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anti-Human BNIP3 Anticorps:
anti-Mouse (Murine) BNIP3 Anticorps:
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Human Polyclonal BNIP3 Primary Antibody pour WB - ABIN548542
Ray, Chen, Vande Velde, Cizeau, Park, Reed, Gietz, Greenberg: BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites. dans The Journal of biological chemistry 2000
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Human Monoclonal BNIP3 Primary Antibody pour ICC, IF - ABIN151087
Landes, Emorine, Courilleau, Rojo, Belenguer, Arnauné-Pelloquin: The BH3-only Bnip3 binds to the dynamin Opa1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms. dans EMBO reports 2010
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Human Polyclonal BNIP3 Primary Antibody pour IHC, WB - ABIN6677247
Chen, Li, Li, Feng, Liu, Wang, Dai, Xia, Lu, Zhou, Guo: 15-Deoxy-Δ12,14-prostaglandin J2 alleviates hepatic ischemia-reperfusion injury in mice via inducing antioxidant response and inhibiting apoptosis and autophagy. dans Acta pharmacologica Sinica 2018
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Human Polyclonal BNIP3 Primary Antibody pour IHC, WB - ABIN6137620
Zhang, Liu, Xue, Ma, Liu, Li, Li, Liu: Endothelial Monocyte-Activating Polypeptide-II Induces BNIP3-Mediated Mitophagy to Enhance Temozolomide Cytotoxicity of Glioma Stem Cells via Down-Regulating MiR-24-3p. dans Frontiers in molecular neuroscience 2018
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Human Polyclonal BNIP3 Primary Antibody pour ICC, IF - ABIN4284980
Yang, Yang, Guo, Williams, Weissler: PLAGL2 expression-induced lung epithelium damages at bronchiolar alveolar duct junction in emphysema: bNip3- and SP-C-associated cell death/injury activity. dans American journal of physiology. Lung cellular and molecular physiology 2009
Human Polyclonal BNIP3 Primary Antibody pour WB - ABIN5692799
Du, Li, Xu, Zhou, Zhang, Wang: MicroRNA-145 induces apoptosis of glioma cells by targeting BNIP3 and Notch signaling. dans Oncotarget 2017
Human Polyclonal BNIP3 Primary Antibody pour IHC - ABIN6713282
Li, Yan, Li, Sun, Hu, Sun, Xu: MicroRNA-145 protects cardiomyocytes against hydrogen peroxide (H₂O₂)-induced apoptosis through targeting the mitochondria apoptotic pathway. dans PLoS ONE 2013
These results suggest that MAC induces autophagy via the AMPK/mTOR signalling pathway and by upregulating HIF-1alpha and BNIP3 protein expression in lung cancer cells
BNIP3 role in the mitophagy in the radiation resistant cancer.
BNIP3 silencing reduced glutamine-mediated effects on melanoma cell growth, migration and bioenergetics
mRNA expression of BNIP3 and p53 was significantly increased in cells from diabetes mellitus pregnancies but not in cells from normoglycemic pregnancies.
Low BNIP3 expression is associated with breast tumor progression.
BNIP3 was involved in the apoptosis of cells undergoing hypoxic-ischemic encephalopathy. The HRE site of BNIP3 promoter bound HIF to promote its transcription.
Histone deacetylation may be the important mechanism of BNIP3 silencing in renal cell carcinoma
the comprehensive role of Mst1 in colorectal cancer stress response involving apoptosis, mobilization, and growth via handling mitophagy by JNK/p53/Bnip3 pathways, is reported.
findings uncovered the mechanistic basis for differential HIF-1alpha-mediated regulation of BNIP3 and IGF2, indicating that copper regulates target gene selectivity of HIF-1alpha at least in part by affecting HIF-1alpha binding to its cognate HRE in the promoters of these two genes
Results found lower levels of BNIP3 expression in clear cell renal cell carcinomas (ccRCCs) tissues and suggest that histone deacetylation, but not methylation, is most likely to cause BNIP3 inactivation in ccRCC.
A new function for BNIP3 in the regulation of cellular proliferation.
BNIP3 was mainly localized in the cytoplasm, and high expression of BNIP3 accounted for 31.9% (15/47) of the uveal melanoma patients in our study. High expression of BNIP3 was demonstrated to be significantly associated with more pigment (P=0.018) and deeper scleral invasion (P=0.013).
lncRNA HULC up-regulated BNIP3.
TUG1 overexpression aggravates hypoxia injury of cardiomyocytes by regulating miR-145-5p-Bnip3 axis to activate Wnt/beta-catenin pathways.
In ESCC cells, although BNIP3-induced autophagy is protective, BNIP3 exerts a pro-death function under hypoxia.
