Recombinant Human Heat Shock 10kDa Protein 1 (chaperonin 10)

Specification :
| Description : HSPE1 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. HSPE1 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/ HSPE1 complex, allowing it to dissociate and release the substrate protein. | Source : E. coli | Species : Human | Tag : N/A | Form : Liquid. In 20 mM Tris-HCl buffer (pH 8.0) containing 50 mM NaCl | Molecular Mass : 10 kDa (102 aa), confirmed by MALDI-TOF | Protein length : 1-102aa | AA Sequence : MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD | Endotoxin : | Purity : >95% by SDS – PAGE | Applications : SDS-PAGE | Storage : Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles. | Concentration : 1 mg/ml (determined by Bradford assay)