Egl nine homolog 3 Recombinant Protein | Egln3 recombinant protein

Recombinant Mouse Egl nine homolog 3 protein

Cat. Num. AAA1265356

• Gene Names: Egln3; Phd3; SM-20; AI505553; AI648162; Hif-p4h-3; 2610021G09Rik
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Egl nine homolog 3; Recombinant Mouse Egl nine homolog 3 protein; Hypoxia-inducible factor prolyl hydroxylase 3; HIF-PH3; HIF-prolyl hydroxylase 3; HPH-3; Prolyl hydroxylase domain-containing protein 3; PHD3SM-20; Egln3 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 2-239aa; Full Length
• Sequence: PLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHYNGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAINFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGVLRIFPEGKSFVADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALAKD
• Sequence Length: 239

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for Egln3 recombinant protein

Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway. 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. ELGN3 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. Target proteins are preferencially recognized via a LXXLAP motif.

References

SM-20 is a novel growth factor-responsive gene regulated during skeletal muscle development and differentiation.Moschella M.C., Menzies K., Tsao L., Lieb M.A., Kohtz J.D., Kohtz D.S., Taubman M.B.Gene Expr. 8:59-66(1999) Characterization and comparative analysis of the EGLN gene family.Taylor M.S.Gene 275:125-132(2001) Mammalian EGLN genes have distinct patterns of mRNA expression and regulation.Lieb M.E., Menzies K., Moschella M.C., Ni R., Taubman M.B.Biochem. Cell Biol. 80:421-426(2002) Abnormal sympathoadrenal development and systemic hypotension in PHD3-/-mice.Bishop T., Gallagher D., Pascual A., Lygate C.A., de Bono J.P., Nicholls L.G., Ortega-Saenz P., Oster H., Wijeyekoon B., Sutherland A.I., Grosfeld A., Aragones J., Schneider M., van Geyte K., Teixeira D., Diez-Juan A., Lopez-Barneo J., Channon K.M., Maxwell P.H., Pugh C.W., Davies A.M., Carmeliet P., Ratcliffe P.J.Mol. Cell. Biol. 28:3386-3400(2008) A feedback loop involving the Phd3 prolyl hydroxylase tunes the mammalian hypoxic response in vivo.Minamishima Y.A., Moslehi J., Padera R.F., Bronson R.T., Liao R., Kaelin W.G. Jr.Mol. Cell. Biol. 29:5729-5741(2009) Oxygen-regulated beta(2) -adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL.Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G., Gygi S.P., Lefkowitz R.J., Stamler J.S.Sci. Signal. 2:RA33-RA33(2009) Prolyl hydroxylase 3 (PHD3) is essential for hypoxic regulation of neutrophilic inflammation in humans and mice.Walmsley S.R., Chilvers E.R., Thompson A.A., Vaughan K., Marriott H.M., Parker L.C., Shaw G., Parmar S., Schneider M., Sabroe I., Dockrell D.H., Milo M., Taylor C.T., Johnson R.S., Pugh C.W., Ratcliffe P.J., Maxwell P.H., Carmeliet P., Whyte M.K.J. Clin. Invest. 121:1053-1063(2011)

NCBI and Uniprot Product Information

• NCBI GI #: 269308213
• NCBI GeneID: 112407
• NCBI Accession #: NP_082409.2
• NCBI GenBank Nucleotide #: NM_028133.2
• UniProt Accession #: Q91UZ4; Q3TCG8; Q8C8M6; Q8CCA8; Q8R5C7
• Molecular Weight: 31.2 kDa
• NCBI Official Full Name: egl nine homolog 3
• NCBI Official Synonym Full Names: egl-9 family hypoxia-inducible factor 3
• NCBI Official Symbol: Egln3
• NCBI Official Synonym Symbols: Phd3; SM-20; AI505553; AI648162; Hif-p4h-3; 2610021G09Rik
• NCBI Protein Information: egl nine homolog 3
• UniProt Protein Name: Egl nine homolog 3
• Protein Family: Egl nine
• UniProt Gene Name: Egln3
• UniProt Synonym Gene Names: HIF-PH3; HIF-prolyl hydroxylase 3; HPH-3; PHD3
• UniProt Entry Name: EGLN3_MOUSE

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: EC 1.14.11.29; Oxidoreductase

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