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Mouse (Murine) GRP78 Kit ELISA pour Sandwich ELISA - ABIN425546
Li, Zhu, Shen, Wan, Arnold, Peng: Deficiency of rac1 blocks NADPH oxidase activation, inhibits endoplasmic reticulum stress, and reduces myocardial remodeling in a mouse model of type 1 diabetes. dans Diabetes 2010
In amphibians, the association of BiP with unfolded protein and its possible role in aggresome function may be vital in the maintenance of cellular proteostasis.
Hspa5 is essential for pronephros formation by mediating retinoic acid signaling.
High expression of GRP78 is associated with nonalcoholic steatohepatitis.
Data show that cancer-associated fibroblasts (CAFs (Montrer TBX1 Kits ELISA))-derived hepatocyte growth factor (HGF (Montrer HGF Kits ELISA)) or recombinant HGF (Montrer HGF Kits ELISA) activated c-Met/phosphoinositide 3-kinase (PI3K (Montrer PIK3CA Kits ELISA))/Akt (Montrer AKT1 Kits ELISA) and glucose-regulated protein 78 (GRP78) signalling pathways in ovarian cancer cells.
HSPA5/BIP has roles in endoplasmic reticulum stress, autophagy and apoptosis; inhibitors of HSPA5 could be useful in cancer treatment
Immunohistochemical analysis showed that STAT3 (Montrer STAT3 Kits ELISA), GRP78 and BAX (Montrer BAX Kits ELISA) protein levels in the combination group were significantly higher than those in STAT3 (Montrer STAT3 Kits ELISA) group and CDDP group (P<0.05). Exogenous STAT3 (Montrer STAT3 Kits ELISA) and CDDP may synergistically inhibit the xenograft tumour growth through up-regulation of BAX (Montrer BAX Kits ELISA) protein via GRP78.
GRP78 inhibition enhances ATF4 (Montrer ATF4 Kits ELISA)-induced cell death by the deubiquitination and stabilization of CHOP (Montrer DDIT3 Kits ELISA) in human osteosarcoma cells.
the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD (Montrer MVD Kits ELISA) against PDI (Montrer PADI1 Kits ELISA)-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 (Montrer ADAM17 Kits ELISA) inhibition.
Endoplasmic reticulum resident chaperone GRP78, mitochondrial protein (Montrer COX6B2 Kits ELISA) Prohibitin (Montrer PHB Kits ELISA) and heterogeneous nuclear ribonucleoprotein (Montrer PCBP2 Kits ELISA) hnRNPC (Montrer HNRNPC Kits ELISA) (C1/C2) have been shown to interact with viral RNA. Hence it is proposed that these are the principle candidates governing endoplasmic reticulum stress-induced apoptosis in JEV infection.
We revealed that a small amount of GRP78 effectively inhibited fibrillation of Abeta (Montrer APP Kits ELISA) fragments. Intriguingly, the fibrillation inhibition by GRP78 was confirmed in the absence of ATP, suggesting GRP78 exhibited ATP-independent interaction with Abeta (Montrer APP Kits ELISA) fragments.
Testosterone exposure could deregulate glucose availability by reducing GRP78 protein levels in endometrial stromal cells
Low GRP78 expression is associated with cancer.
This paper reports the localization of both GRP78 and HSP60 (Montrer HSPD1 Kits ELISA) on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 (Montrer HSPD1 Kits ELISA) in the sperm midpiece.
BiP is a master regulator of endoplasmic reticulum function, and its cleavage by subtilase cytotoxin represents a previously unknown trigger for cell death
Over-expression of GRP78 enhances replication of Porcine Circovirus 2.
Data suggest that activation of GRP78/Ire1 (Montrer ERN1 Kits ELISA)/Xbp1 (Montrer XBP1 Kits ELISA) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
Upregulating HSF1 (Montrer HSF1 Kits ELISA) relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (Montrer DDIT3 Kits ELISA) and increasing HSP70 (Montrer HSP70 Kits ELISA) a5 (BiP/GRP78). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 (Montrer HSF1 Kits ELISA) being one likely key player in both systems.
These results demonstrate a key role for GRP78 in alveolar epithelial cell survival.
These results indicate that GRP78, an endoplasmic reticulum chaperon of the HSP70 (Montrer HSP70 Kits ELISA) family, is a novel host factor involved at multiple steps of the Japanese encephalitis virus life cycle and could be a potential therapeutic target.
Genetic or pharmacologic inhibition of the HSPA5-GPX4 pathway enhanced gemcitabine sensitivity by disinhibiting ferroptosis in vitro and in both subcutaneous and orthotopic animal models of PDAC.
The data presented indicate that the unfolded protein response is activated in fibrotic lung tissue and strongly localized to macrophages. GRP78- and CHOP (Montrer DDIT3 Kits ELISA)-mediated macrophage apoptosis was found to protect against bleomycin-induced fibrosis.
Endoplasmic reticulum stress gene GRP78 is involved in signaling pathway during hepatitis B virus-mediated hepatocarcinogenesis.
data show that Med inhibits ER stress-induced apoptosis and promotes osteoblast cell survival by targeting GRP78.
These results suggested the important roles of endoplasmic reticulum-related chaperons, Bip and SIL1 (Montrer SIL1 Kits ELISA), in Alzheimer's disease-like tau hyperphosphorylation.
We show that chronic VPA treatment did not modify the ATXN3 (Montrer ATXN3 Kits ELISA) inclusion load and astrogliosis in affected brain regions However, VPA chronic treatment was able to increase GRP78 protein levels at 30 weeks of age, one of its known neuroprotective effects
Phosphatidylinositol deficient zebrafish have elevated hspa5 expression in the liver and hepatic lipid accumulation due to endoplasmic reticulum stress response.
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.
78 kDa glucose-regulated protein
, heat shock 70 kDa protein 5
, Protein 1603
, 78 kDa glucose-regulated protein homolog
, luminal-binding protein
, glucose-regulated protein 78
, glucose-regulated protein 78kDa
, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
, GRP 78
, heavy-chain binding protein BiP
, immunoglobulin heavy chain-binding protein
, endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
, glucose-regulated protein, 78kDa
, XAP-1 antigen
, glucose regulated protein, 78 kDa
, heat shock 70kD protein 5 (glucose-regulated protein, 78kD)
, heat shock 70kD protein 5
, heat shock 70kDa protein 5 (glucose-regulated protein)
, steroidogenesis-activator polypeptide