

| Каталожный номер | HY029014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Описание |
Anti-HSPA1A Polyclonal Antibody (HY029014) is a rabbit polyclonal antibody detecting HSPA1A in ELISA, IHC, WB. Suitable for Human, Mouse, Rat, Bovine, and Bos mutus grunniens.
Highlights
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| Реактивность видов | Human, Mouse, Rat | ||||||||
| Применения | ELISA, IHC, WB | ||||||||
| Хозяинский вид | Rabbit | ||||||||
| Клоональность | Polyclonal | ||||||||
| Изотип | IgG | ||||||||
| Иммуноген | E. coli - derived recombinant Human HSPA1A (Met1-Asp641). | ||||||||
| Цель | HSP70.1, HSP70-1, HSPA1, HSPA1A, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1, HSP72, HSX70 | ||||||||
| Очистка | Purified by antigen affinity column. | ||||||||
| Номер доступа | P0DMV8 | ||||||||
| Форма | Liquid | ||||||||
| Буфер хранения | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Пожалуйста, обратитесь к конкретной информации о буфере в печатной версии даташита или в индивидуальном сертификате качества (COA) для партии. |
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| Информация об использовании продукта |
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| Устойчивость и хранение | 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. | ||||||||
| Фон | 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 | ||||||||
| Примечание | For research use only. |
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