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- Email: info@nsjbio.com
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Heat shock protein 90 is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. Inhibitors of it are investigated as anti-cancer drugs. Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species. HSP90 acts as a capacitor for morphologic evolution through epigenetic and genetic mechanisms. It is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including HER2/ERBB2, AKT, RAF1, BCR-ABL, and mutated p53. Although it is highly expressed in most cells, HSP90 inhibitors selectively kill cancer cells compared to normal cells, and the the inhibitor 17-allylaminogeldanamycin (17-AAG) exhibited antitumor activity in preclinical models.
The stated application concentrations are suggested starting points. Titration of the HSP90 alpha antibody may be required due to differences in protocols and secondary/substrate sensitivity.
Human partial recombinant protein (AA 2-365) was used as the immunogen for this HSP90 alpha antibody.
After reconstitution, the HSP90 alpha antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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