Target: HSP90
Conjugate: PerCP
Product Type: Monoclonal
Clone Number: D7A
Immunogen: Full length protein HSP90 purified from chicken brain
Swiss-Prot: P11501
Purification: Protein G Purified
Storage Buffer: PBS pH7.2, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Concentration: 1 mg/ml
Specificity: Recognizes 90kDa. Can isolate complexes of HSP90, Src kinase and cec37.
Cellular Localization: Cytoplasm,Melanosome
Scientific Background: HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (4-7). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90- regulated proteins that have been discovered to date are involved in cell signaling (8-9). The number of proteins now known to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase(6). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immune-adsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (10). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.
References: 1. Schuh S. et al. (1985) J Biol Chem. 260 (26): 14292-14296.2. Lipsich L.A., Cutt J.R. and Brugge J.S. (1982) Mol. Cell Biol. 2(7): 875-880.3. Brugge J.S., Yonemoto W., and Darrow D. (1983) Mol. Cell. Biol. 3(1): 9-19.4. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.5. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186.6. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61.7. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133.8. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360.9. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.10. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
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