Egl nine homolog 1 (EGLN1) Recombinant Protein | EGLN1 recombinant protein

Recombinant Human Egl nine homolog 1 (EGLN1), partial

Cat. Num. AAA9018614

• Gene Names: EGLN1; HPH2; PHD2; SM20; ECYT3; HALAH; HPH-2; HIFPH2; ZMYND6; C1orf12; HIF-PH2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Egl nine homolog 1 (EGLN1); Recombinant Human Egl nine homolog 1 (EGLN1); partial; Egl nine homolog 1(EC 1.14.11.29)(Hypoxia-inducible factor prolyl hydroxylase 2)(HIF-PH2)(HIF-prolyl hydroxylase 2)(HPH-2)(Prolyl hydroxylase domain-containing protein 2)(PHD2)(SM-20); EGLN1 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 177-426aa, Partial
• Sequence: GGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF

• Species: Homo sapiens (Human)
• Relevance: 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. Target proteins are preferentially recognized via a LXXLAP motif.
• Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 degree C/-80 degree C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
• Preparation and Storage: Store at -20 degree C. For extended storage, store at -20 or -80 degree C.

Product Categories/Family for EGLN1 recombinant protein

Cancer

References

"Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor."Hirsila M., Koivunen P., Gunzler V., Kivirikko K.I., Myllyharju J.J. Biol. Chem. 278:30772-30780(2003)

NCBI and Uniprot Product Information

• NCBI GI #: 32129514
• NCBI GeneID: 54583
• UniProt Accession #: Q9GZT9; Q8N3M8; Q9BZS8; Q9BZT0
• 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; HALAH; 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
• Protein Family: Egl nine
• UniProt Gene Name: EGLN1
• UniProt Synonym Gene Names: HIF-PH2; HIF-prolyl hydroxylase 2; HPH-2; PHD2
• UniProt Entry Name: EGLN1_HUMAN

NCBI Description

The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3). [provided by RefSeq, Nov 2009]

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