

| Catalog No. | HY489023 | ||||||
|---|---|---|---|---|---|---|---|
| Species reactivity | Human | ||||||
| Applications | ELISA, FCM, IHC, Inhibition, WB | ||||||
| Host species | Human | ||||||
| Isotype | IgG1, kappa | ||||||
| Clone ID | huMAb159 | ||||||
| Clonality | Monoclonal | ||||||
| Target | 78 kDa glucose-regulated protein, BiP, Binding-immunoglobulin protein, EC:3.6.4.10, Endoplasmic reticulum chaperone BiP, GRP-78, GRP78, HSP70 family protein 5, HSPA5, Heat shock protein 70 family protein 5, Heat shock protein family A member 5, Immunoglobulin heavy chain-binding protein | ||||||
| Endotoxin level | Please contact with the lab for this information. | ||||||
| Purity | >95% as determined by SDS-PAGE. | ||||||
| Purification | Protein A/G purified from cell culture supernatant. | ||||||
| Accession | P11021 | ||||||
| Form | Liquid | ||||||
| Storage buffer | 0.01M PBS pH 7.4 Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| 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. | ||||||
| Background | Endoplasmic reticulum chaperone BiP (GRP78/HSPA5) is a ~72 kDa protein. Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Also binds and inactivates EIF2AK3/PERK in unstressed cells. 1. Dana, RC. et al. (1990) Endocrinology 126, 672-4. PMID: 2294010 2. Oka, OB. et al. (2013) Molecular cell 50, 793-804. PMID: 23769672 3. Evensen, NA. et al. (2013) Journal of the National Cancer Institute 105, 1402-16. PMID: 23990668 4. Cuevas, EP. et al. (2017) Scientific reports 7, 44988. PMID: 28332555 5. Ma, K. et al. (2002) The Journal of biological chemistry 277, 18728-35. PMID: 11907036 6. Ng, DT. et al. (1992) Molecular biology of the cell 3, 143-55. PMID: 1550958 7. Oikawa, D. et al. (2009) Experimental cell research 315, 2496-504. PMID: 19538957 8. Kovaleva, V. et al. (2023) Cell reports 42, 112066. PMID: 36739529 9. Kang, JM. et al. (2015) Cancer research 75, 3087-97. PMID: 26045166 | ||||||
| Note | For research use only |




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