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Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Additionally we are shipping EGLN3 Proteins (8) and many more products for this protein.
Showing 10 out of 137 products:
Human Polyclonal EGLN3 Primary Antibody for EM, ICC - ABIN151073
Bai, Zeng, Hu, Li, Lin, Shang, Shi: Expression and characteristic of synthetic human epidermal growth factor (hEGF) in transgenic tobacco plants. in Biotechnology letters 2007
Show all 34 references for ABIN151073
Human Polyclonal EGLN3 Primary Antibody for ChIP, ICC - ABIN151769
Mikhaylova, Ignacak, Barankiewicz, Harbaugh, Yi, Maxwell, Schneider, Van Geyte, Carmeliet, Revelo, Wyder, Greis, Meller, Czyzyk-Krzeska: The von Hippel-Lindau tumor suppressor protein and Egl-9-Type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress. in Molecular and cellular biology 2008
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Human Monoclonal EGLN3 Primary Antibody for IHC, IHC (p) - ABIN447479
Fujita, Gogate, Chiba, Toyama, Shapiro, Risbud: Prolyl hydroxylase 3 (PHD3) modulates catabolic effects of tumor necrosis factor-α (TNF-α) on cells of the nucleus pulposus through co-activation of nuclear factor κB (NF-κB)/p65 signaling. in The Journal of biological chemistry 2012
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Human Polyclonal EGLN3 Primary Antibody for IHC (p), WB - ABIN658142
Sato, Sakota, Nakayama: Human PRP19 interacts with prolyl-hydroxylase PHD3 and inhibits cell death in hypoxia. in Experimental cell research 2010
Show all 3 references for ABIN658142
Chicken Polyclonal EGLN3 Primary Antibody for WB - ABIN2784911
Ginouvès, Ilc, Macías, Pouysségur, Berra: PHDs overactivation during chronic hypoxia "desensitizes" HIFalpha and protects cells from necrosis. in Proceedings of the National Academy of Sciences of the United States of America 2008
Human Polyclonal EGLN3 Primary Antibody for ELISA, WB - ABIN302149
Nakayama, Gazdoiu, Abraham, Pan, Ronai: Hypoxia-induced assembly of prolyl hydroxylase PHD3 into complexes: implications for its activity and susceptibility for degradation by the E3 ligase Siah2. in The Biochemical journal 2006
comparative analysis of phd1 (show EGLN2 Antibodies), 2, and 3 expression in Xenopus laevis
PHD3 is an active participant in atherogenesis
Cardiomyocyte-specific transgenic expression of PHD3 impairs the myocardial response to ischemia.
PHD3 protects intestinal epithelial barrier function and reveal a hydroxylase-independent function of PHD3 in stabilizing occludin (show OCLN Antibodies)
depletion of PHD3 leads to increased stabilization of HIF-1alpha (show HIF1A Antibodies) and inhibition of DNA damage response, both of which may contribute to the cardioprotective effect seen with depletion of PHD3.
PHD3 loss sustains cell proliferation through the control of EGFR (show EGFR Antibodies).
combined deletion of Phd2 (show EGLN1 Antibodies) and Phd3 dramatically decreased expression of phospholamban (PLN (show PLN Antibodies)), resulted in sustained activation of calcium/calmodulin (show Calm2 Antibodies)-activated kinase II (CaMKII (show CAMK2G Antibodies)), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury
PHD1 (show EGLN2 Antibodies) and PHD3 deletions promote angiogenesis in ischemia-injured tissue by increasing HIF1-alpha (show HIF1A Antibodies) stability.
Using conditional PHD3-knockout mice, it was shown that PHD3 affects the production of Angptl2 (show ANGPTL2 Antibodies) and additionally influences the response toward this apoptosis-modulating factor.
ablation of the PHD3 gene resulted in increased angiogenesis and cardiac function after infarction thereby offering a potential target for management of ischemic myocardial disease
PHD3 depletion did not affect the expression of the PDH (show PDP Antibodies)-E1alpha, E1beta (show PDHB Antibodies), and E2 subunits, or the phosphorylation status of E1alpha, but destabilized the PDH (show PDP Antibodies) complex (PDC (show PDC Antibodies)), resulting in less functional PDC (show PDC Antibodies).
In pancreatic Beta cells, knock-down of PHD3 inhibited glucose-stimulated insulin (show INS Antibodies) secretion.
Loss of PHD3 expression is associated with breast cancer.
The selective efficacy of PZ was further demonstrated at the cellular level by observing inhibition of the PHD3-dependent DNA damage response pathway without stabilization of HIF-1alpha (show HIF1A Antibodies).
The enhanced expression of PHD3 might likely contribute to the poor neovascularization and affect the biological characterization in PDAC cancer cells
The data demonstrates that PHD3 can drive cell cycle entry at the G1/S transition through decreasing the half-life of p27 (show PAK2 Antibodies) that occurs by attenuating p27S10 phosphorylation.
PHD3 controls EGFR (show EGFR Antibodies) activity by acting as a scaffolding protein that associates with the endocytic adaptor Eps15 (show EPS15 Antibodies) and promotes the internalization of EGFR (show EGFR Antibodies).
PHD3 SUMOylation occurs at a cluster of four lysines at the C-terminal end of the protein. Furthermore, PHD3 SUMOylation by SUMO2 (show SUMO2 Antibodies) or SUMO3 (show SUMO3 Antibodies) contributes to PHD3-mediated repression of HIF1 (show HIF1A Antibodies)-dependent transcriptional activity.
HIFPH3 expression in human non-small cell lung cancer lesions is significantly higher than that in para-cancerous and normal lung tissues and is positively associated with lymph node metastasis and microvessel density.
A novel role for PHD3 as a negative regulator of cell motility through posttranslational modification of nonmuscle actins.
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM2 in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurones, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation.
, egl nine homolog 3
, egl nine homolog 3 (C. elegans)
, HIF-prolyl hydroxylase 3
, egl nine homolog 3, mitochondrial
, factor-responsive smooth muscle protein
, hypoxia-inducible factor prolyl hydroxylase 3
, prolyl hydroxylase domain-containing protein 3
, HIF prolyl hydroxylase 3
, egl nine-like protein 3 isoform