontech). Five μl of the PCR reaction was removed at 18, 20, and 22 cycles and used for agarose gel electrophoresis. PCR was performed using an MJ Research thermal cycler under the foUowing conditions: initial denaturation was at 94°C for 15 sec, foUowed by a 18, 20, and 22 cycles of 94°C for 15, 65°C for 2 min, 72°C for 5 sec. A final extension at 72°C was carried out for 2 min. After agarose gel electrophoresis, the band intensities of the 283 bp β-actin bands from multiple tissues were compared by visual inspection. DUution factors for the first strand cDNAs were calculated to result in equal β-actin band intensities in aU tissues after 22 cycles of PCR. Three rounds of normalization were required to achieve equal band intensities in aU tissues after 22 cycles of PCR. To determine expression levels of the 36P6D5 gene, 5 μl of normalized first strand cDNA was analyzed by PCR using 25, 30, and 35 cycles of amphfication using the foUowing primer pairs: 36P6D5.1 GCATTCTTGGCATCGTTATTCAG (SEQ ID NO: 13) 36P6D5.2 TAACTGGGAATGTGACAGCAACAC (SEQ ID NO: 14) Semi quantitative expression analysis was achieved by comparmg the PCR products at cycle numbers that give hght band intensities. RESULTS: The SSH experiment described m the Materials and Methods, supra, led to the isolation of numerous candidate gene fragment clones (SSH clones). AU candidate clones were sequenced and subjected to homology analysis agamst aU sequences m the major pubhc gene and EST databases m order to provide information on the identity of the corresponding gene and to help guide the decision to analyze a particular gene for differential expression. In general, gene fragments which had no homology to any known sequence m any of the searched databases, and thus considered to represent novel genes, as weU as gene fragments showmg homology to previously sequenced expressed sequence tags (ESTs), were subjected to differential expression analysis by RT-PCR and/or Northern analysis. One of the SHH clones compnsmg about 423 bp, showed no homology to any known gene, and was designated 36P6D5. Initial expression analysis of 36P6D5 by RT- PCR showed highest expression m LAPC-4 AD (IT) and normal prostate compared to the other samples. This clone, therefore, was utihzed for obtaining a fuU length cDNA encoding 36P6D5 as described in Example 2, below. EXAMPLE 2 ISOLATION OF FULL LENGTH cDNA ENCODING THE 36P6D5 GENE The isolated 36P6D5 gene fragment of 423 bp was used as a probe to identify the full length cDNA for 36P6D5 in a human prostate cDNA library. This resulted m the isolation of a 931 bp cDNA, clone 36P6D5-GTC4, which encodes a 235 amino acid ORF with significant homology to two previously reported sequences, the 2-19 protem precursor (Genbank P98173) and a gene isolated from human osteoblasts termed GS3786 (Q92520) The nucleotide and deduced amino acid sequences of the clone 36P6D5-GTC4 cDNA are shown in FIG. 1. The encoded amino acid sequence exhibits an N-terminal signal sequence, which predicts the protein to be secreted (using the PSORT program). amino Acid sequence alignments of the 36P6D5 protein with 2-19 protein precursor and osteoblast protein GS3786 are shown in FIG. 2. EXAMPLE 3 NORTHERN BLOT ANALYSIS OF 36P6D5 GENE EXPRESSION 36P6D5 mRNA expression in normal human tissues was first analyzed by Northern blotting two multiple tissue blots obtained from Clontech (Palo Alto, California), comprising a total of 16 different normal human tissues, using labeled 36P6D5 cDNA as a probe. RNA samples were quantitatively normalized with a β— actin probe. The results are shown in FIG. 3 and indicate that, within the 16 tissues tested, the 36P6D5 gene is predominandy expressed in pancreas, with very low level expression also detected in prostate and smaU intestine. In addition, in order to analyze 36P6D5 expression in human cancer tissues and ceU lines, RNAs derived from LAPC-4 human prostate cancer xenografts and a panel of non-prostate cancer ceU lines were analyzed by Northern blot using the 36P6D5 cDNA as probe. AU RNA samples were quantitatively normahzed by ethidium bromide staining and subsequent analysis with a labeled β— actin probe. The results of this analysis are presented in FIG. 4, and show 36P6D5 expression in LAPC-4 prostate cancer xenografts growing subcutaneously and intratibiaUy, in aU cases at higher levels relative to normal prostate. AdditionaUy, significant expression was detected in several non-prostate cancer ceU lines including pancreatic (Capan-1), colon (CaCo-2, Colo-205), breast (CAMA-1, DU4475), and ovarian (SW626, CAOV-3, OV1063) cancer ceUs, also at high levels in some cases. In particular, the highest level of expression was detected in the breast cancer ceU line DU4475. EXAMPLE 4: PRODUCTION AND PURIFICATION OF RECOMBINANT 36P6D5 To express recombinant 36P6D5 for use in a number of contexts such as analyzing the subceUular localization of 36P6D5 protein, a partial or the full length cDNA can cloned into any one of a variety of expression vectors such as those that provide a 6His tag at the carboxyl-terminus (e.g. pCDNA 3.1 myc-his, InVitrogen). In a typical embodiment, in order to drive high level expression of 36P6D5 protein, the 36P6D5 cDNA encoding amino acids 30-235 (minus N-terminal signal sequence) was cloned into the pAPTag5 mammalian secretion vector (GenHuntcr) with and without fusion to the provided alkaline phosphatase (AP) cDNA sequence. This vector provides a C-terminal 6XHis and MYC tag for purification and detection and an N-terminal Ig leader sequence to drive secretion. 