Anti-HSP60 antibody
Specifications
| Product Cat#: | AB-06-2277 |
| Product type: | Primary antibody |
| Antigen: | HSP60 |
| Immunogen: | Peptide |
| Species immunized: | Mouse |
| Isotype: | IgG1 |
| Applications: | Western Blot (1:1800-1:2000); Immunohistochemistry (1:180-1:200); Immunocytochemistry (1:180-1:200) |
| Reactivity: | Mouse, Rat and Human |
| Clonality (clone number): | Monoclonal （1-80） |
| Form: | Liquid |
| Buffer: | Tris-HCl buffer (pH7.4),1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide. |
| Concentration: | 2 mg/ml |
| Purity: | Protein A affinity purified |
| Storage: | Aliquot and freeze at -20℃. Avoid multiple freeze/thaw cycles. |
| Alternative names: | 60 kDa chaperonin antibody |
| 60 kDa heat shock protein, mitochondrial antibody | |
| CH60_HUMAN antibody | |
| Chaperonin 60 antibody | |
| Chaperonin, 60-KD antibody | |
| CPN60 antibody | |
| Fa04a05 antibody | |
| GROEL antibody | |
| Heat shock 60kDa protein 1 (chaperonin) antibody | |
| Heat shock protein 1 (chaperonin) antibody | |
| Heat shock protein 60 antibody | |
| Heat shock protein 65 antibody | |
| Heat shock protein family D (Hsp60) member 1 antibody | |
| HLD4 antibody | |
| Hsp 60 antibody | |
| HSP 65 antibody | |
| HSP-60 antibody | |
| HSP60 antibody | |
| HSP65 antibody | |
| HSPD1 antibody | |
| HuCHA60 antibody | |
| Mitochondrial matrix protein P1 antibody | |
| P60 lymphocyte protein antibody | |
| short heat shock protein 60 Hsp60s1 antibody | |
| SPG14 antibody |
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
