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Human GRP78 Protein expressed in Escherichia coli (E. coli) - ABIN1686700
Yang, Turner, Gaut: The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. in The Journal of biological chemistry 1998
Show all 10 Pubmed References
Human GRP78 Protein expressed in Escherichia coli (E. coli) - ABIN1686682
Rechthand, Smith, Latker, Rapoport: Altered blood-nerve barrier permeability to small molecules in experimental diabetes mellitus. in Journal of neuropathology and experimental neurology 1987
Show all 9 Pubmed References
Human GRP78 Protein expressed in Wheat germ - ABIN1307202
Taylor, Gercel-Taylor, Parker: Patient-derived tumor-reactive antibodies as diagnostic markers for ovarian cancer. in Gynecologic oncology 2009
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.
Concomitant high expression of ERalpha36, GRP78 and GRP94 (show HSP90B1 Proteins) is associated with aggressive papillary thyroid cancer behavior and may be used as a predictor for extrathyroid extension, lymph node metastasis, and distant metastasis.
We found that downregulation of GRP78 led to inhibition of autophagy, cell cycle arrest in the G0/G1 phase, and activation of caspase-7 (show CASP7 Proteins)-induced apoptosis, and this was affected by the initial autophagy level.
GRP78 promotes cigarette smoke-induced inflammatory response and mucus hyperproduction in airway epithelial cells, likely through upregulation of necroptosis and subsequent activation of NF-kappaB (show NFKB1 Proteins) and AP-1 (show FOSB Proteins) pathways.
Data suggested that GRP78 silencing increased chemo-sensitivity and improved the effects of cisplatin-induced apoptosis in SiHa cells. Moreover, inhibition of GRP78 could upregulate caspase-3 (show CASP3 Proteins) and CHOP (show DDIT3 Proteins) expression and downregulate Bcl-2 (show BCL2 Proteins) expression.
Upon IgM expression, its levels temporarily eclipse those of the endoplasmic reticulum chaperone BiP (show GDF10 Proteins), leading to acute, full-geared unfolded protein response activation. Once BiP (show GDF10 Proteins) is in excess (show RCC1 Proteins) again, the unfolded protein response transitions to chronic, submaximal activation, indicating that the unfolded protein response senses endoplasmic reticulum stress in a ratiometric fashion.
GRP78 binds to and acts in concert with a glycosylphosphatidylinositol-anchored protein, CD109 (show CD109 Proteins), in blocking TGF-beta (show TGFB1 Proteins) signaling by promoting the routing of the TGF-beta (show TGFB1 Proteins) receptor to the caveolae, thereby disrupting its binding to and activation of Smad2 (show SMAD2 Proteins).
this study demonstrates the reaction of placental GRP78 with sera from women with multiple sclerosis
This meta-analysis shows that BiP (show GDF10 Proteins) or anti-BiP (show GDF10 Proteins) antibodies have a moderate accuracy for the diagnosis of rheumatoid arthritis with a moderate sensitivity and high specificity. It can be an efficient supplement to the existing diagnostic method. [Meta-Analysis]
the expression of three cytokines for the pathogenesis of osteoarthritis (OA). which include IL-1beta (show IL1B Proteins), MMP14 (show MMP14 Proteins) and GRP78 was decreased by the various concentrations of icariin. These preliminary results imply that icariin might be an effective compound for the treatment of OA disease.
In a retrospective cervical cancer cohort, high GRP78 expression was correlated with poor survival. miR (show MLXIP Proteins)-181a suppressed cervical cancer development via downregulating GRP78.
This paper reports the localization of both GRP78 and HSP60 (show HSPD1 Proteins) on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 (show HSPD1 Proteins) 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.
GRP78 promotes cigarette smoke-induced inflammatory response and mucus hyperproduction in airway epithelial cells, likely through upregulation of necroptosis and subsequent activation of NF-kappaB (show NFKB1 Proteins) and AP-1 (show JUN Proteins) pathways.
siRNA of Grp78 disturbed the fusion of mouse palate cultured in vitro, suggesting a role in the palate development during embryogenesis..
prolonged endoplasmic reticulum stress promotes apoptosis via a p53 (show TP53 Proteins)-dependent inhibition of BiP expression
analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma
candidate genes that modulate Hspa5 expression in the retina, were examined.
These results indicate that GRP78, but not nutritional status, is a potent up-regulator of hepatic PTC (show PTCH1 Proteins)-mRNA levels during induction of ER stress in vivo.
Data suggest that activation of GRP78/Ire1 (show ERN1 Proteins)/Xbp1 (show XBP1 Proteins) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
Upregulating HSF1 (show HSF1 Proteins) relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (show DDIT3 Proteins) and increasing HSP70 (show HSP70 Proteins) a5 (BiP/GRP78). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 (show HSF1 Proteins) 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 (show HSP70 Proteins) family, is a novel host factor involved at multiple steps of the Japanese encephalitis virus life cycle and could be a potential therapeutic target.
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