PHD2 Recombinant Rabbit Monoclonal Antibody [PSH12-74]

Function

PHD2 (Prolyl Hydroxylase Domain-containing protein 2), also known as EGLN1, is a critical cellular oxygen sensor that plays a central role in regulating the hypoxia-inducible factor (HIF) pathway. Under normoxic conditions, PHD2 catalyzes the post-translational hydroxylation of specific proline residues (Pro-402 and Pro-564 in HIF-1α) within the oxygen-dependent degradation (ODD) domains of HIF-α subunits (HIF-1α and HIF-2α). This hydroxylation marks HIF-α for proteasomal degradation via the von Hippel-Lindau (VHL) ubiquitination complex, thereby maintaining oxygen homeostasis. PHD2 is widely expressed, with the highest levels found in skeletal muscle, heart, kidney, and brain. It is the primary oxygen sensor under normoxic conditions and is essential for regulating cellular responses to oxygen availability. Under hypoxic conditions, PHD2 activity is reduced, allowing HIF-α subunits to escape degradation, translocate to the nucleus, and activate the transcription of hypoxia-inducible genes involved in angiogenesis, metabolism, and cell survival. PHD2 is encoded by the EGLN1 gene, located on chromosome 1q42.1. Mutations in EGLN1 are associated with familial erythrocytosis type 3 (ECYT3), an autosomal dominant disorder characterized by increased red blood cell mass and elevated hemoglobin levels.

Background References

1. Song, X. et al. 2013. Wogonin inhibits tumor angiogenesis via degradation of HIF-1α protein. Toxicol. Appl. Pharmacol. 271: 144-155.

2. Yan, B. et al. 2011. Prolyl hydroxylase domain protein 3 targets Pax2 for destruction. Biochem. Biophys. Res. Commun. 409: 315-320.

Subcellular Location

Cytoplasm, Nucleus.

UNIPROT

SwissProt: Q9GZT9 Human

Synonyms