Silencing of BNIP3 suppressed free fatty acid synthesis in mesenchymal stem cells. BNIP3 induction by hypoxia stimulates FASN-dependent free fatty acid production.
Apoptosis, but not autophagy, that is induced via p21-activated BNIP3 expression accounts for the efficacy of ICMT inhibition in sensitive pancreatic cancer cells in both in vitro and in vivo models. In contrast, cells resistant to ICMT inhibition demonstrated no mitochondria dysfunction or p21 signaling changes under ICMT suppression
BNIP3 is a significant contributor to the pathogenesis of inflammation-induced heart failure pathologies [review]
The authors find that KDM3A promotes anoikis through transcriptional activation of BNIP3 and BNIP3L, which encode pro-apoptotic proteins.
This study showed that hepatic mitochondrial adaptations to physical activity are more dependent on sex than PGC1alpha and BNIP3.
aberrant accumulation of mitochondria in Neuro-2a cells may be attributed to insufficient BNIP3-mediated mitophagy due to poor interaction between BNIP3 and LC3-II. ... our data indicated for the first time that impaired autophagy degradation and inefficient BNIP3-mediated mitophagy may constitute mechanisms underlying neuronal cell damage during chronic hypoxia.
High-fat-mediated liver damage is associated with Sirt3 downregulation, which is followed by ERK-CREB pathway inactivation and Bnip3-mediated inhibition of mitophagy, causing hepatocytes to undergo mitochondria-dependent cell death.
JNK activates Mff and Bnip3, contributing to the fatal mitochondrial fission and mitophagy, respectively.
BNIP3 expression was upregulated in hypoxic keratinocytes, and BNIP3 silencing suppressed hypoxia-induced cell migration.
In a neuronal model of dominant optic atrophy, BNIP3 down-regulation reduced autophagy and mitophagy.
Down-regulation of Bcl2/adenovirus E1B 19-kDa-interacting protein 3 (BNIP3) by olomoucine, a cyclin-dependent kinasesinhibitor, reduces lipopolysaccharide - and nitric oxide-induced cell death in BV2 microglial cells. Olomoucine may protect cells by limiting proinflammatory responses, thereby reducing nitric oxide generation.
data outline Bnip3 as a key effector of PPARgamma-mediated adipose mitochondrial network fragmentation, improving insulin sensitivity and limiting oxidative stress.
the results suggest that BNIP3 plays a vital role in regulating PINK1 mitochondrial outer membrane localization, the proteolytic process of PINK1 and PINK1/parkin-mediated mitophagy under physiological conditions.
BNIP3 interacts with the mitochondrial outer membrane directly via mitochondrial BAX.
Data show that TGFbeta-activated kinase-1 (TAK1) activated nuclear factor of activated T-cells (NFAT)/NF-kappa B (NFkappaB), downregulated BCL2-adenovirus E1B interacting protein 3 (Bnip3), and inhibited cardiac cell death.
propose that BNIP3 acts as a brake on HIF-1 activity serving to increase rates of mitophagy in response to hypoxia and to limit production of damaging ROS that would further amplify HIF-1 expression and promote tumor progression to metastasis
Results suggest that Bnip3 regulates cardiac gene expression and perhaps myocyte morphology by activating nuclear p300 acetyltransferase and hyperacetylating histones and its selective transcription factors.
Bnip3 dual-functionality and crosstalk between mitophagy and apoptosis pathways is presented here.
regulates mitophagy during hypoxia, whereas NIX is required for mitophagy during development of the erythroid lineage.
role in the generation of robust NK cell memory in the process of mitophagy during viral infection
BNIP3 primarily regulates basal level of mitophagy in physiological conditions, whereas BNIP3 exclusively activates excessive mitophagy leading to cell death.
Bnip3 generation, mediated by PARP1, causes mitochondrial damage and neuron death.
Suggest pro-tumorigenic role of BNIP3 driving melanoma cell's aggressive features, like migration and vasculogenic mimicry.
BNIP3 has a protective effect against UVB-induced apoptosis in keratinocytes
This gene is a member of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. It interacts with the E1B 19 kDa protein, which protects cells from virally-induced cell death. The encoded protein also interacts with E1B 19 kDa-like sequences of BCL2, another apoptotic protector. This protein contains a BH3 domain and a transmembrane domain, which have been associated with pro-apoptotic function. The dimeric mitochondrial protein encoded by this gene is known to induce apoptosis, even in the presence of BCL2.
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
, BCL2/adenovirus E1B 19kD-interacting protein 3
, BCL2/adenovirus E1B 19 kDa-interacting protein 1, NIP3
, BCL2/adenovirus E1B 19kDa-interacting protein 1, NIP3
, BCL2/adenovirus E1B interacting protein 1, NIP3
, BCL2/adenovirus E1B 19 kDa-interacting protein 3