|Reactivity||Human, Mouse, Rat|
|Calculated MW||61055 Da|
|Application & Usage||Western blot analysis (0.5-4 µg/ml). However, the optimal conditions should be determined individually. The antibody recognizes ~60 kDa of Hsp60 from samples of human, mouse and rat origins. Reactivity to other species has not been determined.|
|Other Names||HSPD1, HuCHA60, chaperonin, CPN60, SPG13, HSP65, Hsp60, GROEL, HSP-60, HSP60|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit anti-human Hsp60 polyclonal antibody in phosphate (PBS, pH 7.2) containing 30% glycerol, 0.5 % BSA and 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Hsp60 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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).|
|Cellular Location||Mitochondrion matrix.|
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Hsp60, also known as Cpn60, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell stress or shock. It is present in all species analyzed so far and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian Hsp60.
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