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anti-Human GRP78 Anticorps:
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Chicken Polyclonal GRP78 Primary Antibody pour FACS, ICC - ABIN446401
Pepping, Freeman, Gupta, Keller, Bruce-Keller: NOX2 deficiency attenuates markers of adiposopathy and brain injury induced by high-fat diet. dans American journal of physiology. Endocrinology and metabolism 2013
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Human Polyclonal GRP78 Primary Antibody pour ICC, IF - ABIN152679
Shin, Feltri, Wrabetz: Altered Trafficking and Processing of GALC Mutants Correlates with Globoid Cell Leukodystrophy Severity. dans The Journal of neuroscience : the official journal of the Society for Neuroscience 2016
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Human Polyclonal GRP78 Primary Antibody pour 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. dans Archives of biochemistry and biophysics 2010
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Human Monoclonal GRP78 Primary Antibody pour IHC, ELISA - ABIN969204
Honda, Horie, Daito, Ikuta, Tomonaga: Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface. dans Journal of virology 2009
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Human Polyclonal GRP78 Primary Antibody pour 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. dans The Journal of biological chemistry 2007
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Human Polyclonal GRP78 Primary Antibody pour ELISA, WB - ABIN561386
Lindenmeyer, Rastaldi, Ikehata, Neusser, Kretzler, Cohen, Schlöndorff: Proteinuria and hyperglycemia induce endoplasmic reticulum stress. dans Journal of the American Society of Nephrology : JASN 2008
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Cow (Bovine) Polyclonal GRP78 Primary Antibody pour 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. dans Molecular and cellular biology 2006
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Dog (Canine) Polyclonal GRP78 Primary Antibody pour ICC, IF - ABIN863190
Cho, Park, Kim, Kim, Kim, Jang: BiP internal ribosomal entry site activity is controlled by heat-induced interaction of NSAP1. dans Molecular and cellular biology 2006
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Chicken Polyclonal GRP78 Primary Antibody pour 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. dans Clinical cancer research : an official journal of the American Association for Cancer Research 2016
Human Polyclonal GRP78 Primary Antibody pour WB - ABIN2801942
Ting, Lee: Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. dans 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.
This meta-analysis shows that BiP (Montrer GDF10 Anticorps) or anti-BiP (Montrer GDF10 Anticorps) 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 (Montrer IL1B Anticorps), MMP14 (Montrer MMP14 Anticorps) 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 (Montrer MLXIP Anticorps)-181a suppressed cervical cancer development via downregulating GRP78.
We revealed that DAL-1 (Montrer EPB41L3 Anticorps) was downregulated while HSPA5 was upregulated in NSCLC and found the protein of DAL-1 (Montrer EPB41L3 Anticorps) and HSPA5 co-localized in the cytoplasm and nucleus. We demonstrated that DAL-1 (Montrer EPB41L3 Anticorps) can suppress the expression of HSPA5 on mRNA and protein levels, and decrease EMT (Montrer ITK Anticorps), migration, invasion and proliferation abilities by down-regulating HSPA5
We found that inhibiting the function of surface GRP78 suppressed cancer cell survival and growth proving that the surface-expressed GRP78 is a vital receptor involved in the proliferation of high-grade glioma.
BiP/GRP78 is significantly associated with tumor aggressiveness and progression. The increased expression of BiP/GRP78 was identified as an independent factor for predicting poor OS in patients with early stage of disease.
GRP78 overexpression decreased advanced glycation end product levels and rescued the cells from Ribosome-induced cytotoxicity.
This study established a macrophage polarization model with human monocytes and found that the conditioned medium from M2 macrophages increased GRP78 expression in tumor cells and facilitated tumor cell migration.
GRP78 silencing promoted lung epithelial cell apoptosis during hyperoxia, via regulation of the CHOP (Montrer DDIT3 Anticorps) pathway.
GRP78 role in dengue virus infection.
This paper reports the localization of both GRP78 and HSP60 (Montrer HSPD1 Anticorps) on the luminal/apical surface of oviduct epithelial cells, their binding to spermatozoa, and the presence of endogenous HSP60 (Montrer HSPD1 Anticorps) 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.
prolonged endoplasmic reticulum stress promotes apoptosis via a p53 (Montrer TP53 Anticorps)-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 (Montrer PTCH1 Anticorps)-mRNA levels during induction of ER stress in vivo.
Data suggest that activation of GRP78/Ire1 (Montrer ERN1 Anticorps)/Xbp1 (Montrer XBP1 Anticorps) pathway of ER stress-unfolded protein response is involved in mouse decidualization.
Upregulating HSF1 (Montrer HSF1 Anticorps) relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (Montrer DDIT3 Anticorps) and increasing HSP70 (Montrer HSP70 Anticorps) 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 Anticorps) 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 Anticorps) 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 Anticorps)-mediated macrophage apoptosis was found to protect against bleomycin-induced fibrosis.
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