CircuLex Human Clusterin/Apo-J ELISA Kit

  • Applications
    • ELISA
  • Code # CY-8099
  • Size 96 Assays
  • Price


Clusterin, also called apolipoprotein J, sulfated glycoprotein-2, and testosterone-repressed prostate message-2, is a highly conserved secreted heterodimeric glycoprotein constitutively expressed by diverse epithelial cells. Clusterin has been implicated in diverse physiological processes, including lipid transportation (1), complement inhibition (1), tissue remodeling (2), membrane recycling (3), clearance of cellular debris (4), regulation of apoptosis, membrane protection, and promotion of cell-cell interactions (5). Clusterin is induced in injured organs in various disease states, such as Alzheimer's disease, atherosclerosis, myocardial infarction, and multiple forms of acute and chronic renal disease (5, 6). Clusterin has been shown to associate with both normal in vitro aging, namely replicative senescence, as well as with stress induced premature senescence. In vivo, the protein is up-regulated in many severe physiological disturbances that relate to advanced aging, including accumulation in the artery wall during the development of atherosclerosis. In cancer, clusterin up-regulation has been described in renal cell carcinoma (7), breast carcinoma (8), ovarian cancer (9), anaplastic large cell lymphomas (10), desmoplastic melanoma (11), transitional cell carcinoma of the bladder (12), pancreatic cancer (13), and serous carcinoma and hepatocellular carcinoma (14). However, a number of tumor processes where clusterin is downregulated have also been described such as esophageal squamous cell carcinoma (15), testicular germ cell tumors (16) and prostate cancer (17). The structure of clusterin has not provided much insight into function. Mammalian clusterins are approximately 80-kDa heterodimers (18, 19) consisting of two 40-kDa chains joined by a unique five-disulfide-bond motif (20). The protein has limited homology to other proteins and lacks clear functional motifs (18). It does contain three putative amphipathic α-helical regions, which could allow it to interact with lipids and hydrophobic regions of other proteins (21).
  • Application:
  • Components:
    • Microplate
    • 10X Wash Buffer
    • Dilution Buffer
    • Human Clusterin/Apo-J Standard
    • HRP conjugated Detection Antibody
    • Substrate Reagent
    • Stop Solution
  • Description:

    This Kit is used for the quantitative measurement of human Clusterin/Apo-J in serum, plasma, cell culture supernatant and other biological media It can be used for 96 Assays.

  • Product Type:
    ELISA Kit
  • Research Area:
  • Short Description:

    CircuLex HumanClusterin/Apo-J ELISA Kit.

