HEAt shock protein 90 (Hsp90) is the inducible cytosolic isoform of Hsp90 that is encoded by HSP90AA in humans.1 Hsp90 is a multidomain protein that functions as a molecular chaperone to assist in folding and activation of nascent peptides, refolding unfolded or misfolded proteins, and preventing protein aggregation.2 C-terminal dimerization of Hsp90, coupled with ATPase molecular clamp activity induces a conformational change in the N-terminal nucleotide binding domain that facilitates substrate binding and initiates the chaperone cycle.3 Hsp90 interacts with many co-chaperones during its chaperone cycle including p23 and Sba1, which help recruit substrates to the Hsp90 complex, Hsp70 (Item Nos. 22739 | 23002), which loads nascent polypeptides onto the Hsp90 dimer, and the ATPase activator Aha1 that promotes ATP hydrolysis and substrate relEAse.4,5 Hsp90 is overexpressed in cancer cells and stabilizes client proteins that promote oncogenesis, including transcription factors, signaling proteins, and kinases.1,5 Hsp90 also decrEAses -synuclein fibril formation and toxicity as well as Q35 aggregation in in vitro models of Parkinson's and Huntington's disEAse, respectively, implying a role in neurodegenerative disEAse.6Technical InformationSynonymsHEAt Shock Protein 90Purity90% as estimated by SDS-PAGESourceActive N-terminal histidine-tagged human Hsp90 protein (full length) purified from E. coliAmino Acids2-732 (full length)MW87 kDaFormulation50 mM HEPES, pH 8, 150 mM sodium chloride, 1 mM DTT, 10% glycerolUniProt Accession P07900