Human EGLN1/PHD2 Alexa Fluor® 488-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: EGLN1/PHD2

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.

Product Datasheets

Product Specific Notices

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Related Research Areas

• Additional Reduction/Oxidation (Redox) Enzymes
• HIF Transcription Factors
• Oxygenases/Hydroxylases
• Redox Enzymes