Egl Nine Homolog 1

E2500Hu

Sandwich

48T,96T

10.14ng/L

20-4500ng/L

Serum, plasma, cell culture supernates

Human

2-8ºC

1h 30m

Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then 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. EGLN1 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. Target proteins are preferentially recognized via a LXXLAP motif.

46,021

54583

C1orf12;ECYT3;Egl nine homolog 1;EGLN1;HALAH;HIF-PH2;HIF-prolyl hydroxylase 2;HPH2;HPH-2;Hypoxia-inducible factor prolyl hydroxylase 2;PHD2;Prolyl hydroxylase domain-containing protein 2;SM20;SM-20;ZMYND6

EGLN1

Cardiovascular

EGLN1