| ADI-SPA-831-050 | 50 µg | 256.00 USD |  |
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| ADI-SPA-831-200 | 200 µg | 515.00 USD | |
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| Alternative Name: | Heat shock protein 90 |
| Clone: | 2D11B9 |
| Host: | Mouse |
| Isotype: | IgG1 |
| Immunogen: | Recombinant human Hsp90. |
| UniProt ID: | P07900 (HSP90α), P08238 (HSP90β) |
| Source: | Purified from ascites. |
| Species reactivity: | Human, Mouse, Rat Dog, Drosophila, Fish, Guinea pig, Hamster, Horse, Monkey, Porcine, Sheep |
| Applications: | WB |
| Recommended Dilutions/Conditions: | Western Blot (1µg/ml, colorimetric) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application. |
| Application Notes: | Detects a band of ~92kDa by Western blot. |
| Purity Detail: | Protein G affinity purified. |
| Formulation: | Liquid. In PBS containing 50% glycerol and 0.09% sodium azide. |
| Handling: | Avoid freeze/thaw cycles. |
| Shipping: | Blue Ice |
| Long Term Storage: | -20°C |
| Scientific Background: | The 90kDa molecular chaperone family includes 90kDa heat shock protein Hsp90 and 94kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells contain isoforms Hsp90α and Hsp90β, encoded by separate genes. The amino acid sequences of human and yeast Hsp90α are 85% and 90% homologous to those of Hsp90β, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 functions as part of the cell’s powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signalling and cell cycle control. In this context, researchers identified key regulatory proteins as substrates of Hsp90, including steroid receptors, cell cycle kinases involved in signal transduction, and p53. Hsp90 may act as a capacitor for morphological evolution by buffering widespread variation, potentially affecting morphogenic pathways. When temperature and other stress factors compromise Drosophilia Hsp90 buffering, cryptic variant expression occurs, and selection can lead to the continued expression of these traits, even after Hsp90 function is restored. |
| Regulatory Status: | RUO - Research Use Only |
HeLa (heat shocked) , (cell lysate) |
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| Human, WB | Print as PDF | ||||||
| ADI-LYC-HL101-F | 200 µg | 141.00 USD | |
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HeLa, (cell lysate) |
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| Human, WB | Print as PDF | ||||||
| ADI-LYC-HL100-F | 200 µg | 141.00 USD | |
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