Anti-HSP60 (Heat Shock Protein 60) (Mitochondrial Marker) Monoclonal Antibody (Clone: CPTC-HSPD1-1)

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes, and the regulation of protein folding. The mitochondrial and cytosolic localization of HSP60, combined with its binding and catalysis of folding of newly synthesized proteins destined for the mitochondrial matrix, classify this protein as a molecular chaperone. An additional role of HSP 60 is to act as a cell surface marker for T cell recognition, as well as being involved in a danger signal cascade immune response. HSP60 has been shown to influence apoptosis in tumor cells, and changes in its expression level may serve as a biomarker, as down-regulated HSP60 expression indicates a poor prognosis as well as a risk of tumor infiltration development, especially with regard to urothelial carcinomas. In ovarian cancer, decreased expression of HSP60 correlates with aggressive tumor types, while overexpression is correlated with a better patient prognosis. Protein function: 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). [The UniProt Consortium]