HSP60 polyclonal, anti-human, mouse, rat

Background:
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

Synonyms: CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13

Cellular Location: Cytoplasm

Immunogen:
Recombinant protein of human HSP60

Gene Symbol: HSP60

Gene ID: 3329

Swiss prot: P10809

Calculated MW: 60kDa

Recommended dilution:
WB 1:500-2000, IHC 1:50-200,

Purity:
Affinity purification

Storage Buffer:
Buffer: PBS with 0.03% Proclin300, 50% glycerol, pH7.3.

Storage:
Store at -20℃. Avoid freeze / thaw cycles.