| CatalogCode: | NB110-61641 |
| ProductName: | Hsp90 alpha Antibody |
| Product Description: | Mouse Monoclonal anti-Hsp90 alpha (Hyb-K41009) |
| Clone: | Hyb-K41009 |
| Clonality: | Monoclonal |
| Immunogen: | Recombinant human hsp90 alpha |
| Specificity: | Detects 90kD proteins corresponding to the molecular mass of hsp90alpha. |
| CrossReactivity: | Human (alpha-specific), rat. Not tested in other species. |
| Packaging: | 0.1 mg protein G purified Mouse ascites. |
| Background: | HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta; exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it's label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% ofcytosolic 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. (7-8). The number of proteins now know 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.5 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 immunoadsorption 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 (9). |
| Storage: | Aliquot and store at -20C. |
| Purity: | protein G purified |
| Isotype: | IgG2a |
| Host_Name: | Mouse |
| Buffer: | PBS, pH 7.2, 50% glycerol. |
| ListPrice: | 325 |
| AppSummary: | ELISA, IHC, WB |
| SpeciesSummary: | Hu, Rt |
| ALTnames: | anti-HSP 86 antibody; anti-Renal carcinoma antigen NY REN 38 antibody; anti-heat shock protein 90kDa alpha (cytosolic), class A member 2 antibody; anti-HSP90ALPHA antibody; anti-HSPC1 antibody; anti-HSPCA antibody; anti-HSPCAL3 antibody |
| PackageSize: | 0.1 mg |
| GeneralRef: | 1. Nemoto, T. et al. (1997) J.Biol Chem. 272, 26179-26187. 2. Minami, Y, et al. (1991), J.Biol Chem. 266, 10099-10103. 3. Arlander SJH, et al. (2003) J Biol Chem 278, 52572-52577. 4. Pearl H, et al. (2001) Adv Protein Chem 59,157-186. 5. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 6. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 7. Pratt W, Toft D. (1997) Endocr Rev 18,306-360. 8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217, 420-434. 9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91, 8324-8328. 10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5), 881-889. |
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