catalog number :
MBS857756
products full name :
BiP/GRP78 Antibody
products short name :
[BiP/GRP78]
products name syn :
[MIF2; HSPA5; FLJ26106]
other names :
[endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone BiP; endoplasmic reticulum chaperone BiP; heat shock protein family A (Hsp70) member 5; 78 kDa glucose-regulated protein]
products gene name :
[BiP/GRP78]
products gene name syn :
[BIP; MIF2; GRP78]
other gene names :
[HSPA5; HSPA5; BIP; MIF2; GRP78; HEL-S-89n; HSP70 family protein 5Curated]
specificity :
This antibody detects endogenous levels BiP/GRP78 and does not cross-react with related proteins.
purity :
Affinity purified
form :
Purified mouse monoclonal in buffer containing 0.1M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.2% sodium azide, 50%, glycerol
tested application :
Western Blot (WB), Immunocytochemistry (ICC)
image1 heading :
Testing Data
image2 heading :
Testing Data #2
other info1 :
Immunogen: Purified recombinant human BiP/GRP78 protein fragments expressed in E Coli. Cellular Localization: Endoplasmic reticulum lumen; Melanosome
products categories :
Autophagy antibody; Cancer; Cardiovascular; Cell Biology; Epigenetics & Nuclear Signaling; Developmental Biologys; Immunology; Drug Discovery Products; Metabolism; Neuroscience; Signal Transduction; Stem Cells
products description :
UniPort Summary Function: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Entrez Summary: The 78 kDa glucose regulated protein/BiP (GRP78) belongs to the family of ~70 kDa heat shock proteins (HSP 70). GRP78 is a resident protein of the endoplasmic reticulum (ER) and may associate transiently with a variety of newly synthesized secretory and membrane proteins or permanently with mutant or defective proteins that are incorrectly folded, thus preventing their export from the ER lumen. GRP78 is a highly conserved protein that is essential for cell viability. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the C terminus of GRP78 and other resident ER proteins including glucose regulated protein 94 (GRP 94) and protein disulfide isomerase (PDI). The presence of carboxy terminal KDEL appears to be necessary for retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
ncbi acc num :
NP_005338.1
ncbi gb acc num :
NM_005347
ncbi pathways :
Activation Of Chaperone Genes By ATF6-alpha Pathway (530770); Activation Of Chaperones By ATF6-alpha Pathway (105905); Activation Of Chaperones By IRE1alpha Pathway (105906); Adaptive Immune System Pathway (366160); Antigen Presentation: Folding, Assembly And Peptide Loading Of Class I MHC Pathway (366163); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Class I MHC Mediated Antigen Processing Presentation Pathway (366161); Hemostasis Pathway (106028); Immune System Pathway (106386)
ncbi summary :
The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.[provided by RefSeq, Sep 2010]
uniprot summary :
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). 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 ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). 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 (). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 ().