Anti-Hsp60/HSPD1 Antibody Picoband® (Dylight488 Conjugate)

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

Implicated in mitochondrial protein import and macromolecular assembly. May facilitate 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.

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat<br> Immunohistochemistry (Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat<br> Immunocytochemistry/Immunofluorescence, 2μg/ml, Human<br>