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

Mouse IgG1

60 kDa

Western blot, 0.1-0.5?g/ml

Immunohistochemistry (Paraffin-embedded Section), 0.5-1?g/ml

Immunocytochemistry/Immunofluorescence, 5?g/ml

Flow Cytometry (Fixed), 1-3?g/1x10⁶ cells

heat shock protein family D (Hsp60) member 1

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.

Each vial contains 4 mg Trehalose, 0.9mg NaCl, 0.2mg Na₂HPO₄, 0.05 mg NaN₃.

Add 0.2 ml of distilled water will yield a concentration of 500 µg/ml.

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.

Boster Bio Anti-Hsp60/HSPD1 Antibody Picoband® (monoclonal, 6G2) catalog # M01280-3. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.