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 protein corresponding to aa1-102 from human HSP10, expressed in E. coli. Uniprot/Swiss Accession: P61604 Molecular Weight: ~10kD (102aa) Amino Acid Sequence: MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.