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EGLN1 Protein, Human, Recombinant (His & Myc)

Catalog No. TMPH-01280
Synonyms: HPH-2, EGLN1, PHD2, SM-20, HIF-prolyl hydroxylase 2, HIF-PH2, C1orf12, Egl nine homolog 1

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.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
EGLN1 Protein, Human, Recombinant (His & Myc)
Pack Size Availability Price/USD Quantity
20 μg 20 days $ 284.00
100 μg 20 days $ 537.00
1 mg 20 days $ 2,300.00
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Biological Description
Technical Params
Product Properties
Description 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.
Species Human
Expression System E. coli
Tag N-terminal 10xHis-tagged and C-terminal Myc-tagged
Accession Number Q9GZT9
Synonyms HPH-2, EGLN1, PHD2, SM-20, HIF-prolyl hydroxylase 2, HIF-PH2, C1orf12, Egl nine homolog 1
Amino Acid GGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Construction 177-426 aa
Protein Purity > 85% as determined by SDS-PAGE.
Molecular Weight 35.3 kDa as predicted
Formulation Tris-based buffer，50% glycerol
Reconstitution A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage

Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shipping

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background 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.

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Keywords

EGLN1 Protein, Human, Recombinant (His & Myc) HPH-2 EGLN1 PHD2 SM-20 HIF-prolyl hydroxylase 2 HIF-PH2 C1orf12 Egl nine homolog 1 recombinant recombinant-proteins proteins protein

 

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