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comparative analysis of phd1 (show EGLN2 ELISA Kits), 2, and 3 expression in Xenopus laevis
Opposing regulation and roles for PHD3 in lung dendritic cells and alveolar macrophages
PHD3 loss in cancer enables metabolic reliance on fatty acid oxidation via deactivation of ACC2 (show ACACB ELISA Kits).
Our observations disclose a novel role of PHD3 in the development of Tregs.
Epo (show EPO ELISA Kits) transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 (show EGLN1 ELISA Kits) and PHD3, oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
deleting Phd1 (show EGLN2 ELISA Kits)-3 genes in osteoblasts increased osteoclast formation in vitro and in bone.
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 ELISA Kits)
depletion of PHD3 leads to increased stabilization of HIF-1alpha (show HIF1A ELISA Kits) 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 ELISA Kits).
These findings indicate that downregulation of PHD3 and FIH (show CASR ELISA Kits) in HCC (show FAM126A ELISA Kits) is associated with more aggressive tumor behavior and a poor prognosis in hepatocellular carcinoma
demonstrate that downregulation of PHD3 augments metastatic spread in human colorectal cancer and identify MCL-1 (show MCL1 ELISA Kits) as a novel downstream effector of oxygen sensing
In pancreatic Beta cells, knock-down of PHD3 inhibited glucose-stimulated insulin (show INS ELISA Kits) 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 ELISA Kits).
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 ELISA Kits) that occurs by attenuating p27S10 phosphorylation.
PHD3 controls EGFR (show EGFR ELISA Kits) activity by acting as a scaffolding protein that associates with the endocytic adaptor Eps15 (show EPS15 ELISA Kits) and promotes the internalization of EGFR (show EGFR ELISA Kits).
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