HSP10, 1-102aa, Human, Recombinant, E.coli

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 ca.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.

Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.

1 mg/ml (determined by Bradford assay)

• Lin KM., et al. (2004), FASEB J. 18(9):1004-6
• Hohfeld J., et al. (1994), J. Cell BIol. 126(2):305-15

>, 95% by SDS - PAGE

MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD

<, 1.0 EU per 1 microgram of protein (determined by LAL method)