P3373-02

Sheep Anti-PHD1 (Prolyl Hydroxylase Domain-containing Protein 1, PHD-1, DKFZp434E026, EGL Nine (C.elegans) Homolog 2, Egl Nine Homolog 2, EGLN2, Estrogen-induced Tag 6, EIT6, EIT-6, Hypoxia-inducible Factor Prolyl Hydroxylase 1, HIF Prolyl Hydroxylase 1, HIF-PH1, HIF-P4H 1, HIFPH1, HPH-3, P4H1)

EGLN2 (EGL/EGg LayingNine #2; also known as PHD1 and HPH3) is a 43kD member of the EglN family of proteins. It is ubiquitously expressed and found principally in the nucleus. EGLN2 hydroxylates proline on HIF1 a. HIF1 is an a/b heterodimeric transcriptional activa that up regulates genes involved in mitigating the effects of hypoxia. Normally, and in the presence of abundant oxygen, the HIF 1 a chain is hydroxylated by PHD family members, which results in its ubiquitylation and degradation. Under low oxygen tension, EGLN2 activity is decreased, the HIF1 a subunit is retained, and HIF1 activates genes. Human EGLN2 is 407aa in length. It contains one iron 2oxoglutarate (Fe2OG) dioxygenase domain (aa278-376) plus an ironbinding (His297 His358), and a 2,oxoglutaratebinding (Arg367) site. There is one alternative start site at Met34 that generates a 40kD isoform. In addition, there is another potential splice form that shows a 16aa substitution for aa1281 fulllength human EGLN2 shares 91% aa sequence identity with mouse EGLN2.