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anti-Human GRP78 Antibodies:
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Chicken Polyclonal GRP78 Primary Antibody for FACS, ICC - ABIN446401
Pepping, Freeman, Gupta, Keller, Bruce-Keller: NOX2 deficiency attenuates markers of adiposopathy and brain injury induced by high-fat diet. in American journal of physiology. Endocrinology and metabolism 2013
Show all 14 Pubmed References
Human Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN152679
Shin, Feltri, Wrabetz: Altered Trafficking and Processing of GALC Mutants Correlates with Globoid Cell Leukodystrophy Severity. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2016
Show all 4 Pubmed References
Human Monoclonal GRP78 Primary Antibody for IHC, ELISA - ABIN969204
Honda, Horie, Daito, Ikuta, Tomonaga: Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface. in Journal of virology 2009
Show all 4 Pubmed References
Human Polyclonal GRP78 Primary Antibody for IF (cc), IF (p) - ABIN673554
Du, Zhou, Jia, Huang: SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis. in Archives of biochemistry and biophysics 2010
Show all 3 Pubmed References
Human Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN4316288
Sharma, Masri, Jo, Bernath, Martin, Funk, Gera: Protein kinase C regulates internal initiation of translation of the GATA-4 mRNA following vasopressin-induced hypertrophy of cardiac myocytes. in The Journal of biological chemistry 2007
Show all 3 Pubmed References
Cow (Bovine) Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN361825
Luo, Mao, Lee, Lee: GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. in Molecular and cellular biology 2006
Show all 10 Pubmed References
Dog (Canine) Polyclonal GRP78 Primary Antibody for ICC, IF - ABIN863190
Cho, Park, Kim, Kim, Kim, Jang: BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1. in Molecular and cellular biology 2006
Show all 9 Pubmed References
Human Polyclonal GRP78 Primary Antibody for ELISA, WB - ABIN561386
Lindenmeyer, Rastaldi, Ikehata, Neusser, Kretzler, Cohen, Schlöndorff: Proteinuria and hyperglycemia induce endoplasmic reticulum stress. in Journal of the American Society of Nephrology : JASN 2008
Show all 2 Pubmed References
Chicken Polyclonal GRP78 Primary Antibody for FACS, ICC - ABIN446404
Rasche, Menoret, Dubljevic, Menu, Vanderkerken, Lapa, Steinbrunn, Chatterjee, Knop, Düll, Greenwood, Hensel, Rosenwald, Einsele, Brändlein: A GRP78-Directed Monoclonal Antibody Recaptures Response in Refractory Multiple Myeloma with Extramedullary Involvement. in Clinical cancer research : an official journal of the American Association for Cancer Research 2016
Human Polyclonal GRP78 Primary Antibody for WB - ABIN2801942
Ting, Lee: Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. in DNA (Mary Ann Liebert, Inc.) 1988
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.
Cancer-associated fibroblasts induced GRP78 expression in A549 and SPCA-1 (show ATP2C1 Antibodies) cells to facilitate Non-Small Cell Lung Cancer cell migration and invasion
results suggest that the cooperative effects of radiotherapy and cetuximab could be further improved by inhibiting GRP78 in non-responsive oropharyngeal carcinoma patients
Study reports that the endoplasmic reticulum luminal co-chaperone ERdj4/DNAJB9 (show DNAJB9 Antibodies) is a selective IRE1 (show ERN1 Antibodies) repressor that promotes a complex between the luminal Hsp70 (show HSP70 Antibodies) BiP (show GDF10 Antibodies) and the luminal stress-sensing domain of IRE1alpha (show ERN1 Antibodies).
GRP78 role in the resistance to cisplatin in the nasopharyngeal carcinoma cells.
High expression of GRP78 is associated with nonalcoholic steatohepatitis.
Data show that cancer-associated fibroblasts (CAFs (show TBX1 Antibodies))-derived hepatocyte growth factor (HGF (show HGF Antibodies)) or recombinant HGF (show HGF Antibodies) activated c-Met/phosphoinositide 3-kinase (PI3K (show PIK3CA Antibodies))/Akt (show AKT1 Antibodies) 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 (show STAT3 Antibodies), GRP78 and BAX (show BAX Antibodies) protein levels in the combination group were significantly higher than those in STAT3 (show STAT3 Antibodies) group and CDDP group (P<0.05). Exogenous STAT3 (show STAT3 Antibodies) and CDDP may synergistically inhibit the xenograft tumour growth through up-regulation of BAX (show BAX Antibodies) protein via GRP78.
GRP78 inhibition enhances ATF4 (show ATF4 Antibodies)-induced cell death by the deubiquitination and stabilization of CHOP (show DDIT3 Antibodies) in human osteosarcoma cells.
the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD (show MVD Antibodies) against PDI (show PADI1 Antibodies)-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 (show ADAM17 Antibodies) inhibition.
This paper reports the localization of both GRP78 and HSP60 (show HSPD1 Antibodies) on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 (show HSPD1 Antibodies) 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.
These results indicate that GRP78, but not nutritional status, is a potent up-regulator of hepatic PTC (show PTCH1 Antibodies)-mRNA levels during induction of ER stress in vivo.
Data suggest that activation of GRP78/Ire1 (show ERN1 Antibodies)/Xbp1 (show XBP1 Antibodies) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
Upregulating HSF1 (show HSF1 Antibodies) relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (show DDIT3 Antibodies) and increasing HSP70 (show HSP70 Antibodies) 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 Antibodies) 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 Antibodies) 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 (show DDIT3 Antibodies)-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 (show SIL1 Antibodies), in Alzheimer's disease-like tau hyperphosphorylation.
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