antibody

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

M01280-3

100µg/vial

monoclonal

mouse

nonconjugated

6G2

human, mouse, rat

western blot, immunocytochemistry, flow cytometry, immunohistochemistry - paraffin section

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

100µg/vial

Monoclonal

6G2

Mouse

Human, Mouse, Rat

Flow Cytometry, IF, IHC-P, ICC, WB

Western blot, 0.1-0.5µg/ml. Immunohistochemistry (Paraffin-embedded Section), 0.5-1µg/ml. Immunocytochemistry/Immunofluorescence, 5µg/ml. Flow Cytometry, 1-3μg/1x10^6 cells.

Tested Species: In-house tested species with positive results. By Heat: Boiling the paraffin sections in 10mM citrate buffer, pH6.0, for 20mins is required for the staining of formalin/paraffin sections. Other applications have not been tested. Optimal dilutions should be determined by end users.

Boster Bio Anti-Hsp60/HSPD1 Antibody Picoband™ (monoclonal, 6G2) catalog # M01280-3. Tested in Flow Cytometry, IF, IHC-P, ICC, WB applications. This antibody reacts with Human, Mouse, Rat.

HSPD1

P10809

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.

Lyophilized

Each vial contains 4mg Trehalose, 0.9mg NaCl, 0.2mg Na 2 HPO 4 , 0.05mg NaN 3 .

No cross reactivity with other proteins.

IgG1

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

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

heat shock protein family D (Hsp60) member 1

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

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.

Mitochondrion matrix.

Boster recommends Enhanced Chemiluminescent Kit with anti-Mouse IgG (EK1001) for Western blot, and HRP Conjugated anti- Mouse IgG Super Vision Assay Kit (SV0001-1) for IHC(P) and ICC.

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.