

| 货号 | PX-P5754 |
|---|---|
| 品牌 | ProteoGenix |
| 描述 |
Recombinant Human HSPA1L Protein, N-His (PX-P5754) expressed in E. coli, Purity: >90% as determined by SDS-PAGE..
Highlights
|
| 表达系统 | E. coli |
| Accession号 | P34931 |
| 蛋白长度 | Met1-Asp641 |
| 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 | 72.68 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 | HSP70-Hom, Heat shock 70 kDa protein 1L, Heat shock 70 kDa protein 1-like, HSPA1L, Heat shock 70 kDa protein 1-Hom |
| 背景 | Heat shock 70 kDa protein 1-like (HSPA1L) is a ~70 kDa protein. Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. 1. Radons, J. (2016) Cell stress & chaperones 21, 379-404. PMID: 26865365 2. Hasson, SA. et al. (2013) Nature 504, 291-5. PMID: 24270810 |
| Note | For research use only. |

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