293T ceUs stably expressing either pAPTag5-36P6D5 or pTag5-36P6D5 (not fused to AP) serve as a source of recombinant protein for purification as visuahzed by an anti-His Western blot of conchtioned media from these ceU lines (FIG. 5). The HIS-tagged 36P6D5 proteins present in the conditioned media are purified using the foUowing method. Conditioned media is concentrated 5-10 fold and simultaneously buffer exchanged into a phosphate buffer (pH 8.0) containing 500 mM NaCl and 20 mM imidazole (buffer A) using an amicon ultrafiltration unit with a 10 kd MW cutoff membrane. The prep is batch bound to 0.1 to 0.5 ml of nickel metal affinity resin (Ni-NTA, Qiagen) and washed extensively with buffer A. The HIS-tagged SGP-28/CRISP-3 protein is then eluted with a 0 to 400 mM gradient of imidazole in phosphate buffer (pH 6.3) containing 300 mM NaCl and then dialyzed extensively against PBS. The purified protein may then be used for growth assays, hgand binding studies, or as immunogen for generating antibody reagents. Additional embodiments of typical constructs are provided below. pcDNA3.1 /MycHis Construct To express 36P6D5 in mammahan ceUs, the 705 bp (235 amino acid) 36P6D5 ORF was cloned into pcDNA3.1 /MycHis_Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter. The recombinant protein has the myc and six histidines fused to the C-terminus. The pcDNA3.1/MycHis vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability along with the SV40 origin for episomal replication and simple vector rescue in ceU lines expressing the large T antigen. The Neomycin resistance gene aUows for selection of mammalian ceUs expressing the protein and the ampicillin resistance gene and ColEl origin permits selection and maintenance of the plasmid in E. coh. pAPtag The 36P6D5 protein without the signal sequence (amino acids 30 to 235) was cloned into pAPtag-5 (GenHunter Corp. NashviUe, TN). This construct generates an alkaline phosphatase fusion at the C-terminus of the 36P6D5 protein whUe fusing the IgGK signal sequence to N-terminus. The resulting recombinant 36P6D5 protein is optimized for secretion into the media of transfected mammahan ceUs and can be used to identify proteins such as ligands or receptors that interact with the 36P6D5 protein. Protein expression is driven from the CMV promoter and the recombinant protein also contains myc and six histidines fused to the C-terminus of alkaline phosphatase. The Zeosin resistance gene aUows for selection of mammahan ceUs expressing the protein and the ampicillin resistance gene permits selection of the plasmid in E. coh. ptag5 The 36P6D5 protein without the signal sequence (amino acids 30 to 235) was also cloned into pTag-5. This vector is simUar to pAPTag but without the alkaline phosphatase fusion. pSRa Constructs To generate mammahan ceU lines expressing 36P6D5 constitutively, the 705 bp (235 amino acid) ORF was cloned into pSRa constructs. Amphotropic and ecotropic retroviruses are generated by transfection of pSRa constructs into the 293T-10A1 packaging line or co-trans fection of pSRa and a helper plasmid (φD ) in 293 ceUs, respectively. The retrovirus can be used to infect a variety of mammahan ceU lines, resulting in the integration of the cloned gene, 36P6D5, into the host ceU-lines. Protein expression is driven from a long terminal repeat (LTR). The Neomycin resistance gene aUows for selection of mammahan ceUs expressing the protein and the ampicillin resistance gene and ColEl origin permits selection and maintenance of the plasmid in E. coh. An additional pSRa construct was made that fused the FLAG tag to the C-terminus to aUow detection using anti-FLAG antibodies. The FLAG nucleotide sequence was added to cloning primer at the 3' end of the ORF. Additional pSRa constructs can be made to produce both N-terminal and C- terminal GFP and myc/6 HIS fusion protems of the fuU-length 36P6D5 protem. EXAMPLE 5: PRODUCTION OF RECOMBINANT 36P6D5 IN A BACULOVIRUS SYSTEM To generate recombmant 36P6D5 protem m a baculovirus expression system, 36P6D5 cDNA is cloned mto the baculovirus transfer vector pBlueBac 4.5 (Invitrogen) which provides a His-tag at the N-terminus. SpecificaUy, pBlueBac-36P6D5 is co- transfected with helper plasmid pBac-N-Blue (Invitrogen) mto SF9 (Spodoptera frugiperda) msect ceUs to generate recombinant baculovirus (see Invitrogen instruction manual for detads). Baculovirus is then coUected from ceU supernatant and purified by plaque assay. Recombinant 36P6D5 protem is then generated by infection of HighFive msect ceUs (InVitrogen) with the purified baculovirus. Recombinant 36P6D5 protem may be detected usmg 36P6D5-specιfic antibody. 