HSP60 Recombinant Rabbit mAb (Cy5 conjugate) (SDT-R012)
HSP60 Recombinant Rabbit mAb (Cy5 conjugate) (SDT-R012)
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Product Details
Product Details
Product Specification
| Host | Rabbit |
| Antigen | HSP60 |
| Synonyms | 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein |
| Immunogen | N/A |
| Location | Mitochondrion Matrix |
| Accession | P10809 |
| Clone Number | SDT-R012 |
| Antibody Type | Recombinant mAb |
| Application | ICC |
| Reactivity | Hu, Ms, Rt |
| Purification | Protein A |
| Concentration | 2 mg/ml |
| Conjugation | Cy5 |
| Physical Appearance | Liquid |
| Storage Buffer | PBS, 0.1% BSA, 0.01% Proclin 300 |
| Stability & Storage | 12 months from date of receipt / reconstitution, 2 to 8 °C as supplied. |
Dilution
| application | dilution | species |
| ICC | 1:100 |
Background
HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belongs to a large class of molecules that assist protein folding, called molecular chaperones.
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Immunocytochemistry
ICC shows positive staining in HeLa cells. Anti-HSP60 (Cy5 conjugate) antibody was used at 1/100 dilution (magenta) and incubated overnight at 4°C. The cells were fixed with 4% PFA and permeabilized with 0.1% PBS-Triton X-100. Nuclei were counterstained with DAPI (Blue).
ICC shows positive staining in NIH/3T3 cells. Anti-HSP60 (Cy5 conjugate) antibody was used at 1/100 dilution (Green) and incubated overnight at 4°C. The cells were fixed with 4% PFA and permeabilized with 0.1% PBS-Triton X-100. Nuclei were counterstained with DAPI (Blue).
ICC shows positive staining in C6 cells. Anti-HSP60 (Cy5 conjugate) antibody was used at 1/100 dilution (Green) and incubated overnight at 4°C. The cells were fixed with 4% PFA and permeabilized with 0.1% PBS-Triton X-100. Nuclei were counterstained with DAPI (Blue).
