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anti-Rat (Rattus) EGLN3 Anticorps:
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Human Polyclonal EGLN3 Primary Antibody pour EM, ICC - ABIN151073
Bai, Zeng, Hu, Li, Lin, Shang, Shi: Expression and characteristic of synthetic human epidermal growth factor (hEGF) in transgenic tobacco plants. dans Biotechnology letters 2007
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Human Polyclonal EGLN3 Primary Antibody pour 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. dans Molecular and cellular biology 2008
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Human Monoclonal EGLN3 Primary Antibody pour 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. dans The Journal of biological chemistry 2012
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Human Polyclonal EGLN3 Primary Antibody pour ELISA, WB - ABIN409073
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. dans The Biochemical journal 2006
comparative analysis of phd1 (Montrer EGLN2 Anticorps), 2, and 3 expression in Xenopus laevis
PHD3 expression induced by cytokines is NF-kappaB (Montrer NFKB1 Anticorps) dependent in mesangial cells. Endogenously produced NO further augments PHD3 expression via HIF-1 alpha (Montrer HIF1A Anticorps).
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 (Montrer ACACB Anticorps).
Our observations disclose a novel role of PHD3 in the development of Tregs.
Epo (Montrer EPO Anticorps) transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 (Montrer EGLN1 Anticorps) and PHD3, oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
deleting Phd1 (Montrer EGLN2 Anticorps)-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 (Montrer OCLN Anticorps)
depletion of PHD3 leads to increased stabilization of HIF-1alpha (Montrer HIF1A Anticorps) and inhibition of DNA damage response, both of which may contribute to the cardioprotective effect seen with depletion of PHD3.
provides a rationale for targeting the PHD3-mediated regulation of the adaptive cellular hypoxic response in MM and suggests that targeting the O2-sensing pathway, alone or in combination with other anti-myeloma chemotherapeutics, may have clinical efficacy
These results indicate that the immunohistochemistry analysis of the protein expression of PDK1 (Montrer PDK1 Anticorps), PHD3, and HIF-1alpha (Montrer HIF1A Anticorps) defines the hypoxic status of Neuroblastoma (Montrer ARHGEF16 Anticorps) tumors.
These findings indicate that downregulation of PHD3 and FIH (Montrer CASR Anticorps) in HCC (Montrer FAM126A Anticorps) 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 (Montrer MCL1 Anticorps) as a novel downstream effector of oxygen sensing
In pancreatic Beta cells, knock-down of PHD3 inhibited glucose-stimulated insulin (Montrer INS Anticorps) 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 (Montrer HIF1A Anticorps).
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 (Montrer PAK2 Anticorps) that occurs by attenuating p27S10 phosphorylation.
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