| CatalogCode: | NB120-13494 |
| ProductName: | Hsp90 Antibody |
| Product Description: | Rat Monoclonal anti-Hsp90 (16F1) |
| Clone: | 16F1 |
| Clonality: | Monoclonal |
| Immunogen: | Human Hsp90 purified from therapeutic orchiectomy specimens. |
| Specificity: | This affinity purified antibody identifies purified bovine and human (alpha and beta) Hsp90 and will detect an ~90 kDa protein, corresponding to the apparent molecular mass of Hsp90 on SDS-PAGE immunoblots, in human, monkey, mouse, rat, hamster, guinea pig, rabbit, dog, bovine, sheep, pig, chicken, frog, plants (cotton, tomato), Drosophila, salmon, carp, rainbow trout, brook trout, beluga, mussel and scallop origins. This antibody only recognizes high molecular weight degradation fragments, suggesting an epitope which may be complex and easily destroyed by proteolysis. This antibody immunoprecipitates both free and complexed Hsp90 and also picks up both hsp90􀀁 and 􀀂 equally well (detects 100ng of each). This antibody is highly recommended over other Hsp90 antibodies for use with samples of fish origin. |
| CrossReactivity: | Cross-reacts with Human, Mouse, Rat, Frog, Cow, Carp, Chicken, Dog, Drosophilia melanogaster, Guinea pig, Hamster, Monkey, Pig, Plants (cotton), Rainbow trout, Salmon, Sheep, Brook trout, Beluga, Mussel and Scallop. Not yet tested in other species. |
| Packaging: | 0.1 mg protein G purified Rat ascites. |
| Localization: | Cytoplasmic |
| Control: | HeLa Cell Lysate (Heat Shocked) |
| Background: | The 90 kDa molecular chaperone family comprises several proteins including the 90 kDa heat shock protein, Hsp90 and the 94 kDa glucose-regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90􀀁 and hsp90􀀂 which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90􀀁 is 85% and 90% homologous to that of Hsp90 respectively (1). All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions which have been shown to contain independent chaperone sites with different substrate specificity (2,3). These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signalling and cell cycle control. In this context several key regulatory proteins such as steroid receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90 (4). It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways. Recent studies indicate that when Drosophilia Hsp90 buffering is compromised by temperature etc., cryptic variants are expressed and selection can lead to the continued expression of these traits, even if Hsp90 function is restored (5). |
| Storage: | Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze thaw cycles. |
| Purity: | protein G purified |
| Isotype: | IgG2a |
| Host_Name: | Rat |
| Buffer: | PBS with 50% Glycerol |
| ListPrice: | 325 |
| AppSummary: | IHC, IP, WB, ICC, EIA |
| SpeciesSummary: | Bv, Ca, Ch, Dr, Ha, Hu, Mu, Po, Mk, Rt, Rb, Gp, Sh |
| ALTnames: | anti-Heat Shock Protein 90 antibody |
| ProteinTarget: | Hsp90 |
| PackageSize: | 0.1 mg |
| GeneralRef: | 1. Nemoto, T. et al (1998) Biochem. J. 330: 989-995. 2. Scheibel, T., Buchner, J. (1997) in Guidebook to Chaperones, ed. Gething, M.J. (Oxford Univ. Press, Oxford), pp. 147-150 3. Scheibel, T., et al (1999) J. PNAS 96: 1297-1302. 4. Scheibel, T. et al (1998) J. Biochem. Pharmacol. 56: 675-682. 5. Rutherford, S. L. et al (1998) Nature 396: 336-342. 6. Lai, B-T., et al (1984) Molecular & Cellular Biol. 4: 2802-2810. 7. Holmberg, C. I., et al (1997) J. Biol. Chem. 272: 6792-6798. 8. Kondo, T., et al. (2000) J. Biol. Chem. 275: 8872-8879. 9. Gusarova, V., et al (2001) J Biol Chem 276(27): 24891-24900. 10. Cwiklinska, H., et al (2003) Int Immunol 15(2): 241-249. 11. Hayem, G., et al (1999) Ann Rheum Dis 58(5): 291-296. 12. Ricart, J., et al (1997) Biochem J 324(2): 635-643. 13. White, R.J., et al (2002) Dig Dis Sci 47(8): 1873-1885. 14. de Carcer, G.; et al (2001) EMBO J 20(11): 2878-2884. |
| NotesMain: | This antibody is highly recommended over other Hsp90 antibodies for use with samples of fish origin. |
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