Anti-HSP60 antibody
Specifications
| Product Cat#: | AB-07-3026 |
| Product type: | Primary antibody |
| Antigen: | HSP60 |
| Immunogen: | A synthetic peptide derived from human HSP60. The exact amino-acid sequence is proprietary. |
| Species immunized: | Rabbit |
| Isotype: | IgG |
| Applications: | Western Blot (1:500-1:2500); Immunohistochemistry (1:50-1:80); Immunofluorescence (1:100-1:400); ELISA (1:8000) |
| Reactivity: | Mouse, Rat and Human |
| Clonality (clone number): | Polyclonal |
| Form: | Liquid |
| Buffer: | PBS (without Mg2+ and Ca2+ ), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol |
| Concentration: | 1 mg/ml |
| Purity: | Antigen affinity chromatography |
| Storage: | Aliquot and freeze at -20°C. Avoid multiple freeze/thaw cycles. |
| Alternative names: | CPN60, CHAPERONIN 60-KD, GroEL E. COLI HOMOLOG OF HEAT-SHOCK 60-KD PROTEIN 1, heat shock 60kDa protein 1 (chaperonin) |
Target information
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 (PubMed:1346131, PubMed:11422376). 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 (Probable).
Provider
Erpantech Laboratory
