Anti-Human GRP78/HSPA5 Reference Antibody (PAT-SM6, RUO) (HY489016)

Name: Anti-Human GRP78/HSPA5 Reference Antibody (PAT-SM6, RUO)
Brand: abinScience
SKU: HY489016
Price: 370 USD
Availability: InStock

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Overview

Catalog No.	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 ●Research Grade — For PK/PD studies, assay development, and ADA research. ●Native Glycosylation — Mammalian expression ensures native-like patterns.
Species reactivity	Human
Applications	ELISA, Bioactivity: FACS, Functional assay, Research in vivo
Host species	Human
Isotype	IgG
Clone ID	PAT-SM6
Expression system	Mammalian cells
Clonality	Monoclonal
Target	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
Endotoxin level	< 10 EU/mg
Purity	>95% purity 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.
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	PAT-SM6, PATSM6, PATSM6
Background	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.