Description
Hsp90, a mammalian heat shock protein, is a molecular chaperone that helps to keep a target protein in a folding-competent state. It has been found in cell cytosol, nucleus, and endoplasmic reticulum of many different tissues. Hsp90 functions as a dimer. It has an ATP-binding site and low ATPase activity. Its chaperone activity is enhanced at high temperatures, and its function is sensitive to bivalent cation concentrations.
Recombinant human Hsp90 produced in E. coli is a single, non-glycosylated polypeptide containing 732 amino acids with a molecular weight of 86.8kDa. It is expressed with a 6X His-tag