Recombinant Human GroES

Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:7912672, PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). {PubMed:11422376, PubMed:1346131, PubMed:7912672, PubMed:25918392}.

Store at 4°C if entire vial will be used within 2-4 weeks. Store at or below -20°C for longer periods of time. For long term storage, addition of a carrier protein (0.1% HSA or BSA) is recommended.

Hsp10 is a molecular chaperone that plays a role in protein folding under normal and stress conditions. It binds to Hsp60 in the presence of ATP causing a change in Hsp60 conformation and thus enclosing a protein substrate within this complex. ATP hydrolysis by chaperonin-60 destabilizes the Hsp10- Hsp60 complex allowing it to dissociate and release the protein substrate.