Recombinant Human PHD2 / prolyl hydroxylase protein is a Human Fragment protein, in the 299 to 426 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
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Key facts
- Expression system
- Wheat germ
- Tags
- GST tag N-Terminus
- Applications
- SDS-PAGE, ELISA, WB
- Biologically active
- No
Amino acid sequence
M V A C Y P G N G T G Y V R H V D N P N G D G R C V T C I Y Y L N K D W D A K V S G G I L R I F P E G K A Q F A D I E P K F D R L L F F W S D R R N P H E V Q P A Y A T R Y A I T V W Y F D A D E R A R A K V K Y L T G E K G V R V E L N K P S D S V G K D V F
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
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Target data
Function
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.
Alternative names
C1orf12, PNAS-118, PNAS-137, EGLN1, Egl nine homolog 1, Hypoxia-inducible factor prolyl hydroxylase 2, Prolyl hydroxylase domain-containing protein 2, SM-20, HIF-PH2, HIF-prolyl hydroxylase 2, HPH-2, PHD2
Recommended products
Recombinant Human PHD2 / prolyl hydroxylase protein is a Human Fragment protein, in the 299 to 426 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
Key facts
- Expression system
- Wheat germ
- Tags
- GST tag N-Terminus
- Applications
- SDS-PAGE, ELISA, WB
- Biologically active
- No
- Accession
- Q9GZT9-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Sequence info
Amino acid sequence
- M V A C Y P G N G T G Y V R H V D N P N G D G R C V T C I Y Y L N K D W D A K V S G G I L R I F P E G K A Q F A D I E P K F D R L L F F W S D R R N P H E V Q P A Y A T R Y A I T V W Y F D A D E R A R A K V K Y L T G E K G V R V E L N K P S D S V G K D V F
- Accession
- Q9GZT9
- Protein length
- Fragment
- Predicted molecular weight
- 41 kDa
- Amino acids
- 299 to 426
- Nature
- Recombinant
- Tags
- GST tag N-Terminus
Specifications
- Form
- Liquid
General info
- Function
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.
- Post-translational modifications
S-nitrosylation inhibits the enzyme activity up to 60% under aerobic conditions. Chelation of Fe(2+) has no effect on the S-nitrosylation. It is uncertain whether nitrosylation occurs on Cys-323 or Cys-326.
- Subcellular localisation
- Nucleus
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
The protein PHD2 also known as prolyl hydroxylase 3 EGLN1 or 366G is a member of the prolyl hydroxylase family with a molecular mass of approximately 46 kDa. PHD2 is expressed in a variety of tissues particularly those in the human body's oxygen-sensing cellular machinery. This protein functions mechanically by adding hydroxyl groups to proline residues on its target proteins an enzymatic activity essential for its role in cellular oxygen sensing.
- Biological function summary
This hydroxylation process influences the stability of hypoxia-inducible factor (HIF) by marking it for degradation under normal oxygen levels. PHD2 is a monomeric enzyme but its hydroxylase activity does not require association with other proteins to function. By regulating HIF PHD2 plays a critical role in cellular responses to oxygen availability controlling genes involved in processes such as angiogenesis metabolism and cell survival.
- Pathways
PHD2 participates in the HIF signaling pathway and oxygen homeostasis pathways. The regulation of HIF by PHD2 occurs alongside PHD1 and PHD3 which have similar hydroxylase activities. Importantly PHD2 protects cells from hypoxia-related stress by ensuring the degradation of HIF-α subunits under normoxic conditions thereby maintaining cellular homeostasis and proper metabolic function.
- Associated diseases and disorders
PHD2 has connections with conditions such as cancer and chronic kidney disease. Its role in cancer is linked to its regulation of HIF where dysregulation can lead to abnormal cell growth and angiogenesis. In chronic kidney disease the insights into PHD2's function offer potential therapeutic targets particularly since HIF stabilization can ameliorate anemia frequently associated with this condition. Interactions between PHD2 and other proteins in these disease pathways make it a significant focal point for research aimed at developing new treatments.
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1 product image
SDS-PAGE - Recombinant Human PHD2 / prolyl hydroxylase protein (ab132273)
12.5% SDS-PAGE analysis of ab132273 stained with Coomassie Blue.
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