HSP60 Antibodies

Target Information

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. 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. Belongs to the chaperonin (HSP60) family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.

Alternate Names

60 kDa chaperonin; 60 kDa heat shock protein, mitochondrial; CH60; Chaperonin 60; CPN60; epididymis secretory sperm binding protein; GROEL; heat shock 60kDa protein 1 (chaperonin); Heat shock protein 60; heat shock protein 65; heat shock protein family D (Hsp60) member 1; HLD4; HSP-60; HSP60; HSP65; HSPD1; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; short heat shock protein 60 Hsp60s1; SPG13