Rabbit EGLN1 Polyclonal Antibody | anti-EGLN1 antibody

EGLN1 Conjugated Antibody

Cat. Num. AAA9443332

• Gene Names: EGLN1; HPH2; PHD2; SM20; ECYT3; HALAH; HPH-2; HIFPH2; ZMYND6; C1orf12; HIF-PH2
• Reactivity: Human, Mouse, Rat
• Applications: Most Applications
• Synonyms: EGLN1; Polyclonal Antibody; EGLN1 Conjugated Antibody; C1orf12; DKFZp761F179; ECYT3; HIFPH2; anti-EGLN1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Specificity: The antibody detects endogenous level of total EGLN1 protein.
• Form/Format: 0.01M Sodium Phosphate, 0.25M NaCl, pH 7.6, 5mg/ml Bovine Serum Albumin, 0.02% Sodium Azide

• Applicable Applications for anti-EGLN1 antibody: Most Applications
• Application Notes: Suggested Dilution:; AF350 conjugated: most applications: 1:50-1:250; AF405 conjugated: most applications: 1:50-1:250; AF488 conjugated: most applications: 1:50-1:250; AF555 conjugated: most applications: 1:50-1:250; AF594 conjugated: most applications: 1:50-1:250; AF647 conjugated: most applications: 1:50-1:250; AF680 conjugated: most applications: 1:50-1:250; AF750 conjugated: most applications: 1:50-1:250; Biotin conjugated: working with enzyme-conjugated streptavidin, most applications: 1:50-1:1000
• Immunogen: Recombinant protein of human EGLN1.
• Conjugation: Biotin AF350 AF405 AF488 AF555 AF594 AF647 AF680 AF750
• Excitation Emission: AF350: 346nm/442nm
• Preparation and Storage: Store at 4 degree C for 6 months.

Related Product Information for anti-EGLN1 antibody

PHD1 (Egln2), PHD-2 (Egln1), and PHD3 (Egln3) are members of the Egln family of proline hydroxylases. They function as oxygen sensors that catalyze the hydroxylation of HIF on prolines 564 and 402, initiating the first step of HIF degradation through the VHL/ubiquitin pathway (1, 2). PHD1 is highly expressed in a wide array of tissues whereas PHD2 and PHD3 are expressed mainly in heart and skeletal muscle (1, 3). The mRNA levels of PHD are upregulated by HIF through the hypoxia-response element under low oxygen conditions (4-7). These three enzymes also exhibit different peptide specificity target proteins, PHD1 and PHD2 can hydroxylate both proline 402 and proline 564, but PHD3 can only hydroxylate proline 564 (2, 8). In addition to HIF, PHD enzymes have also has been shown to catalyze the hydroxylation of RNA polymerase subunits and myogenin (3, 9).

NCBI and Uniprot Product Information

• NCBI GI #: 32129514
• NCBI GeneID: 54583
• UniProt Accession #: Q9GZT9; Q8N3M8; Q9BZS8; Q9BZT0
• Molecular Weight: 426
• NCBI Official Full Name: Egl nine homolog 1
• NCBI Official Synonym Full Names: egl-9 family hypoxia-inducible factor 1
• NCBI Official Symbol: EGLN1
• NCBI Official Synonym Symbols: HPH2; PHD2; SM20; ECYT3; HALAH; HPH-2; HIFPH2; ZMYND6; C1orf12; HIF-PH2
• NCBI Protein Information: egl nine homolog 1; egl nine-like protein 1; HIF prolyl hydroxylase 2; HIF-prolyl hydroxylase 2; zinc finger MYND domain-containing protein 6; hypoxia-inducible factor prolyl hydroxylase 2; prolyl hydroxylase domain-containing protein 2
• UniProt Protein Name: Egl nine homolog 1
• Protein Family: Egl nine
• UniProt Gene Name: EGLN1
• UniProt Synonym Gene Names: HIF-PH2; HIF-prolyl hydroxylase 2; HPH-2; PHD2
• UniProt Entry Name: EGLN1_HUMAN

NCBI Description

The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3). [provided by RefSeq, Nov 2009]

Uniprot Description

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 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

Chromosomal Location of Human Ortholog: 1q42.1

Cellular Component: cytoplasm; cytosol; nucleus

Molecular Function: peptidyl-proline dioxygenase activity; protein binding; enzyme binding; L-ascorbic acid binding; iron ion 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

Biological Process: oxygen homeostasis; negative regulation of cAMP catabolic process; negative regulation of transcription factor activity; cardiac muscle morphogensis; response to hypoxia; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; negative regulation of cyclic-nucleotide phosphodiesterase activity; regulation of angiogenesis

Disease: Erythrocytosis, Familial, 3; Hemoglobin, High Altitude Adaptation