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> home > Products > Primary Antibodies > Antibody Collections > Goat Antibodies > Goat anti-HSP60 / HSPD1 (aa333-344) Antibody
Goat anti-HSP60 / HSPD1 (aa333-344) Antibody
Peptide-affinity purified goat antibody
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Application 
| WB, IHC, IF, Pep-ELISA |
|---|---|
| Primary Accession | P10809 |
| Other Accession | NP_002147.2 |
| Reactivity | Human, Pig, Dog, Bovine |
| Host | Goat |
| Clonality | Polyclonal |
| Clone Names | HSPD1 |
| Calculated MW | 61055 Da |
| Gene ID | 3329 |
|---|---|
| Other Names | HSPD1; heat shock 60kDa protein 1 (chaperonin); CPN60; GROEL; HLD4; HSP-60; HSP60; HSP65; HuCHA60; SPG13; 60 kDa chaperonin; 60 kDa heat shock protein, mitochondrial; P60 lymphocyte protein; chaperonin 60; heat shock protein 65; mitochondrial matrix prote |
| Format | Supplied at 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. Aliquot and store at -20°C. Minimize freezing and thawing. |
| Immunogen | Reported variants represent identical protein: NP_955472.1, NP_002147.2. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat anti-HSP60 / HSPD1 (aa333-344) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| 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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$ 341.00
Cat# AF4378a
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