

| 货号 | PX-P5760 |
|---|---|
| 品牌 | ProteoGenix |
| 描述 |
Recombinant Human HSPD1 Protein, N-His (PX-P5760) expressed in E. coli, Purity: >90% as determined by SDS-PAGE..
Highlights
|
| 表达系统 | E. coli |
| Accession号 | P10809 |
| 蛋白长度 | Ala27-Phe573 |
| 应用 | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| 种属 | Homo sapiens (Human) |
| 性质 | Recombinant |
| 内毒素水平 | Please contact with the lab for this information. |
| 纯度 | >90% as determined by SDS-PAGE. |
| 预测分子量 | 60.27 kDa |
| 状态 | Lyophilized |
| 保存溶液 | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| 重悬 | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| 运输 | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| 稳定性和存储 | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| 别名 | 60 kDa heat shock protein, mitochondrial, HSP-60, HuCHA60, Chaperonin 60, HSP60, Mitochondrial matrix protein P1, Hsp60, HSPD1, 60 kDa chaperonin, CPN60, P60 lymphocyte protein, Heat shock protein 60 |
| 背景 | 60 kDa heat shock protein, mitochondrial (HSPD1) is a ~61 kDa protein. 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. 1. Levy-Rimler, G. et al. (2001) European journal of biochemistry 268, 3465-72. PMID: 11422376 2. Viitanen, PV. et al. (1992) The Journal of biological chemistry 267, 695-8. PMID: 1346131 |
| Note | For research use only. |

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