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Recombinant PHD2 (EGLN1) protein
Recombinant PHD2 (EGLN1) protein
- 中文名称：
- Recombinant PHD2 (EGLN1) protein
- 英文名称：
- Recombinant PHD2 (EGLN1) protein
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA60116
- 规格：
- 0.02 mg|1 mg|2x1 mg|3x1 mg|4x1 mg
- 保存建议：
- 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
- 货期：
- 6-8周
- 纯度：
- N/A
- 产品形式：
- 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.
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
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.
