CycLex® Poly-Ubiquitinated Protein Enrichment Detection Kit

  • Target Ubiquitinated
  • Code # CY-7001
  • Size 20 Assays
  • Price
    $513.71
Specifications

Background

The ubiquitin-proteasome pathway is the principle pathway of proteolysis in eukaryotic cells and may contribute to controlling the intracellular levels of a variety of short-lived proteins (1-3), in addition to degrading abnormal proteins in the cytosol and nucleus. Protein substrates are marked with a poly-ubiquitin chain (4) and then degraded to peptides and free ubiquitin by a large multicatalytic complex, the proteasome, which exists within all eukaryotic cells (1-3). Numerous examples of regulatory proteins have been found to undergo ubiquitin-dependent proteolysis. Protein substrates of the ubiquitin-proteasome pathway include a number of cell regulatory molecules, such as cyclins, the Myc oncogene protein, and p53, and the regulated degradation of these molecules has been linked to the control of cell proliferation and cell cycle progression (5-7). By controlling the intracellular levels of such proteins, the activity of the ubiquitin-proteasome pathway might also be linked to apoptosis.
  • Components:
    • Poly-Ubiquitin Affinity Resin
    • 10X Poly-Ubiquitinated Protein Control
    • 10X Cell Extraction Buffer
    • 10X Anti-Poly-Ubiquitin Monoclonal Antibody
    • 10X HRP conjugated Anti-Mouse IgG
    • 10X Antibody Dilution Buffer
  • Description:

    The CycLex Research Product Poly-Ubiquitinated Protein Enrichment & Detection Kit is designed to enrich and detect total poly-ubiquitinated proteins in cell lysate. It can be used for 20 assays.

  • Product Type:
    Kit
  • Short Description:

    CycLex Poly-Ubiquitinated Protein Enrichment  Detection Kit.

  • Size:
    20 Assays
  • Storage Temperature:
    4°C
  • Target:
    Ubiquitinated
References
  1. Goldberg A. L., Stein R., Adams J. Chem. Biol., 2: 503-508, 1995.
  2. Coux O., Tanaka K., Goldberg A. L. Annu. Rev. Biochem., 65: 801-847, 1996.
  3. King R. W., Deshaies R. J., Peters J-M., Kirschner M. W. Science, 274: 1652-1659, 1996.
  4. Chau V., Tobias J. W., Bachmair A., Marriott D., Ecker D. J., Gonda D. K., Varshavsky A. Science, 243: 1576-1583, 1989.
  5. Hochstrasser, M. Curr. Opin. Cell Biol. 7: 215-223, 1995
  6. Ciechanover, A. Cell 79: 13-21, 1994
  7. Jentsch, S., and Schlenker, S. Cell 82: 881-884, 1995
  8. Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., and Goldberg, A. L. Cell 78: 761-771, 1994
  9. Jensen, T. J., Loo, M. A., Pind, S., Williams, D. B., Goldberg, A. L., and Riordan, J. R. Cell 83: 129-135, 1994
  10. Ward, C. L., Omura, S., and Kopito, R. R. Cell 83: 121-127, 1995
  11. Fenteany, G., Standaert, R. F., Lane, W. S., Choi, S., Corey, E. J., and Schreiber, S. L. Science 268: 726-731, 1995
  12. Ciechanover A. EMBO J. 17: 7151-60, 1998
  13. Chen, L. and Madura, K. Mol. Cell Biol. 22: 4902, 2002