Anti-Cpn10 antibody
Specifications
| Product type: | Primary antibody |
| Antigen: | Cpn10 |
| Immunogen: | Recombinant protein within human Cpn10 aa 1-150 |
| Species immunized: | Rabbit |
| Isotype: | IgG |
| Applications: | Western Blot (1:500-1:2000); Immunoprecipitation (1:10-1:50); Immunohistochemistry (1:50-1:200) |
| Reactivity: | Human, Mouse, Rat |
| Clonality (clone number): | Monoclonal (JG82-34) |
| Form: | Liquid |
| Buffer: | Tris-HCl buffer (pH7.4), 1% BSA, 40% glycerol, 0.05% NaN3. |
| Concentration: | 1mg/ml |
| Purity: | Protein A affinity purified |
| Storage: | Aliquot and freeze at -20℃. Avoid multiple freeze/thaw cycles. |
| Alternative names: | 10 kDa chaperonin antibody |
| 10 kDa heat shock protein mitochondrial antibody | |
| 10 kDa heat shock protein, mitochondrial antibody | |
| CH10_HUMAN antibody | |
| Chaperonin 10 antibody | |
| Chaperonin 10 homolog antibody | |
| CPN10 antibody | |
| cpn10 homolog antibody | |
| Early pregnancy factor antibody | |
| Early-pregnancy factor antibody | |
| EPF antibody | |
| GROES antibody | |
| GroES homolog antibody | |
| Heat shock 10kD protein 1 chaperonin 10 antibody | |
| Heat shock 10kDa protein 1 antibody | |
| Heat shock 10kDa protein 1 chaperonin 10 antibody | |
| Heat shock protein family E (Hsp10) member antibody | |
| Heat-shock 10-kD protein antibody | |
| Hsp10 antibody | |
| Hspe1 antibody |
Target information
Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, 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:7912672, 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