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> home > Products > Primary Antibodies > Signal Transduction > Anti-Hsp60 HSPD1 Rabbit Monoclonal Antibody
Anti-Hsp60 HSPD1 Rabbit Monoclonal Antibody
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Application 
| WB, IHC |
|---|---|
| Primary Accession | P10809 |
| Host | Rabbit |
| Isotype | Rabbit IgG |
| Reactivity | Rat, Human, Mouse |
| Clonality | Monoclonal |
| Format | Liquid |
| Description | Anti-Hsp60 HSPD1 Rabbit Monoclonal Antibody . Tested in WB, IHC applications. This antibody reacts with Human, Mouse, Rat. |
| Gene ID | 3329 |
|---|---|
| Other Names | 60 kDa heat shock protein, mitochondrial, 5.6.1.7, 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, Hsp60, Heat shock protein family D member 1, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1, HSP60 |
| Calculated MW | 61055 MW KDa |
| Application Details | WB 1:500-1:2000 IHC 1:50-1:200 |
| Subcellular Localization | Mitochondrion matrix. |
| Contents | Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol, 0.4-0.5mg/ml BSA. |
| Clone Names | Clone: DOI-8 |
| Immunogen | A synthesized peptide derived from human Hsp60 |
| Purification | Affinity-chromatography |
| Storage | Store at -20°C for one year. For short term storage and frequent use, store at 4°C for up to one month. Avoid repeated freeze-thaw cycles. |
| Name | HSPD1 |
|---|---|
| Synonyms | HSP60 |
| Function | 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:11422376, PubMed:1346131). 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). |
| Cellular Location | Mitochondrion matrix. |
Research Areas
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Application Protocols
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$ 370.00
Cat# ABO13632
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