|Product Name||Anti-HSP60/HSPD1 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for 60 kDa heat shock protein, mitochondrial(HSPD1) detection. Tested with WB, IHC-P, ICC in Human;Mouse;Rat.|
|Cite This Product||Anti-HSP60/HSPD1 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1106)|
|Contents/Buffer||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.|
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of rat HSP60(503-516aa YDAMLGDFVNMVEK), different from the related human sequence by one amino acid.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Immunocytochemistry , 0.5-1μg/ml, Human, -
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat
Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P) and ICC.
Images And Assay Conditions
Anti-HSP60 antibody, PA1106, Western blotting
Lane 1: Rat Brain Tissue Lysate
Lane 2: Rat Liver Tissue Lysate
Lane 3: CEM Cell Lysate
Lane 4: HELA Cell Lysate
Lane 5: SMMC Cell Lysate
Lane 6: COLO320 Cell Lysate
Anti-HSP60 antibody, PA1106, IHC(P)
IHC(P): Rat Intestine Tissue
Anti-HSP60 antibody, PA1106, ICC
ICC: SMMC Cell
Protein Target Info (Source: Uniprot.org)
|Protein Name||60 kDa heat shock protein, mitochondrial|
|Alternative Names||60 kDa heat shock protein, mitochondrial;60 kDa chaperonin;Chaperonin 60;CPN60;HSP-65;Heat shock protein 60;HSP-60;Hsp60;Mitochondrial matrix protein P1;Hspd1;Hsp60;|
|Subcellular Localization||Mitochondrion matrix .|
|Molecular Weight||60955 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||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.|
|Research Areas||Chaperones, Heat Shock Proteins, Mitochondria, Organelles, Protein Trafficking, Signal Transduction, Subcellular Markers, Tags & Cell Markers
*You can search these to find other products in these research areas.
|Background||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.|
Other Recommended Resources
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,