Anti-EGLN1 / PHD2, clone 366G/76/3

0.2 mg/ml with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. 366G/76/3 recognises human prolyl hydroxylase 2 (PHD2), a 46kDa enzyme expressed abundantly in all tissues with the highest expression in testis. Hypoxia inducible factor-1 (HIF-1) is a transcriptional complex, consisting of an alpha and beta subunit, which plays a key role in coordinating the cellular response to hypoxia. During normal oxygen conditions, the alpha subunit of HIF-1 is rapidly degraded, however when hypoxia occurs this degradation is suppressed and HIF-1 activates the transcription of various genes important for survival and adaptation to hypoxia. Prolyl hydroxylase 2 catalyses the hydroxylation of specific prolyl residues within the HIF-1 alpha subunit, thereby targeting this subunit for degradation. Protein function: 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. [The UniProt Consortium]