

| 货号 | PTX19553 |
|---|---|
| 品牌 | ProteoGenix |
| 描述 |
Anti-HSPA1A Polyclonal Antibody (PTX19553) is a rabbit polyclonal antibody detecting HSP70.1,HSP70-1,HSPA1,HSPA1A,Heat shock 70 kDa protein 1A,Heat shock 70 kDa protein 1,HSP72,HSX70 in ELISA, IHC, WB. Suitable for Human, Mouse, Rat.
Highlights
|
| 种属反应性 | Human, Mouse, Rat |
| 应用 | ELISA, IHC, WB |
| 宿主 | Rabbit |
| 同种型 | IgG |
| 克隆类型 | Polyclonal |
| 免疫原 | E. coli - derived recombinant Human HSPA1A (Met1-Asp641). |
| 靶标 | HSP70.1,HSP70-1,HSPA1,HSPA1A,Heat shock 70 kDa protein 1A,Heat shock 70 kDa protein 1,HSP72,HSX70 |
| 纯化方式 | Purified by antigen affinity column. |
| Accession号 | P0DMV8 |
| 状态 | Liquid |
| 保存溶液 | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| 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. |
| 背景 | Heat shock 70 kDa protein 1A (HSPA1A) 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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. 1. Mayer, MP. (2013) Trends in biochemical sciences 38, 507-14. PMID: 24012426 2. Rauch, JN. et al. (2014) The Journal of biological chemistry 289, 1402-14. PMID: 24318877 3. Radons, J. (2016) Cell stress & chaperones 21, 379-404. PMID: 26865365 4. Seo, JH. et al. (2016) Nature communications 7, 12882. PMID: 27708256 5. Fang, CT. et al. (2016) Cellular and molecular life sciences : CMLS 73, 3949-60. PMID: 27137183 6. Shang, Y. et al. (2014) Biochemical and biophysical research communications 446, 387-92. PMID: 24613385 7. Chen, Z. et al. (2013) Immunity 39, 272-85. PMID: 23973223 8. Shi, Y. et al. (1998) Genes & development 12, 654-66. PMID: 9499401 9. Wang, WF. et al. (2017) Nature communications 8, 363. PMID: 28842558 |
| Note | For research use only. |

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