

| Número de catálogo | HY029014 | ||||||||
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| Descripción |
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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| Reactividad de especies | Human, Mouse, Rat | ||||||||
| Aplicaciones | ELISA, IHC, WB | ||||||||
| Especie huésped | Rabbit | ||||||||
| Clonalidad | Polyclonal | ||||||||
| Isotipo | IgG | ||||||||
| Inmunógeno | E. coli - derived recombinant Human HSPA1A (Met1-Asp641). | ||||||||
| Objetivo | HSP70.1, HSP70-1, HSPA1, HSPA1A, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1, HSP72, HSX70 | ||||||||
| Purificación | Purified by antigen affinity column. | ||||||||
| Número de acceso | P0DMV8 | ||||||||
| Forma | Liquid | ||||||||
| Buffer de almacenamiento | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Consulte la información específica del buffer en la copia impresa del datasheet o en el COA específico del lote. |
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| Información de uso del producto |
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| Estabilidad y almacenamiento | 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. | ||||||||
| Fondo | 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 | ||||||||
| Nota | For research use only. |
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