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SDS-Page (Recombinant PHD2 (EGLN1) protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 47 kDa Purity: > 90%)

PHD2 recombinant protein

Recombinant PHD2 (EGLN1) protein

Gene Names
EGLN1; HPH2; PHD2; SM20; ECYT3; HPH-2; HIFPH2; ZMYND6; C1orf12; HIF-PH2
Synonyms
PHD2; Recombinant PHD2 (EGLN1) protein; Egl-9 Family Hypoxia Inducible Factor 1; Hypoxia-Inducible Factor Prolyl Hydroxylase 2; HIF Prolyl Hydroxylase 2; PHD2 recombinant protein
Ordering
For Research Use Only!
Host
Baculovirus
Form/Format
Recombinant PHD2/EGLN1 protein is supplied in 25mM HEPES-NaOH pH7.5, 300mM NaCl, 10% glycerol, 0.04% Triton X-100 and 0.5mM TCEP.
Protein Species
Human
Tag
DYKDDDDK-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 PHD2 (EGLN1) protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 47 kDa Purity: > 90%)

SDS-Page (Recombinant PHD2 (EGLN1) protein gel 10% SDS-PAGE gel with Coomassie blue staining MW: 47 kDa Purity: > 90%)

Testing Data

(MALDI-TOF for PHD2 (EGLN1) protein activity 3 uM HIF1A (HIF-1a) peptide (peptide sequence: biotin-DLDLEALAPYIPADDDFQL) was incubated with 300 nM PHD2 (EGLN1) protein in a 30 ul reaction system containing 20 mM Tris-HCl pH 7.5, 5 mM KCl, 1.5 mM MgCl2, 1 mM DTT, 100 uM 2-oxoglutarate, 100 uM ascorbate and 50 uM (NH4)2Fe(SO4)2·6H2O for 2 hr at 3°ree;. Single 3 uM HIF1A peptide was used as negative control. MALDI-TOF was used for detection.)

Testing Data (MALDI-TOF for PHD2 (EGLN1) protein activity 3 uM HIF1A (HIF-1a) peptide (peptide sequence: biotin-DLDLEALAPYIPADDDFQL) was incubated with 300 nM PHD2 (EGLN1) protein in a 30 ul reaction system containing 20 mM Tris-HCl pH 7.5, 5 mM KCl, 1.5 mM MgCl2, 1 mM DTT, 100 uM 2-oxoglutarate, 100 uM ascorbate and 50 uM (NH4)2Fe(SO4)2·6H2O for 2 hr at 3°ree;. Single 3 uM HIF1A peptide was used as negative control. MALDI-TOF was used for detection.)
Related Product Information for PHD2 recombinant protein
Short Description: Recombinant human PHD2 (EGLN1) protein was expressed in a baculovirus expression system as the full-length protein (accession number NP_071334.1) with an N-terminal DYKDDDDK tag. The molecular weight of the protein is 47 kDa. It is suitable for use in binding assays, inhibitor screening, and selectivity profiling.

Background: Prolyl Hydroxylase Domain-Containing Protein 2 (PHD2) or Egl-9 Family Hypoxia Inducible Factor 1 (EGLN1), also known as HIF-PH2 or HPH-2, 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. PHD1 has a preference for the CODD site for both HIF1A and HIF2A. 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. PHD2 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. Its target proteins are preferentially recognized via a LXXLAP motif.
Product Categories/Family for PHD2 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
426
NCBI Official Full Name
egl nine homolog 1
NCBI Official Synonym Full Names
egl-9 family hypoxia-inducible factor 1
NCBI Official Symbol
EGLN1
NCBI Official Synonym Symbols
HPH2; PHD2; SM20; ECYT3; HPH-2; HIFPH2; ZMYND6; C1orf12; HIF-PH2
NCBI Protein Information
egl nine homolog 1; egl nine-like protein 1; HIF prolyl hydroxylase 2; HIF-prolyl hydroxylase 2; zinc finger MYND domain-containing protein 6; hypoxia-inducible factor prolyl hydroxylase 2; prolyl hydroxylase domain-containing protein 2
UniProt Protein Name
Egl nine homolog 1
UniProt Gene Name
EGLN1
UniProt Synonym Gene Names
HIF-PH2; HIF-prolyl hydroxylase 2; HPH-2; PHD2
UniProt Entry Name
EGLN1_HUMAN

Uniprot Description

EGLN1: 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. Monomer. Interacts with ING4; the interaction inhibits the hydroxylation of HIFs. Interacts with LIMD1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with EPAS1. 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. Following exposure to hypoxia, activated in HeLa cells but not in cardiovascular cells. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 1.14.11.29; Oxidoreductase

Chromosomal Location of Human Ortholog: 1q42.1

Cellular Component: cytoplasm; cytosol; nucleus

Molecular Function: peptidyl-proline dioxygenase activity; protein binding; enzyme 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: oxygen homeostasis; negative regulation of cAMP catabolic process; negative regulation of transcription factor activity; cardiac muscle morphogensis; response to hypoxia; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; negative regulation of cyclic-nucleotide phosphodiesterase activity; regulation of angiogenesis

Disease: Erythrocytosis, Familial, 3; Hemoglobin, High Altitude Adaptation

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Product Notes

The PHD2 egln1 (Catalog #AAA389124) is a Recombinant Protein produced from Baculovirus and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "PHD2, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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