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.
Molecular Weight: 10kD (102 aa)
Sequence: MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VDGeneral references:Storage and Stability:May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile 40-50% glycerol, aliquot and store at -20°C. Aliquots are stable for at least 6 months at -20°C. 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.
仕様
Size：100ug
Source Antigen：Recombinant, E. coli
Grade：Highly Purified
Purity：≥ 98% by SDS PAGE
Form：Supplied as a liquid in 20mM Tris, pH 8.0, 50mM sodium chloride.
