Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species
the results suggest that BNIP3 plays a vital role in regulating PINK1 mitochondrial outer membrane localization, the proteolytic process of PINK1 and PINK1/parkin (show PARK2 ELISA Kits)-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 (show HTT ELISA Kits) protein, are dependent and linked to BNip3 and not to Bax (show BAX ELISA Kits)/Bak (show BAK1 ELISA Kits) activation.
Hypoxia-induced autophagy contributes to the invasion of salivary adenoid cystic carcinoma through the HIF-1alpha (show HIF1A ELISA Kits)/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 (show HIF1A ELISA Kits)marker of tumor progression to metastasis in human triple-negative breast cancer
BNIP3 expression was found to be regulated by Sp3 (show SP3 ELISA Kits) 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 (show ROS1 ELISA Kits)-dependent mitochondrial dysfunction and ATP depletion involving BNIP3 in MCF7 cells.
Down-regulation of Bcl2/adenovirus E1B 19-kDa-interacting protein 3 (BNIP3) by olomoucine, a cyclin (show PCNA ELISA Kits)-dependent kinasesinhibitor, reduces lipopolysaccharide - and nitric oxide-induced cell death in BV2 (show DNAH9 ELISA Kits) microglial cells. Olomoucine may protect cells by limiting proinflammatory responses, thereby reducing nitric oxide generation.
data outline Bnip3 as a key effector of PPARgamma (show PPARG ELISA Kits)-mediated adipose mitochondrial network fragmentation, improving insulin (show INS ELISA Kits) sensitivity and limiting oxidative stress.
BNIP3 interacts with the mitochondrial outer membrane directly via mitochondrial BAX (show BAX ELISA Kits).
Data show that TGFbeta (show TGFB1 ELISA Kits)-activated kinase-1 (TAK1 (show NR2C2 ELISA Kits)) activated nuclear factor of activated T-cells (NFAT (show NFATC1 ELISA Kits))/NF-kappa B (NFkappaB (show NFKB1 ELISA Kits)), downregulated BCL2-adenovirus E1B interacting protein 3 (Bnip3), and inhibited cardiac cell death.
propose that BNIP3 acts as a brake on HIF-1 (show HIF1A ELISA Kits) activity serving to increase rates of mitophagy in response to hypoxia and to limit production of damaging ROS (show ROS1 ELISA Kits) that would further amplify HIF-1 (show HIF1A ELISA Kits) 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 (show BNIP3L ELISA Kits) is required for mitophagy during development of the erythroid lineage.
BNIP3 primarily regulates basal level of mitophagy in physiological conditions, whereas BNIP3 exclusively activates excessive mitophagy leading to cell death.
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