Recombinant Human GroEL

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, 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: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: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.

Hsp60 is a mitochondrial chaperonin responsible for transportation and refolding of proteins from the cytoplasm directly into the mitochondrial matrix. Hsp60 is regulated by the Hsp10 co- chaperonin. Hsp10 coordinates the ATPase activity of the Hsp60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding.