PHD3 recombinant protein

Recombinant PHD3 (EGLN3) protein

Cat. Num. AAA389092

• Gene Names: EGLN3; PHD3; HIFPH3; HIFP4H3
• Synonyms: PHD3; Recombinant PHD3 (EGLN3) protein; Egl-9 Family Hypoxia Inducible Factor 3; Prolyl Hydroxylase Domain-Containing Protein 3; HIF-Prolyl Hydroxylase 3; PHD3 recombinant protein

• Host: E Coli
• Form/Format: Recombinant PHD3 (EGLN3) protein is supplied in 25mM Tris-HCl pH8, 300mM NaCl, 10% glycerol and 0.5mM TCEP.

• Protein Species: Human
• Tag: His-Tag
• Notes: This product was manufactured as described in Protein Details. Where possible, We has developed functional or activity assays for recombinant proteins. Additional characterization such as enzyme kinetic activity assays, inhibitor screening or other biological activity assays may not have been performed for every product. All available data for a given product is shown on the lot-specific Technical Data Sheet.
• Dry Ice Shipment: Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
• Preparation and Storage: Recombinant proteins in solution are temperature sensitive and must be stored at -80 degree C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.; Shipping Temp: Dry Ice

SDS-Page

(Recombinant PHD3 / EGLN3 protein 10% SDS-PAGE Coomassie staining. MW: 31.1 kDa Purity: >80%)

Related Product Information for PHD3 recombinant protein

Short Description: Recombinant human PHD3 (EGLN3) protein was expressed in E Coli as the full-length protein (accession number NP_071356.1) with an N-terminal 6xHis-tag. The molecular weight of the protein is 31.1 kDa. It is suitable for use in binding assays, inhibitor screening, and selectivity profiling.

Background: Prolyl Hydroxylase Domain-Containing Protein 3 (PHD3) or Egl-9 Family Hypoxia Inducible Factor 3 (EGLN3), also known as PHIF-PH3 or HPH-3, is a prolyl hydroxylase. PHD3 is a cellular oxygen sensor that catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins under normoxic conditions. It can hydroxylate a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A, also HIF2A. PHD3 has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by PHD3 appears to require prior hydroxylation on the CODD site, and then hydroxylated HIFs are 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. PHD3 can also hydroxylate PKM in hypoxia, limiting glycolysis, while under normoxia, hydroxylate and regulates the stability of ADRB2. In cardiomyocytes, it inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, it has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. PHD3 is essential for hypoxic regulation of neutrophilic inflammation. Beside, it 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. Its target proteins are preferentially recognized via a LXXLAP motif.

Product Categories/Family for PHD3 recombinant protein

Recombinant Proteins; Transcription

NCBI and Uniprot Product Information

• NCBI GI #: 11545787
• NCBI GeneID: 112399
• NCBI Accession #: NP_071356.1
• NCBI GenBank Nucleotide #: NM_022073.3
• UniProt Accession #: Q9H6Z9; Q2TA79; Q3B8N4; Q6P1R2
• Molecular Weight: 27,261 Da
• 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; HIFPH3; HIFP4H3
• NCBI Protein Information: egl nine homolog 3; HIF prolyl hydroxylase 3; HIF-PH3; HIF-prolyl hydroxylase 3; HPH-1; HPH-3; egl nine-like protein 3 isoform; hypoxia-inducible factor prolyl hydroxylase 3; prolyl hydroxylase domain-containing protein 3
• UniProt Protein Name: Egl nine homolog 3
• UniProt Gene Name: EGLN3
• UniProt Synonym Gene Names: HIF-PH3; HIF-prolyl hydroxylase 3; HPH-3; PHD3
• UniProt Entry Name: EGLN3_HUMAN

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

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