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Egl nine

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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. 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 HIF1B. 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. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.

Below are the list of possible Egl nine products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

Egl nine homolog 1

 Egl nine homolog 1 ELISA Kit
 Egl nine homolog 1 Recombinant
 Egl nine homolog 1 Antibody
Also known as Egl nine homolog 1 (Hypoxia-inducible factor prolyl hydroxylase 2) (HIF-PH2) (HIF-prolyl hydroxylase 2) (HPH-2) (Prolyl hydroxylase domain-containing protein 2) (PHD2).
EGLN1: 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
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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 HIF1B. 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. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Monomer. Interacts with ING4; the interaction inhibits the hydroxylation of HIFs. Interacts with LIMD1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with EPAS1. According to PubMed:11056053, widely expressed with highest levels in skeletal muscle and heart, moderate levels in pancreas, brain (dopaminergic neurons of adult and fetal substantia nigra) and kidney, and lower levels in lung and liver. According to PubMed:12351678 widely expressed with highest levels in brain, kidney and adrenal gland. Expressed in cardiac myocytes, aortic endothelial cells and coronary artery smooth muscle. According to PubMed:12788921; expressed in adult and fetal heart, brain, liver, lung, skeletal muscle and kidney. Also expressed in placenta. Highest levels in adult heart, brain, lung and liver and fetal brain, heart spleen and skeletal muscle. Following exposure to hypoxia, activated in HeLa cells but not in cardiovascular cells. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 1.14.11.29; Oxidoreductase

Cellular Component: cytoplasm; cytosol

Molecular Function: enzyme binding; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; peptidyl-proline 4-dioxygenase activity; peptidyl-proline dioxygenase activity

Biological Process: cardiac muscle morphogensis; cellular iron ion homeostasis; negative regulation of cAMP catabolic process; negative regulation of cyclic-nucleotide phosphodiesterase activity; negative regulation of transcription factor activity; oxygen homeostasis; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; positive regulation of apoptosis; positive regulation of transcription from RNA polymerase II promoter; regulation of angiogenesis; response to hypoxia
 Egln1 ELISA Kit
 Egln1 Recombinant
 Egln1 Antibody
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Egl nine homolog 2

 Egl nine homolog 2 ELISA Kit
 Egl nine homolog 2 Recombinant
 Egl nine homolog 2 Antibody
Also known as Egl nine homolog 2 (Estrogen-induced tag 6) (HPH-3) (Hypoxia-inducible factor prolyl hydroxylase 1) (HIF-PH1) (HIF-prolyl hydroxylase 1) (HPH-1) (Prolyl hydroxylase domain-containing protein 1) (PHD1).
EGLN2: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydro
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xylates 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. 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. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. 2 isoforms of the human protein are produced by alternative initiation.

Protein type: EC 1.14.11.29; Oxidoreductase

Chromosomal Location of Human Ortholog: 19q13.2

Cellular Component: nucleoplasm; nucleus

Molecular Function: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; oxygen sensor activity; peptidyl-proline 4-dioxygenase activity; protein binding

Biological Process: cell redox homeostasis; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; positive regulation of protein catabolic process; regulation of neuron apoptosis; response to hypoxia
 EGLN2 ELISA Kit
 EGLN2 Recombinant
 EGLN2 Antibody
 EIT6 ELISA Kit
 EIT6 Recombinant
 EIT6 Antibody
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Egl nine homolog 3

 Egl nine homolog 3 ELISA Kit
 Egl nine homolog 3 Recombinant
 Egl nine homolog 3 Antibody
Also known as Egl nine homolog 3 (HPH-1) (Hypoxia-inducible factor prolyl hydroxylase 3) (HIF-PH3) (HIF-prolyl hydroxylase 3) (HPH-3) (Prolyl hydroxylase domain-containing protein 3) (PHD3).
EGLN3: 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 prolin
>>>
e 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. EGLN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM 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 neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation.

Protein type: EC 1.14.11.29; Oxidoreductase

Chromosomal Location of Human Ortholog: 14q13.1

Cellular Component: cytoplasm; cytosol; nucleoplasm; nucleus

Molecular Function: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; peptidyl-proline 4-dioxygenase activity; protein binding

Biological Process: apoptosis; caspase activation; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; protein amino acid hydroxylation; regulation of cell proliferation; regulation of neuron apoptosis; response to hypoxia
 EGLN3 ELISA Kit
 EGLN3 Recombinant
 EGLN3 Antibody
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