36P6D5 protem may be purified and used m various ceU based assays or as immunogen to generate polyclonal and monoclonal antiboches specific for 36P6D5 EXAMPLE 6: GENERATION OF 36P6D5 POLYCLONAL ANTIBODIES To generate polyclonal sera to 36P6D5 a peptide was synthesized corresponding to ammo acids 163-177 (MVTYDDGSTRLNNDA) (SEQ ID NO: 12) of the SGP- 28/CRISP-3 protem sequence was coupled to Keyhole limpet hemacyanin (KLH) and was used to immunize a rabbit as foUows. The rabbit was lnitiaUy immunized with 200 ug of peptide-KLH mixed in complete Freund's adjuvant. The rabbit was then mjected every two weeks with 200 ug of peptide-KLH m mcomplete Freund's ad j uvant. Bleeds were taken approximately 7-10 days foUowmg each immunization. ELISA and Western blotting analyses were used to determine specificity and titer of the rabbit serum to the immunizing peptide and 36P6D5 protem respectively. Affinity purified 36P6D5 polyclonal antibodies were prepared by passage of crude serum from immunized rabbit over an affinity matrix comprised of 36P6D5 peptide (MVTYDDGSTRLNNDA) (ammo acids 163-177 of SEQ ID NO 2) covalendy coupled to Affigel 15 (BioRad). After extensive washing of the matrix with PBS, antibodies specific to 36P6D5 peptide were eluted with low pH glycme buffer (0 1M, pH 2.5), immediately neutralized, and extensively dialyzed agamst PBS. To test the rabbit polyclonal antibody for reactivity with 36P6D5 protem, Western blot analysis was carried out agamst conchtioned media of 293T ceUs transfected with the pAPTag5-36P6D5 or PTag5-36P6D5 expression vectors. Affinity purified rabbit anti-36P6D5 pAb (1 μg/ml) recognizes both forms of recombmant 36P6D5 protem secreted from 293T ceUs (FIG. 5). EXAMPLE 7: GENERATION OF 36P6D5 MONOCLONAL ANTIBODIES In order to generate 36P6D5 monoclonal antiboches, purified 293T-expressed HIS-tagged 36P6D5 protem is used to immunize Balb/C mice. Balb C mice are lnitiaUy immunized intrapeπtoneaUy with 50 μg of 36P6D5 protem mixed m complete Freund's adjuvant. Mice are subsequendy immunized every 2 weeks with 50 μg of 36P6D5 protem mixed m Freund's incomplete adjuvant for a total of 3 immunizations. Reactivity of serum from immunized mice to fuU length 36P6D5 protein is momtored by ELISA usmg the immunogen and by Western blot usmg conchtioned media from ceUs expressmg 36P6D5 protem Mice showmg the strongest reactivity are rested for 3 weeks and given a final m j ection of fusion protem m PBS and then sacrificed 4 days later. The spleens of the sacrificed mice are then harvested and fused to SPO/2 myeloma ceUs or other suitable myeloma fusion partner usmg standard procedures (Harlow and Lane, 1988). Supernatants from growth weUs foUowmg HAT selection are screened by ELISA and Western blot to identify 36P6D5 specific antibody producing clones. The binding affinity of a 36P6D5 monoclonal antibody may be determined usmg standard technology. Affinity measurements quantify the strength of antibody to epitope bmding and may be used to help define which 36P6D5 monoclonal antibodies are preferred for diagnostic or therapeutic use The BIAcore system (Uppsala, Sweden) is a preferred method for determinmg bmdmg affinity. The BIAcore system uses surface plasmon resonance (SPR, Welford K 1991, Opt. Quant. Elect. 23:1; Morton and Myszka, 1998, Methods m Enzymology 295- 268) to momtor biomolecular interactions m real time. BIAcore analysis conveniendy generates association rate constants, dissociation rate constants, equilibrium dissociation constants, and affinity constants. In a specific lUustration of a typical method for generating 36P6D5 monoclonal antibodies, purified 293T-expressed HIS-tagged 36P6D5 protem was used to immunize 3 female Balb C mice Balb C mice were mitiaUy immunized lntraperitoneaUy (IP) with 50 μg of 36P6D5 protem mixed in Ribi adjuvant and boosted 2 additional times IP m 2 week intervals with 25 ug of 36P6D5 protem in Ribi adjuvant. FoUowmg the third boost, mice were subsequendy immunized with 25 ug of protem IP in PBS. ELISA analysis of test bleeds foUowing the fourth immunization indicated a titer of at least 2X10 6 for each of the immunized mice toward the immunogen. The serum from the immunized mice specificaUy recognize endogenous 36P6D5 protem m ceU lysates and conchtioned media from a variety of cancer ceU hnes mcludmg ceU hnes derived from prostate (LAPC4 xenograft), colon (Colo 205, CaCo-2), breast (DU4475), and pancreatic (Capan-1) cancers (Fig 9). In addition, purified polyclonal antibodies from the sera were used to develop a capture ELISA that specificaUy detects 36P6D5 protem in the supernatants of PC-3-36P6D5 and DU4475 ceU hnes and m clinical serum samples (Table 2). For generation of anti-36P6D5 hybridomas, mice are given a final boost of 25 ug of 36P6D5 IP, sacrificed 3 days later and harvested spleen ceUs are fused to myeloma partners usmg standard procedures (Harlow and Lane, 1988). Supernatants from fused hybridoma growth weUs are screened by ELISA and Western blot to identify 36P6D5 specific antibody producmg clones. Usmg these antibodies, 36P6D5 protem was detected m several cancer ceU hnes mcludmg those derived from colon, pancreas, and breast, and in prostate cancer xenografts (Figure 9). In addition, 36P6D5 protem was detected in conditioned medium of ceUs that express the protem endogenously, demonstrating that it is a secreted protein and that it may serve as a diagnostic serum marker. Indeed, usmg a sensitive capture ELISA (Figure 10), 36P6D5 protem was detected m 7/10 colon cancer