|Detection of Human EGLN1/PHD2 by Western Blot. Western blot shows lysates of human brain (cerebellum) tissue, human pancreas tissue, and human heart tissue. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human EGLN1/PHD2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7680) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for EGLN1/PHD2 at approximately 45-50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
PHD2 (Prolyl Hydroxylase Domain-containing protein 2; also HPH2, EGLN1 and HIF-PH2) is a 45-47 kDa dioxygenase member of the PH family of enzymes. It is ubiquitously expressed, and serves to regulate the availability of the oxygen-sensitive HIF transcription factor. Active HIF1 alpha is a heterodimer of alpha - and beta -subunits and when intact, promotes VEGF and EPO production. The beta -subunit is constitutively expressed, while alpha -subunit levels are regulated by intracellular oxygen concentration. At normoxic levels, the alpha -subunit is hydroxylated on Pro by one of three PHDs, inducing its ubiquitination/degradation. The hydroxylation event requires oxygen, and thus PH activity (particularly PHD2) is a measure of a cell's oxygen concentration. Human PHD2 is 426 amino acids (aa) in length. It contains an NES (aa 6-20), a Zn-finger region (aa 21-58), and a catalytic domain (aa 291-392). There are five nitrosylated cysteines plus one acetylated alanine. Two isoform variants are known, one that shows a deletion of aa 338-359, and another that contains a 17 aa substitution for aa 58-175. Over aa 157-426, human PHD2 shares 93% aa sequence identity with mouse PHD2.
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