Anti-Hsp60 Antibody

EC 5.6.1.7, 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, Hsp60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein

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}.

Immunoblotting: use at 0.25-1ug/mL. A band of ~60 kDa is detected. <br><br>Immunohistochemistry: use at 5ug/mLFlow cytometry: use at 10ug/mL <br><br>These are recommended concentrations. User should determine optimal concentrations for their application. <br><br>Positive control: Heat-shocked HeLa cell lysate.

This antibody recognizes human, mouse, rat, rabbit, bovine, canine, porcine, guinea pig, hamster, chicken, monkey, white fly, yeast and bacterial* Hsp60 (60 kDa). The epitope recognized is within aa 383-419 of human Hsp60. *Borellia, E. coli, Helicobacter pylori, M. bovis, Salmonella typhimurium, Streptococcus pyogenes, Treponema hyodysenteriae, Treponema innocense, Trichinella spiralis, Yersinia enterocolitica.

Hsp60 is an abundant protein synthesized constitutively in various cell types that is induced to higher concentrations after cell shock. It is present in mitochondria of many mammalian species and has highly similar counterparts in bacteria and plants (where it is localized to chloroplasts). In general, Hsp60 proteins are present in high concentrations, are induced in response to environmental stresses (such as heat shock) are homo-oligomeric structures of 7 or 14 subunits that dissociate reversibly in the presence of Mg2+ and ATP, have ATPase activity, and play a role in folding and assembly of oligomeric protein structures. Hsp60 has been linked to Alzheimer's disease, coronary artery disease, multiple sclerosis, diabetes, and other autoimmune diseases.