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 cognate 71 kDa protein (HSPA8) 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, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. 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 of HSP70, 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 of HSP70 for polypeptides is regulated by its nucleotide bound state.
1. Grove, DE. et al. (2011) Molecular biology of the cell 22, 301-14. PMID: 21148293
2. Yamamoto, YH. et al. (2010) Cell structure and function 35, 107-16. PMID: 21150129
3. Sopha, P. et al. (2012) Cell structure and function 37, 177-87. PMID: 23018488
4. Goodwin, EC. et al. (2014) PloS one 9, e94322. PMID: 24732912
5. Li, K. et al. (2017) Molecular cell 65, 52-65. PMID: 27916661
6. Chiang, HL. et al. (1989) Science (New York, N.Y.) 246, 382-5. PMID: 2799391
7. Wang, L. et al. (2023) Molecular cell 83, 281-297.e10. PMID: 36586411
