Anti-Hsp60/HSPD1 Antibody Picoband® (monoclonal, 6G2) Fluoro488 Conjugated

HSP60 is a member of the chaperonin class of protein factors, which include the Escherichia coli groEL protein and the Rubisco subunit-binding protein of chloroplasts. It acts as a costimulator of human regulatory CD4-positive/CD25 -positive T cells, which inhibit lymphoproliferation and IFNG and TNF secretion by CD4-positive and CD8-positive T cells. HSP60 enhances Treg activity via TLR2, leading to activation of an intracellular signaling cascade that included p38, as well as inhibition of ERK phosphorylation. Suppression of target T cells is mediated by both cell-to-cell contact and by secretion of TGFB and IL10, and it leads to downregulation of ERK, NFKB, and TBET expression. The self-molecule HSP60 can downregulate adaptive immune responses by upregulating Tregs through TLR2 signaling.

60 kDa heat shock protein, mitochondrial; 60 kDa chaperonin; Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; Hsp60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; HSPD1; HSP60

E.coli-derived human Hsp60/HSPD1 recombinant protein (Position: A260-Q496) . Human Hsp60 shares 97% amino acid (aa) sequence identity with both mouse and rat Hsp60.

Cancer, Cell Biology, Cell Cycle, Cell Cycle Inhibitors, Deubiquitination, Epigenetics and Nuclear Signaling, Host-Virus Interaction, Interspecies Interaction, Microbiology, p53 Pathway, Proteasome / Ubiquitin, Proteolysis/Ubiquitin, Ubiquitin & Ubiquitin Like Modifiers

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.

1. Cheng, M. Y.; Hartl, F.-U.; Martin, J.; Pollock, R. A.; Kalousek, F.; Neupert, W.; Hallberg, E. M.; Hallberg, R. L.; Horwich, A. L. : Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337: 620-625, 1989. 2. Zanin-Zhorov, A.; Cahalon, L.; Tal, G.; Margalit, R.; Lider, O.; Cohen, I. R. : Heat shock protein 60 enhances CD4+CD25+ regulatory T cell function via innate TLR2 signaling. J. Clin. Invest. 116: 2022-2032, 2006.