samples and 6/10 pancreatic cancer samples, but only 1 /6 normal male samples (Table 2). These results provide evidence that 36P6D5 may serve as a diagnostic and possibly a therapeutic target for colon and pancreatic cancer as weU as other cancers mcludmg those denved from prostate and breast tissues. EXAMPLE 8: IDENTIFICATION OF POTENTIAL SIGNAL TRANSDUCTION PATHWAYS To determine whether 36P6D5 direcdy or indirecdy activates known signal transduction pathways in ceUs, luciferase due) based transcriptional reporter assays are carried out in ceUs expressing 36P6D5. These transcriptional reporters contain consensus binding sites for known transcription factors which he downstream of weU characterized signal transduction pathways. The reporters and examples of there associated transcription factors, signal transduction pathways, and activation stimuli are listed below. 1. NFkB-luc, NFkB/Rel; Ik-kinase/SAPK; growth/apoptosis/stress 2. SRE-luc, SRF/TCF/ELK1; MAPK/SAPK; growth/differentiation 3. AP-l-luc, FOS/JUN; MAPK/SAPK/PKC; growth/apoptosis/stress 4. ARE-luc, androgen receptor; steroids/MAPK; growth/differentiation/apoptosis 5. p53-luc, p53; SAPK; growth/differentiation/apoptosis 6. CRE-luc, CREB/ATF2; PKA/p38; growth/apoptosis/stress 36P6D5-mediated effects may be assayed in ceUs showing mRNA expression, such as the 36P6D5-expressing cancer ceU lines shown in FIG. 4. Luciferase reporter plasmids may be introduced by lipid mediated transfection (TFX-50, Promega). Luciferase activity, an indicator of relative transcriptional activity, is measured by incubation of ceUs extracts with luciferin substrate and luminescence of the reaction is monitored in a luminometer. EXAMPLE 9: IN VITRO ASSAYS OF 36P6D5 FUNCTION The expression profile of 36P6D5 in cancer suggests a functional role in tumor initiation, progression and/or maintenance. 36P6D5 may function as a secreted factor that stimulates the prohferation of prostate cancer ceUs in bone. 36P6D5 function can be assessed in mammahan ceUs using in vitro approaches. For mammalian expression, 36P6D5 can be cloned into a number of appropriate vectors, including pcDNA 3.1 myc- His-tag and the retroviral vector pSRαtkneo (MuUer et al , 1991, MCB 11:1785). Usmg such expression vectors, 36P6D5 can be expressed m several cancer ceU hnes, mcludmg for example PC-3, NIH 3T3, LNCaP and 293T Expression of 36P6D5 can be momtored usmg anti-36P6D5 antiboches. Mammahan ceU hnes expressmg 36P6D5 can be tested in several in vitro and m vivo assays, mcludmg ceU prohferation m tissue culture, activation of apoptotic signals, primary and metastatic tumor formation m SCID mice, and in vitro mvasion usmg a membrane invasion culture system (MICS) (Welch et al. Int. J. Cancer 43: 449-457). 36P6D5 ceU phenotype is compared to the phenotype of ceUs that lack expression of 36P6D5. CeU hnes expressmg 36P6D5 can also be assayed for alteration of invasive and migratory properties by measuring passage of ceUs through a matngel coated porous membrane chamber (Becton Dickinson). Passage of ceUs through the membrane to the opposite side is momtored usmg a fluorescent assay (Becton Dickinson Technical Bulletin #428) usmg calcein-Am (Molecular Probes) loaded indicator ceUs. CeU hnes analyzed include parental and 36P6D5 overexpressmg PC3, 3T3 and LNCaP ceUs. To assay whether 36P6D5 has chemoattractant properties, parental indicator ceUs are monitored for passage through the porous membrane toward a gradient of 36P6D5 conditioned media compared to control media. This assay may also be used to qualify and quantify specific neutralization of the 36P6D5 mduced effect by candidate cancer therapeutic compositions. CeUs can also be momtored for changes in growth, adhesiveness, and mvasiveness m the presence and absence of exogenously added purified 36P6D5 protem. In another functional assay, ceUs stably expressmg 36P6D5 can be analyzed for their abihty to form colonies m soft agar. In these experiments, ceUs used m such procedures (e.g. NIH-3T3 ceUs), can be transfected to stably express 36P6D5 or neo or activated-Ras (as the test gene, the negative and the positive controls, respectively) m order to assess the transforming capabilities of 36P6D5. TypicaUy experiments are performed in duphcate and the assays are evaluated approximately 4 weeks after ceU plating. Where experimental observations demonstrate that 36P6D5 mduces an increase m colony formation relative to a negative control (e g neo) such results mdicate that 36P6D5 has significant transforming capabilities. In another functional assay, parental ceUs and ceUs expressing 36P6D5 can be compared for their abihty to induce cytoplasmic accumulation of cAMP. In a typical embodiment, ceUs such as an LAPC xenograft (or any of a variety of other ceUs such as 293T ceUs) can be exposed to 36P6D5 and/or transfected with empty pcDNA4 HIS MAX vector or with pcDNA4 HIS MAX 36P6D5. TypicaUy, ceUs are starved in 1% fetal bovine serum (FBS) overnight and incubated with media alone or in the presence of a secretory molecule or 10% FBS. The ceUs are then lysed and analyzed for cAMP content by enzyme linked im unoassay (EIA) according to the manufacturer's recommendations (Linco Research, St Charles, MI). Many genes identified as