|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||46021 Da|
|Positive Control||Western Blot: Various cell lysates|
|Application & Usage||Western blot: 1:500 – 1:2000, IHC: 1:50 – 1:200.|
|Other Names||EGLN1, DKFZp 61F179, ECYT3, HIFPH2, HPH2, PHD2, SM20, SM20, ZMYND6.|
|Formulation||100 µg of antibody in 100 µl PBS containing 0.02% sodium azide, 50% glycerol, pH 7.3|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||EGLN1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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 preferencially recognized via a LXXLAP motif.|
|Cellular Location||Cytoplasm. Nucleus. Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm (PubMed:19631610). Nuclear export requires functional XPO1.|
|Tissue Location||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|
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Provided below are standard protocols that you may find useful for product applications.
PHD1 (Egln2), PHD2 (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. PHD1 is highly expressed in a wide array of tissues whereas PHD2 and PHD3 are expressed mainly in heart and skeletal muscle. The mRNA levels of PHD are upregulated by HIF through the hypoxia response element under low oxygen conditions. 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. In addition to HIF, PHD enzymes have also has been shown to catalyze the hydroxylation of RNA polymerase subunits and myogenin.
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