Heat Shock Protein 90 (Hsp90), human recombinant protein

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Hsp90 (heat shock protein 90) is a molecular chaperone with a mass molecular of roughly 83.1 kDa. Hsp90 account for 1–2% of total protein in unstressed cells. Hsp90 is found in bacteria and all branches of eukarya, but it is apparently absent in archaea. Hsp90 assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. When cells are heated, the fraction of heat shock proteins increases to 4–6% of cellular proteins. Hsp90 also stabilizes a lot of proteins required for tumor growth, that is why Hsp90 inhibitors are investigated as anti-cancer drugs.