playing a role in oncogenesis function by activating the cAMP signaling pathway. TypicaUy, in the absence of hgand, signaling molecules are normaUy in an inactive state. Upon hgand binding or overexpression, such molecules acquire an active conformation and complex with G proteins. This interaction results in the dissociation of G protein subunits and the activation of adenylate cyclase, resulting in cAMP accumulation (Birnbaumer L, CeU 1992, 71:1069). Enhanced production of cAMP results in the activation of several downstream signaling pathways that mediate the effect of such molecules. A demonstration that ceUs contacted by or transfected with 36P6D5 leads to the accumulation of cAMP in response to FBS would indicate that 36P6D5 functions as a signaling molecule under these conditions. EXAMPLE 10: IN VIVO ASSAY FOR 36P6D5 TUMOR GROWTH PROMOTION The effect of the 36P6D5 protein on tumor ceU growth may be evaluated in vivo by gene overexpression in tumor-bearing mice. For example, SCID mice can be injected SQ on each flank with 1 x 10 ' of a number of prostate, breast, colon, pancreatic, and ovarian ceU lines containing tkNeo empty vector or 36P6D5. At least two strategies may be used: (1) Constitutive 36P6D5 expression under regulation of an LTR promoter, and (2) Regulated expression under control of an inducible vector system, such as ecdysone, tet, etc. Tumor volume is then monitored at the appearance of palpable tumors and foUowed over time to determine if 36P6D5 expressing ceUs grow at a faster rate. AdditionaUy, mice may be implanted with 1 x 10 5 of the same ceUs orthotopicaUy to determine if 36P6D5 has an effect on local growth in the target tissue (i.e, prostate) or on the abihty of the ceUs to metastasize, specificaUy to lungs, lymph nodes, hver, bone marrow, etc. In relation to prostate cancer, the effect of 36P6D5 on bone tumor formation and growth may be assessed by injecting prostate tumor ceUs mtratibiaUy, as described in Example 1. These assays are also useful to determine the 36P6D5 inhibitory effect of candidate therapeutic compositions, such as for example, 36P6D5 antiboches, 36P6D5 antisense molecules and ribozymes. EXAMPLE 11: IN VITRO ASSAY OF 36P6D5 PROTEIN INTERACTION CeU hnes expressmg 36P6D5 can also be used to identify protem-protem interactions mediated by 36P6D5. The observation that 36P6D5 is a secreted molecule that bmds to ceUs (see e.g Figure 8) provides evidence that this molecule mteracts with other proteins on the ceU surface. This interaction can be examined using lmmunopreαpitation techniques as shown by others (Hamilton BJ, et al. Biochem Biophys. Res. Commun. 1999, 261.646-51) 36P6D5 protem can be immunoprecipitated from 36P6D5 expressing prostate cancer ceU hnes and examined for protem association by western blotting. Protem interaction may be also studied by a two yeast hybnd system, as described by Shnyreva et. Al. (Shnyreva M et al, J Biol Chem. 2000. 19;275 ;15498-503). These assays may also be used to analyze the effect of potential cancer therapeutics on 36P6D5 function. To determine the contribution of the various domains contamed within the 36P6D5 ORF to 36P6D5 function, 36P6D5 mutants can be generated lacking one or more domams. CeU hnes expressmg mutant 36P6D5 protem wiU be evaluated for alteration in prohferation, invasion, migration, transcriptional activation and protem- protem interaction. EXAMPLE 12: CHROMOSOMAL LOCALIZATION OF 36P6D5 The chromosomal localization of 36P6D5 was determined usmg the GeneBndge4 radiation hybrid panel (Walter et al , 1994, Nat. Genetics 7:22) (Research Genetics, HuntsviUe Al) The foUowmg PCR pnmers were used to localize 36P6D5: 36P6D5.7 ATACCCAAAGAACGAAGCTGACAC (SEQ ID NO: 17) 36P6D5.8 TACTCATCAAATATGGGCTGTTGG (SEQ ID NO: 18) The resulting mappmg vector for the 93 radiation hybrid panel DNAs was: 000101110110100100100110110011111111010111111110111110100000010111011001 110001101110001001011 This the mappmg program which can be found at mternet address http://www- genome.wi.mit.edu/cgi-bm/contig/rhmapper.pl maps 36P6D5 to chromosome 21q22.2- 22.3. EXAMPLE 13: DETECTING EXPRESSION OF 36P6D5 PROTEINS IN HUMAN CANCERS As shown in Figure 9, a subset of cancer ceUs express and secrete 36P6D5 protem. Conditioned media and/or ceU lysates from a variety of cancer ceU hnes representing cancers derived from prostate (LAPC4 xenograft), colon (Colo 205, CaCo- 1), breast (Du4475), and pancreatic (Caρan-1) tissues, as weU as PC3 prostate cancer ceUs engineered to overexpress 36P6D5 protein, were subjected to Western analysis using an anti-36P6D5 murme pAb. Briefly, ceUs (~25 ug total protem) and conditioned media (25 ul of neat, 0 22 uM filtered media) were solubihzed m SDS-PAGE sample buffer and separated on a 10-20% SDS-PAGE gel and transferred to nitroceUulose. Blots were blocked m Tris-buffered saline (TBS) + 3% non-fat milk and then probed with a 1:1,000 dilution (m TBS + 0.15% Tween-20 + 1% milk) of serum derived from mice immunized with purified 36P6D5 protem Blots were then washed and mcubated with a 1:4,000 dilution of anti-mouse IgG-HRP conjugated secondary antibody. FoUowmg washing, anti-36P6D5 immunoreactive bands were developed and visuahzed by enhanced chereuluminescence and exposure to