

| Catalog No. | HY600012 |
|---|---|
| Description |
Recombinant Human HSPA8 Protein, N-His (HY600012) expressed in E. coli, spanning Asp534-Gly615. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | P11142 |
| Protein length | Asp534-Gly615 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 11.83 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. Adjust the volume of sterile water so that, after reconstitution, the final stock concentration matches the value indicated on the product label or datasheet. RECONSTITUTION PROTOCOL 1. Allow the product to be reconstituted and the reconstitution diluent to reach room temperature. 2. Tap or briefly centrifuge the product vial before opening to dislodge any lyophilized material that may be dispersed on the wall or cap of the vial. 3. Use the diluent and stock concentration recommended in the product datasheet. If preparing a stock concentration higher than recommended, contact Technical Service. 4. After adding the diluent, re-cap the vial and invert gently by hand or place on a slow rocking platform to allow the reconstitution diluent to coat all the surfaces inside the vial. Note: Do not mix by vortexing or by pipetting the material up and down. 5. Allow the vial to sit at room temperature with gentle agitation for at least 15 minutes before aliquotting or using. 6. Store the reconstituted material in single use aliquots in polypropylene or siliconized tubes. Aliquots of 10 μL or larger are recommended. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | 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. |
| Alternate Names | Lipopolysaccharide-associated protein 1, HSPA10, Heat shock 70 kDa protein 8, LPS-associated protein 1, LAP-1, HSP73, HSC70, HSPA8, Heat shock cognate 71 kDa protein |
| Background | 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 8. Young, JC. et al. (2003) Cell 112, 41-50. PMID: 12526792 10. Rauch, JN. et al. (2014) The Journal of biological chemistry 289, 1402-14. PMID: 24318877 |
| Note | For research use only. |

SDS-PAGE for Recombinant Human HSPA8 Protein, N-His



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