  • Size:
    96 Assays
  1. Jenne, D. E., and Tschopp, J. (1989) Molecular structure and functional characterization of a human complement cytolysis inhibitor found in blood and seminal plasma: identity to sulfated glycoprotein 2, a constituent of rat testis fluid. Proc. Natl. Acad. Sci. USA. 86, 7123 –7127
  2. Danik, M., Chabot, G., Mercier, C., Benabid, A. L., Chauvin, C., Quirion, R., and Suh, M. (1991) Human gliomas and epileptic foci express high levels of a mRNA related to rat testicular sulfated glycoprotein 2, a purported marker of cell death. Proc. Natl. Acad. Sci. USA. 88, 8577 –8581
  3. Palmer, D. J., and Christie, D. L. (1992) Identification of molecular aggregates containing glycoproteins III, J, K (carboxypeptidase H), and H (Kex2-related proteases) in the soluble and membrane fractions of adrenal medullary chromaffin granules. J. Biol. Chem. 267, 19806 –19812
  4. Bartl, M. M., Luckenbach, T., Bergner, O., Ullrich, O., and Koch-Brandt, C. (2001) Multiple receptors mediate apoJ-dependent clearance of cellular debris into nonprofessional phagocytes. Exp. Cell Res. 271, 130 –141
  5. Rosenberg, M. E., and J. Silkensen. 1995. Clusterin and the kidney. Exp. Nephrol. 3:9-14.
  6. Silkensen, J. R., G. B. Schwochau, and M. E. Rosenberg. 1994. The role of clusterin in tissue injury. Biochem. Cell Biol. 72:483-488
  7. Miyake, H., Gleave, M. E., Arakawa, S., Kamidono, S., and Hara, I. (2002) Introducing the clusterin gene into human renal cell carcinoma cells enhances their metastatic potential. J. Urol. 167, 2203–2208
  8. Redondo, M., Villar, E., Torres-Muñoz, J., Tellez, T., Morell, M., and Petito, C. K. (2000) Overexpression of clusterin in human breast carcinoma. Am. J. Pathol. 157, 393 –399
  9. Xie, D., Lau, S. H., Sham, J. S. T., Wu, Q. L., Fang, Y., Liang, L. Z., Che, L. H., Zeng, Y. X., and Guan, X. Y. (2005) Up-regulated expression of cytoplasmic clusterin in human ovarian carcinoma. Cancer 103, 277 –283
  10. Wellmann, A., Thieblemont, C., Pittaluga, S., Sakai, A., Jaffe, E. S., Siebert, P., and Raffeld, M. (2000) Detection of differentially expressed genes in lymphomas using cDNA arrays: identification of clusterin as a new diagnostic marker for anaplastic large-cell lymphomas. Blood 96, 398 –404
  11. Busam, K. J., Zhao, H., Coit, D. G., Kucukgol, D., Jungbluth, A. A., Nobrega, J., and Viale, A. (2005) Distinction of desmoplastic melanoma from non-desmoplastic melanoma by gene expression profiling. J. Investig. Dermatol. 124, 412 –418
  12. Miyake, H., Gleave, M., Kamidono, S., and Hara, I. (2002) Overexpression of clusterin in transitional cell carcinoma of the bladder is related to disease progression and recurrence. Urology 59, 150 –154
  13. Xie, M. J., Motoo, Y., Su, S. B., Mouri, H., Ohtsubo, K., Matsubara, F., and Sawabu, N. (2002) Expression of clusterin in human pancreatic cancer. Pancreas 25, 234 –238
  14. Kang, Y. K., Hong, S. W., Lee, H., and Kim, W. H. (2004) Overexpression of clusterin in human hepatocellular carcinoma. Hum. Pathol. 35, 1340 –1346
  15. Zhang, L. Y., Ying, W. T., Mao, Y. S., He, H. Z., Liu, Y., Wang, H. X., Liu, F., Wang, K., Zhang, D. C., Wang, Y., Wu, M., Qian, X. H., and Zhao, X. H. (2003) Loss of clusterin both in serum and tissue correlates with the tumorigenesis of esophageal squamous cell carcinoma via proteomics approaches. World J. Gastroenterol. 9, 650 –654
  16. Behrens, P., Jeske, W., Wernert, N., and Wellmann, A. (2001) Downregulation of clusterin expression in testicular germ cell tumours. Pathobiology 69, 19 –23
  17. Scaltriti, M., Brausi, M., Amorosi, A., Caporali, A., D’Arca, D., Astancolle, S., Corti, A., and Bettuzzi, S. (2004) Clusterin (SGP-2, ApoJ) expression is downregulated in low- and high-grade human prostate cancer. Int. J. Cancer 108, 23 –30
  18. Jenne, D. E., and J. Tschopp. 1989. Molecular structure and functional characterization of a human complement cytolysis inhibitor found in blood and seminal plasma: identity to sulfated glycoprotein 2, a constituent of rat testis fluid. Proc. Natl. Acad. Sci. USA 86:7123-7127
  19. Murphy, B. F., L. Kirszbaum, I. D. Walker, and A. J. F. d'Apice. 1988. SP-40,40 a newly identified normal human serum protein found in the SC5b-9 complex of complement and in the immune deposits in glomerulonephritis. J. Clin. Investig. 81:1858-1864
  20. Kirszbaum, L., S. E. Bozas, and I. D. Walker. 1992. SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges. FEBS Lett. 297:70-76
  21. Humphreys, D. T., J. A. Carver, S. B. Easterbrook-Smith, and M. R. Wilson. 1999. Clusterin has chaperone-like activity similar to that of small heat shock proteins. J. Biol. Chem. 274:6875-6881