autoradiographic film. The specific anti-36P6D5 immunoreactive bands representing endogenous 36P6D5 protem are indicated with arrows and run approximately between 35 and 40 kD. The molecular weight of 36P6D5 calculated from the ammo acid sequence is 26 kD suggesting that endogenous 36P6D5 protem is post-translationaUy modified, possibly by glycosylation. These results demonstrate that 36P6D5 may be useful as a diagnostic and therapeutic target for prostate, colon, breast, pancreatic and potentiaUy other human cancers. As shown in Figure 10, a sensitive and specific capture ELISA detects 36P6D5 protem m supernatants of human cancer ceU hnes. A capture ELISA was developed usmg protem G purified murine anti-36P6D5 pAb as capture Ab and a biounylated form of the same pAb as detection Ab Briefly, 1 ug of purified murine anti-36P6D5 pAb was used to coat weUs of an ELISA plate. FoUowmg blocking with PBS contammg 3% milk, 50 ul of conditioned media from either PC3-neo, PC3-36P6D5, or DU4475 ceUs or various amounts of purified Tag5-36P6D5 protem spiked mto tissue culture media were added to weUs and mcubated for 2 hours at room temperature. WeUs were washed 4X with PBS+0.05% Tween-20 (PBS-T) and lx with PBS. WeUs were then mcubated for 1 hour with 3 ug/ml of biotinylated antι-36O6D5 pAb in PBS-T+1% milk (TBS-TM, 50 ul/weU) and washed as above. WeUs were then mcubated with 50 ul of a 1:8,000 dilution of avidin-HRP complex (Neutrahte IM , Southern Biotechnology, Inc) m TBS-TM for 1 hour. FoUowing washing, weUs were then developed by addition of 200 ul of TMB substrate The reaction was stopped by the addition of 50 ul of IM H2SO4 and optical densities of weUs were read at 450 nM. Shown is the standard curve generated usmg the Tag5-36P6D5 protem and specific detection and quantitation of 36P6D5 present m supernatants derived from PC-3 ceUs overexpressmg 36P6D5 and endogenous 36P6D5 protem secreted by Du4475 breast cancer ceUs. Figure 11 also shows 36P6D5 expression m human cancers As shown m Figure 11, m a typical method for detecting expression of 36P6D5 m human cancers, ceU lysates from Colon, breast and kidney cancer tissues (Ca), as weU as their normal matched adjacent tissues (N) were subjected to Western analysis using an anti-36P6D5 mouse monoclonal antibody. Briefly, tissues (~25 ug total protem) were solubihzed m SDS- PAGE sample buffer and separated on a 10-20% SDS-PAGE gel and transferred to nitroceUulose. Blots were blocked m Tris-buffered sahne (TBS) + 3% non-fat milk and then probed with 2μg/ml (m TBS + 0 15% Tween-20 + 1% milk) of purified anti- 36P6D5 antibody. Blots were then washed and mcubated with a 1-4,000 dilution of anti- mouse IgG-HRP conjugated secondary antibody FoUowing washing, anti-36P6D5 immunoreactive bands were developed and visualized by enhanced chemilummescence and exposure to autorachographic film. The specific anti-36P6D5 immunoreactive bands represent a monomeric form of the 36P6D5 protem, which runs approximately between 35 and 40 kD, and multimeric forms of the protem, which run approximately at 90 and 120 kD. These results demonstrate that 36P6D5 may be useful as a diagnostic and therapeutic target for colon, breast, kidney and potentiaUy other human cancers. Throughout this application, various publications are referenced within parentheses. The disclosures of these publications are hereby incorporated by reference herem m their entireties. The present mvention is not to be limited m scope by the embodiments disclosed herem, which are mtended as smgle lUustrations of mdividual aspects of the invention, and any which are functionaUy equivalent are within the scope of the mvention. Various mochfications to the models and methods of the mvention, in adchtion to those descnbed herem, will become apparent to those skiUed m the art from the foregoing descnption and teachings, and are similarly mtended to faU within the scope of the invention. Such mochfications or other embodiments can be practiced without departing from the true scope and spirit of the invention. TABLES TABLE 1- predicted bmdmg of peptides from 36P6D5 protems to the human MHC class I molecule HLA-A2 Table 2: 36P6D5 is detected in serum samples derived from cancer patients. 36P6D5 36P6D5 36P6D5 Sample (ng/ml) Sample (ng/ml) Sample (ng/ml) normal (M) ND colon ND pancreatic 0.15 normal (M) ND colon 3.08 pancreatic 0.38 normal (M) ND colon 0.31 pancreatic 29.70 normal (M) ND colon ND pancreatic ND normal (M) colon 0.92 pancreatic 1.38 1.31 colon 0.77 pancreatic 0.23 normal (M) ND colon 0.62 pancreatic ND (1/6) colon 1.23 pancreatic ND colon 0.46 pancreatic 0.38 PC3-neo ND colon ND pancreatic ND PC-3-36P6D5 3.38 (7/10) (6/10) Du4475 0.92 Clinical serum samples from and pancreatic cancer patients, and normal male donors were screened for 36P6D5 protein using a capture ELISA as described in Figure 10. Supernatants from PC-3-36P6D5 and Du4475 ceUs, and from PC-3-neo ceUs, served as positive and negative controls, respectively for 36P6D5 protein detection. ND: not detected or below detection sensitivity. 36P6D5 protein was detected in 7/10 colon cancer patients and 6/10 pancreatic cancer patients, one of which had relatively high levels (29.70 ng/ml), but only in 1 /6 normal male donors.

