Material Data Sheet

HSP60/HSP10 Glow-Fold Protein Refolding Kit

Price: $475.00
Catalog #: K-300

HSP60/HSP10 Glow-Fold Protein Refolding Kit

1 Kit
Data Sheet: 

HSP60 (also known as Chaperonin 60) and HSP10 (also known as Chaperonin 10) are the eukaryotic homologues of prokaryotic GroEL and GroES chaperones, respectively.  These proteins are found mainly in mitochondria, but can also be detected in cytosol and extracellular fluids including peripheral blood.  The HSP60/HSP10 complex plays an essential role in the translocation and refolding of proteins from the cytosol into the mitochondrial matrix. Under physiological conditions, HSP60 creates two stacked heptameric rings that form a pair of central hydrophobic cavities.  After an unfolded substrate protein enters one of cavities it is capped by a heptameric HSP10 complex, thereby trapping the unfolded protein.  Structural rearrangement of the substrate-containing cavity is effected via HSP60-mediated ATP hydrolysis; this changes the lining of the cavity from hydrophobic to hydrophilic and helps promote refolding of the substrate protein.  Binding of ATP to HSP60 subunits on the distal ring of the complex then causes the dissociation of the HSP10 cap complex and concomitant release of the substrate protein from the proximal cavity.  If the protein is not completely folded, it can be further processed by the HSP60/HSP10 complex, or can interact with other chaperoning systems.   This kit provides a functional in vitro HSP60/HSP10 refolding system.  Using the provided substrate protein, the kit can be used to screen for small molecules affecting the efficiency of the refolding process (such as HSP inhibitors).  Alternatively, the HSP60/HSP10 complex may be used to test refolding of user-supplied proteins if a functional assay is available.   NOTE:  Kit contains reagents sufficient for 15 x 20 μl reactions.



Freeman B.C. & Yamamoto K.R. (2002)  Science  296: 2232-2235 Forsythe H.L., et al. (2001) J. Biol. Chem.  276: 15571-15574 Patwardhan C.A., et al.  (2013)  J. Biol. Chem.  288: 7313-7325