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This product is a conjugated anti-HSP65 Monoclonal antibody (3F7) generated from the Mouse. This antibody can be used for WB.
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specifications |
|
|---|---|
| Antibody Isotype | IgM |
| Clone | 3F7 |
| Applications | WB |
| Target | HSP65 |
| Host | Mouse |
| Clonality | Monoclonal |
| Antibody Type | Primary antibody |
| Species Reactivity | Mycobacterium bovis, Human, Mouse, Rat, Bovine, Cryptospordium, Drosophila, Ecoli, Guinea pig, Hamster |
| Immunogen | Recombinant M. bovis HSP65 |
| Format | Liquid |
| Buffer | PBS |
| Storage | Store at 4° C in dark. Do not freeze. |
Target Information |
|
|---|---|
| Target Name | HSP65 |
| Alternative Names | 60 kDa chaperonin 2; 65 kDa antigen; Antigen A; Cell wall protein A; GroEL protein 2; Heat shock protein 65; Protein Cpn60-2; groL2; groEL-2; groEL2; hsp65 |
| Related Disease | Spastic Paraplegia 13 Autosomal Dominant; Leukodystrophy Hypomyelinating 4 |
| Gene ID | 45424401 |
| UniProt ID | P0A521 |
| Target Overview | 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. 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. |
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Datasheet
