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This product is an unconjugated anti-HSPD1 Monoclonal antibody (2E1/53) generated from the Mouse. This antibody can be used for WB, ELISA, IF, IHC, IP.
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specifications |
|
|---|---|
| Antibody Isotype | IgM |
| Clone | 2E1/53 |
| Applications | WB; ELISA; IF; IHC; IP |
| Target | HSPD1 |
| Epitope | This antibody recognizes an epitope between amino acids 211-288 of human HSP60. |
| Host | Mouse |
| Clonality | Monoclonal |
| Antibody Type | Primary antibody |
| Species Reactivity | Human, Mouse |
| Immunogen | Human placental HSP60 |
| Format | Lyophilized |
| Buffer | PBS with BSA |
| Storage | Store at -20° C to -80° C. Avoid freeze-thaw cycles. |
Target Information |
|
|---|---|
| Target Name | HSPD1 |
| Alternative Names | Heat Shock Protein Family D (Hsp60) Member 1; HSP60; Mitochondrial Matrix Protein P1; P60 Lymphocyte Protein; 60 KDa Chaperonin; Chaperonin 60; HSP-60; CPN60; Spastic Paraplegia 13 (Autosomal Dominant); Epididymis Secretory Sperm Binding Protein; Heat Shock 60kD Protein 1 (Chaperonin); Short Heat Shock Protein 60 Hsp60s1; Heat Shock Protein 60; GROEL; HSP65; SPG13 HSPD1; GroEL; Hsp60; HLD4 |
| Related Disease | Spastic Paraplegia 13 Autosomal Dominant; Leukodystrophy Hypomyelinating 4 |
| Gene ID | 3329 |
| UniProt ID | P10809 |
| 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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