Claims: CLAIMS: 1. A method of detecting the presence of a cancer expressing 36P6D5 protein that comprises determining the level of 36P6D5 protein expressed by ceUs in a test tissue sample from an individual and comparing the level so determined to the level of 36P6D5 expressed in a corresponding normal sample, the presence of elevated 36P6D5 protein in the test sample relative to the normal sample providing an indication of the presence of such cancer in the individual. 2. The method of claim 1, wherein determining the level of 36P6D5 protein expressed by the ceUs comprises contacting the ceUs with an antibody that specificaUy binds 36P6D5 protein. 3. The method of claim 2, wherein the antibody comprises a polyclonal antibody. 4. The method of claim 2, wherein the antibody comprises a monoclonal antibody. 5. A method of monitoring 36P6D5 gene products comprising deterrriining the status of 36P6D5 gene products expressed by ceUs in a test tissue sample from an individual and comparing the status so determined to the status of 36P6D5 gene products in a corresponding normal sample, the presence of altered status of 36P6D5 gene products in the test sample relative to the normal sample providing an indication of dysregulated ceU growth within the individual. 6. A method of exaniining a biological sample for evidence of dysregulated ceUular growth comprising comparing the status of 36P6D5 in the biological sample to the status of 36P6D5 in a corresponding normal sample, wherein alterations in the status of 36P6D5 in the biological sample are associated with dysregulated ceUular growth. 7. The method of claim 6, wherein the status of 36P6D5 in the biological sample is evaluated by exaniining levels of 36P6D5 mRNA expression or levels of 36P6D5 protein expression. 8. The method of claim 6, wherein an alteration in the status of 36P6D5 is identified by the presence of 36P6D5 expressing ceUs in a biological sample from a tissue in which 36P6D5 expressing ceUs are normaUy absent. 9. A method of diagnosing the presence of cancer in an individual comprising: (a) determining the level of 36P6D5 mRNA expressed in a test sample obtained from the individual; and (b) comparing the level so determined to the level of 36P6D5 mRNA expressed in a comparable known normal tissue sample, the presence of elevated 36P6D5 mRNA expression in the test sample relative to the normal tissue sample providing an indication of the presence of cancer. 10. A method of diagnosing the presence of cancer in an individual comprising: (a) deterinining the level of 36P6D5 protein expressed in a test sample obtained from the individual; and (b) comparing the level so determined to the level of 36P6D5 protein expressed in a comparable known normal tissue sample, the presence of elevated 36P6D5 protein in the test sample relative to the normal tissue sample providing an indication of the presence of cancer. 11. The method of claim 10, wherein the cancer is prostate or colon cancer, and the test and normal tissue samples are selected from the group consisting of prostate tissue, colon tissue, lymphatic tissue, serum, blood or semen. 12. The method of claim 10, wherein determining the level of 36P6D5 protein expressed in the test sample comprises contacting the sample with an antibody that specificaUy binds 36P6D5 protein. 13. The method of claim 12, wherein the antibody comprises a polyclonal antibody. 14. The method of claim 12, wherein the antibody comprises a monoclonal antibody. 15. A method of treating a patient with a cancer that expresses 36P6D5 which comprises administering to said patient a vector encoding a single chain monoclonal antibody that comprises the variable domains of the heavy and hght chains of a monoclonal antibody that specificaUy binds to a 36P6D5 protein, such that the vector dehvers the single chain monoclonal antibody coding sequence to the cancer ceUs and the encoded single chain antibody is expressed intraceUularly therein. 16. A pharmaceutical composition comprising a polynucleotide that encodes a 36P6D5 polypeptide, wherein the polynucleotide is selected from the group consisting of: (a) a polynucleotide having the sequence as shown in SEQ ID NO: 1, wherein T can also be U; (b) a polynucleotide having the sequence as shown in SEQ ID NO: 1, from about nucleotide residue number 59 through about nucleotide residue number 763, wherein T can also be U; (c) a polynucleotide encoding a 36P6D5 protein having the amino acid sequence shown in SEQ ID NO: 2: (d) a polynucleotide that is a fragment of the polynucleotide of (a), (b) or (c) that is at least 20 nucleotide bases in length; (e) a polynucleotide that is fully complementary to a polynucleotide of any one of (a)-(d); or (f) a polynucleotide that selectively hybridizes under stringent conditions to the polynucleotide of any one of (a)-(d). 17. A pharmaceutical composition comprising a polynucleotide that encodes a polypeptide that is at least 90% identical to the amino acid sequence shown in SEQ ID NO: 2 over its entire length. 