antibody

Rabbit anti-human egl nine homolog 3 (C. elegans) polyclonal Antibody

MBS710110

0.05 mL

375 USD

polyclonal

rabbit

nonconjugated

human, mouse, rat

western blot, ELISA, immunohistochemistry, enzyme immunoassay

Antibody

Rabbit anti-human egl nine homolog 3 (C. elegans) polyclonal Antibody

egl nine homolog 3

egl nine homolog 3 (C. elegans); EGLN3; FLJ21620; HIFPH3; MGC125998; MGC125999; PHD3

egl nine homolog 3; Egl nine homolog 3; egl nine homolog 3; HPH-1; HPH-3; HIF-PH3; HIF prolyl hydroxylase 3; HIF-prolyl hydroxylase 3; egl nine-like protein 3 isoform; hypoxia-inducible factor prolyl hydroxylase 3; prolyl hydroxylase domain-containing protein 3; egl-9 family hypoxia-inducible factor 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; EGLN3; PHD3; HIFPH3; HIFP4H3; HIF-PH3; HIF-prolyl hydroxylase 3; HPH-3; PHD3

EGLN3_HUMAN

Polyclonal

IgG

Rabbit

Human, Mouse, Rat

239

Antigen Affinity Purified

ELISA (EIA), Western Blot (WB), Immunohistochemistry (IHC)

Immunogen: Human EGLN3

Storage Buffer: PBS with 0.02% Sodium Azide, 50% Glycerol, pH 7.3. -20 degree C, Avoid freeze / thaw cycles.

11545787

NP_071356.1

NM_022073.3

27,261 Da

Cellular Response To Hypoxia Pathway (645259); Cellular Responses To Stress Pathway (645258); HIF-1 Signaling Pathway (695200); HIF-1-alpha Transcription Factor Network Pathway (138045); HIF-2-alpha Transcription Factor Network Pathway (137956); Oxygen-dependent Proline Hydroxylation Of Hypoxia-inducible Factor Alpha Pathway (645262); Pathways In Cancer (83105); Regulation Of Hypoxia-inducible Factor (HIF) By Oxygen Pathway (645260); Renal Cell Carcinoma Pathway (83107); Renal Cell Carcinoma Pathway (519)

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. Chromosomal Location of Human Ortholog: 14q13.1. Cellular Component: nucleoplasm; cytoplasm; nucleus; cytosol. Molecular Function: protein 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: caspase activation; apoptosis; regulation of neuron apoptosis; response to hypoxia; protein amino acid hydroxylation; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; response to DNA damage stimulus; regulation of cell proliferation

0.05 mL

375 USD

0.15 mL

715