Product Details
| Alternative Name: | HSP84, Heat shock protein 90β |
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| Recommended Dilutions/Conditions: | Western Blot (100ng, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application. |
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| MW: | ~90kDa |
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| Source: | Produced in E. coli. |
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| UniProt ID: | P08238 |
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| Formulation: | Liquid. In 20mM TRIS, pH 7.5, containing 500mM sodium chloride, 5% glycerol, and 1mM DTT. |
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| Purity: | ≥85% (SDS-PAGE; Western blot) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Applications: | WB
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| Application Notes: | Western blot control. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | The 90 kDa molecular chaperone family includes 90 kDa heat shock protein HSP90 and 94 kDa glucose-regulated protein Grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible HSP90a and constitutive HSP90β isoforms that are encoded by separate genes. The amino acid sequences of human and yeast HSP90a 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 signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers. |
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| Regulatory Status: | RUO - Research Use Only |
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SDS-PAGE analysis: Lane 1: MW marker, Lane 2: 1µg, Lane 3: 2µg, Lane 4: 5µg HSP90b
Western Blot analysis: Lane 1: MWM, Lane 2: HSP90 beta recombinant protein probed with HSP90 beta, mAb.
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Product Literature References
1,4-Naphthoquinone activates the HSP90/HSF1 pathway through the S-arylation of HSP90 in A431 cells: Negative regulation of the redox signal transduction pathway by persulfides/polysulfides: Y. Abiko, et al.; Free Radic. Biol. Med.
104, 118 (2017),
Abstract;
Cadmium-Mediated Activation of the HSP90/HSF1 Pathway Regulated by Reactive Persulfides/Polysulfides: Y. Shinkai, et al.; Toxicol. Sci.
156, 412 (2017),
Abstract;
Full Text
The Capture of Cadmium by Reactive Polysulfides Attenuates Cadmium-Induced Adaptive Responses and Hepatotoxicity: M. Akiyama, et al.; Chem. Res. Toxicol.
30, 2209 (2017),
Abstract;
Discovery of novel oxazepine and diazepine carboxamides as two new classes of heat shock protein 90 inhibitors: T. Neubert, et al.; Bioorg. Med. Chem. Lett.
25, 1338 (2015),
Application(s): Fluorescence Assay,
Abstract;
Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94: H.J. Patel, et al.; J. Med. Chem.
58, 3922 (2015),
Abstract;
Full Text
Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series: T. Taldone, et al.; J. Med. Chem.
56, 6803 (2013),
Abstract;
Full Text
Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2: P.D. Patel, et al.; Nat. Chem. Biol.
9, 677 (2013),
Abstract;
Full Text
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