18. A pharmaceutical composition compnsmg a polynucleotide that encodes a 36P6D5 polypeptide, wherem the polypeptide mcludes an ammo acid sequence selected from the group consisting of NVTA at residues 120-123 of SEQ ID NO. 2, NHSD at residues 208-211 of SEQ ID NO: 2, SIR at residues 43-45 of SEQ ID NO- 2, STR at residues 160-162 of SEQ ID NO: 2, SIGE at residues 46-49 of SEQ ID NO 2, TYDD at residues 155-158 of SEQ ID NO 2, GGGRSK at residues 81-86 of SEQ ID NO. 2, GINIAI at residues 108-113 of SEQ ID NO: 2, GNVTAT at residues 119-124 of SEQ ID NO. 2, AGGLLKWFWFASLCAWYSGYLLAELIPDAP at residues 5-36 of SEQ ID NO: 2, GLLKWFW (SEQ ID NO: 19), LMGEQLGNV (SEQ ID NO. 20), LLAELIPDA (SEQ ID NO: 21), WVFIAAKGL (SEQ ID NO: 22), WFWFASL (SEQ ID NO: 23), GGLLKWFV (SEQ ID NO: 24), FIAAKGLEL (SEQ ID NO: 25), KICFEDNLL (SEQ ID NO. 26), INIAIVNYV (SEQ ID NO: 27) and NMECFRSSWV (SEQ ID NO. 28). 19. A pharmaceutical composition of claim 16, wherem the polynucleotide is labeled with a detectable marker 20. A pharmaceutical composition compnsmg a 36P6D5 polypeptide encoded by the polynucleotide of claim 16. 21. A pharmaceutical composition compnsmg a polypeptide having at least 15 contiguous ammo acids of the polypeptide of claim 20. 22. A pharmaceutical composition compnsmg an antibody or fragment thereof that specificaUy bmds to the 36P6D5 polypeptide of claim 20 23 The pharmaceutical composition of claim 22, wherem the antibody or fragment thereof is monoclonal. 24. A pharmaceutical composition comprising a recombinant protem havmg the antigen binding region of a monoclonal antibody of claim 23. 25 The pharmaceutical composition of claim 22, wherem the antibody or fragment thereof is labeled with a detectable marker. 26. The pharmaceutical composition of claim 25, wherem the detectable marker is selected from the group consisting of a radioisotope, fluorescent compound, bioluminescent compound, chemilummescent compound, metal chelator or enzyme 27. The pharmaceutical composition of claim 22, wherem the antibody fragment comprises an Fab, F(ab')2, Fv or sFv fragment. 28. The pharmaceutical composition of claim 22, wherem the antibody or fragment thereof comprises a human antibody. 29. The pharmaceutical composition of claim 22, wherem the antibody or fragment thereof is con j ugated to a toxin or a therapeutic agent. 30 The pharmaceutical composition of claim 23, wherein the antibody comprises murine antigen binding region residues and human antibody residues. 31 A pharmaceutical composition compnsmg a smgle cham monoclonal antibody havmg the variable domains of the heavy and hght chains of a monoclonal antibody of claim 23. 32. A vaccme composition for the treatment of a cancer expressmg 36P6D5 comprising an immunogenic portion of a 36P6D5 protem and a physiologicaUy acceptable carrier. 33. The vaccme composition of claim 32, wherem the immunogenic portion of a 36P6D5 protem is selected from the group consisting of GLLKWFW (SEQ ID NO: 19), LMGEQLGNV (SEQ ID NO: 20), LLAELIPDA (SEQ ID NO: 21), WVFIAAKGL (SEQ ID NO: 22), WFWFASL (SEQ ID NO: 23), GGLLKWFV (SEQ ID NO: 24), FIAAKGLEL (SEQ ID NO- 25), KICFEDNLL (SEQ ID NO: 26), INIAIVNYV (SEQ ID NO: 27) and NMKFRSSWV (SEQ ID NO: 28) 34. A vaccme composition for the treatment of a cancer expressmg 36P6D5 compnsmg a polynucleotide encodmg an immunogenic portion of a 36P6D5 protem and a physiologicaUy acceptable carrier. 35. The vaccme composition of claim 34, wherem the immunogenic portion of a 36P6D5 protem is selected from the group consisting of GLLKWFW (SEQ ID NO. 19), LMGEQLGNV (SEQ ID NO: 20), LLAELIPDA (SEQ ID NO. 21), WVFIAAKGL (SEQ ID NO. 22), WFWFASL (SEQ ID NO: 23), GGLLKWFV (SEQ ID NO: 24), FIAAKGLEL (SEQ ID NO: 25), KICFEDNLL (SEQ ID NO: 26), INIAIVNYV (SEQ ID NO: 27) and NMKFRSSWV (SEQ ID NO: 28). 36. A vaccme composition for the treatment of a cancer expressmg 36P6D5 comprising polynucleotide encodmg a smgle cham monoclonal antibody that comprises the vanable domams of the heavy and hght cha s of a monoclonal antibody that specificaUy bmds to a 36P6D5 protem 37. A method of mhibitmg the development of a cancer expressmg 36P6D5 in a patient, compnsmg administermg to the patient an effective amount of the vaccme composition of claim 34. 38. A method of inhibiting the development of a cancer expressing 36P6D5 m a patient, comprising administermg to the patient an effective amount of the vaccme composition of claim 36.

Inventors: AFAR DANIEL E H, FARIS MARY, HUBERT RENE S, JAKOBOVITS AYA, MITCHELL STEVE CHAPPELL, RAITANO ARTHUR B, AFAR, DANIEL, E., H., FARIS, MARY, HUBERT, RENE, S., JAKOBOVITS, AYA, MITCHELL, STEVE, CHAPPELL, RAITANO, ARTHUR, B.
Applicants: UROGENESYS INC, UROGENESYS, INC.
Application year: 2000
Main classification: C12N15
IPC codes: A61K31, A61K35, A61K38, A61K39, A61K48, A61K51, A61P35, C07K14, C12N15, C12Q1, G01N33