Hsp90alpha (human recombinant)

Heat shock protein 90 alpha (Hsp90alpha) is the inducible cytosolic isoform of Hsp90 that is encoded by HSP90AA in humans. 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. 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. Hsp90 interacts with many co-chaperones during its chaperone cycle including p23 and Sba1, which help recruit substrates to the Hsp90 complex, Hsp70 (Cay-22739, Cay-23002), which loads nascent polypeptides onto the Hsp90 dimer, and the ATPase activator Aha1 that promotes ATP hydrolysis and substrate release. Hsp90 is overexpressed in cancer cells and stabilizes client proteins that promote oncogenesis, including transcription factors, signaling proteins, and kinases. Hsp90 also decreases alpha-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.Synonyms: Heat Shock Protein 90alpha. Purity: >90% as estimated by SDS-PAGE. Source: Active N-terminal histidine-tagged human Hsp90alpha protein (full length) purified from E. coli. Amino Acids: 2-732 (full length). MW: 87 kDa. Formulation: (Request formulation change), 50 mM HEPES, pH 8, 150 mM sodium chloride, 1 mM DTT, 10% glycerol. UniProt Accession #: P07900.