Rabbit anti-Mouse Egl nine homolog 3 Polyclonal Antibody | anti-Egln3 antibody
Rabbit anti-mouse Egl nine homolog 3 polyclonal Antibody, FITC
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
NCBI and Uniprot Product Information
Uniprot Description
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 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. 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: Oxidoreductase; EC 1.14.11.29
Cellular Component: cytoplasm; cytosol; nucleus
Molecular Function: dioxygenase activity; iron ion binding; L-ascorbic acid binding; metal ion binding; oxidoreductase activity; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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: apoptosis; peptidyl-proline hydroxylation; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; protein amino acid hydroxylation; regulation of cell proliferation; regulation of neuron apoptosis; response to DNA damage stimulus; response to hypoxia