Anti-HSP10

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Heat shock 10kDa protein 1, also called CPN10, GROES, and HSP10, is a protein that in humans is encoded by the HSPE1 gene. It is a heptameric ring of identical 10.4-kD subunits that binds to each end of GroEL to form a symmetric, functional heterodimer. The transcriptional activity of the promoter fragment in the HSP60 direction is approximately twice that in the HSP10 direction under normal growth conditions, upon heat shock, promoter activity in either direction increased by a factor of approximately 12. Mutational drifts performed in vitro with 4 different enzymes indicated the HSP10 overexpression doubled the number of accumulating mutations, and promoted the folding of enzyme variants carrying mutations in the protein core and/or mutations with higher destabilizing effects. Protein function: 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). [The UniProt Consortium]