

| Numéro de catalogue | HY489016 |
|---|---|
| Description |
Anti-Human GRP78/HSPA5 (PAT-SM6) (HY489016) is a research-grade recombinant antibody targeting Heat shock protein 70 family protein 5. Produced in mammalian cells with native-like glycosylation.
Highlights
|
| Reactivité des espèces | Human |
| Applications | ELISA, Bioactivity: FCM, Functional assay, Research in vivo |
| Espèce hôte | Human |
| Clonalité | Monoclonal |
| Isotype | IgG |
| ID de clone | PAT-SM6 |
| Système d'expression | Mammalian cells |
| Nature | Recombinant |
| Cible | Heat shock protein 70 family protein 5, 78 kDa glucose-regulated protein, HSPA5, Binding-immunoglobulin protein, GRP-78, HSP70 family protein 5, Heat shock protein family A member 5, Endoplasmic reticulum chaperone BiP, GRP78, BiP, Immunoglobulin heavy chain-binding protein |
| Niveau d'endotoxines | < 10 EU/mg as determined by LAL method. |
| Pureté | >95% as determined by SDS-PAGE. |
| Purification | Protein A/G purified from cell culture supernatant. |
| Numéro d'accès | P11021 |
| Forme | Liquid |
| Tampon de stockage | 0.01M PBS pH 7.4. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot. |
| Stabilité et stockage | 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. |
| Noms alternatifs | PAT-SM6, PATSM6, PATSM6 |
| Contexte | Endoplasmic reticulum chaperone BiP (HSPA5/GRP78) 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. Not suitable for clinical or therapeutic use. |

SDS-PAGE for Research Grade Anti-Human GRP78/HSPA5 (PAT-SM6)




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