Description
Heat shock protein (HSP) 10 is a member of the highly conserved group of molecular chaperons, which are necessary for efficient folding of many proteins in normal and stress conditions and have been implicated in several human diseases. HSP10 is the ~10kD mammalian equivalent to GroES of E.coli. The function of Hsp10 is to bind Hsp60 (also known as chaperonin-60), in the presence of ATP, thereby promoting a conformational change in Hsp60 and enclosing the protein substrate within the complex. ATP hydrolysis by Hsp60 destabilizes the Hsp60/ Hsp10 complex, allowing it to dissociate and release the substrate protein. Recombinant human HSP10 was expressed in E.coli and purified by using conventional chromatography techniques