Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Human BNIP3 Antikörper:
anti-Mouse (Murine) BNIP3 Antikörper:
anti-Rat (Rattus) BNIP3 Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Human Polyclonal BNIP3 Primary Antibody für IF, IHC (p) - ABIN388117
Kothari, Cizeau, McMillan-Ward, Israels, Bailes, Ens, Kirshenbaum, Gibson: BNIP3 plays a role in hypoxic cell death in human epithelial cells that is inhibited by growth factors EGF and IGF. in Oncogene 2003
Show all 5 Pubmed References
Human Polyclonal BNIP3 Primary Antibody für 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. in The Journal of biological chemistry 2000
Show all 2 Pubmed References
Human Monoclonal BNIP3 Primary Antibody für 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. in EMBO reports 2010
Show all 2 Pubmed References
Human Polyclonal BNIP3 Primary Antibody für WB - ABIN5692799
Du, Li, Xu, Zhou, Zhang, Wang: MicroRNA-145 induces apoptosis of glioma cells by targeting BNIP3 and Notch signaling. in Oncotarget 2017
Human Polyclonal BNIP3 Primary Antibody für 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. in American journal of physiology. Lung cellular and molecular physiology 2009
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.
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.
High BNIP3 expression is associated with chronic myelogenous leukemia.
Results suggest that changes in mitochondrial morphology and transmembrane potential, induced by mutant htt protein, are dependent and linked to BNip3 and not to Bax/Bak activation.
Hypoxia-induced autophagy contributes to the invasion of salivary adenoid cystic carcinoma through the HIF-1alpha/BNIP3 signaling pathway.
The data indicated that BNIP3 plays a vital role in the tumorigenesis of adenoid cystic carcinoma and could be a new target for gene therapy of adenoid cystic carcinoma.
BNIP3 deletion can be used as a prognostic marker of tumor progression to metastasis in human triple-negative breast cancer
BNIP3 expression was found to be regulated by Sp3 in prostate cancer.
phosphorylation of these C-terminal BNIP3 residues blocks cell death without preventing autophagy, providing evidence that the two functional roles of BNIP3 can be regulated independently
Bnip3 dual-functionality and crosstalk between mitophagy and apoptosis pathways is presented here.
these findings revealed that silibinin induced autophagic cell death through ROS-dependent mitochondrial dysfunction and ATP depletion involving BNIP3 in MCF7 cells.
The findings of the present study reveal a novel survival pathway that functionally couples the unique glycolytic phenotype in cancer cells to hypoxia resistance via a PDK2-dependent mechanism that switches Bnip3 from cell death to survival.
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.
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.
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
The BNIP3 cell death pathway may be a new target for protecting oligodendrocytes from death after stroke
Bnip3 is a required downstream effector of FoxO-driven autophagic flux in mechanically unloaded failing myocardium.
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