Anti-HSP60

Custom conjugation services for this antibody as available (eg. labeling of Anti-HSP60 with HRP. Available labels are AF: AF350, AF488, AF555, AF594, AF647, AF680, AF700, AF750. Proteins: HRP, Alkaline Phosphatase, Streptavidin. Tandems: APC, APC/Cy7, APC/AF750, APC/iFluor(TM) 700, APC/iFluor(TM) 750, PE, PE/Cy5, PE/Cy7, PE/AF610, PE/AF700, PE/iFluor(TM) 594, PE/iFluor(TM) 647, PE/iFluor(TM) 700, PE/iFluor(TM) 750, PE/Texas Red(R), PerCP, PerCP/Cy5.5. Small Molecules: Biotin. Traditional Dyes: FITC (Fluorescein), TRITC (Rhodamine), PacBlue, PacOrange, Cy3, Cy5. iFluor: 350, 405, 430, 450, 488, 514, 532, 546, 555, 560, 568, 594, 610, 633, 647, 660, 670, 680, 700, 710, 750, 790, 800, 810, 820, 840, 860, A7. mFluor: UV375, UV460, Violet 450, Violet 500, Violet 510, Violet 540, Blue 570, Green 620, Red 700, Red 780. 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]