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oxygen via Phd2 has a decisive influence on the formation of the vascular network during vertebrate embryogenesis.
comparative analysis of phd1 (show EGLN2 Proteins), 2, and 3 expression in Xenopus laevis
brain tissue protection and increased angiogenesis upon sub-acute ischemic stroke was completely absent in Phd2 knockout mice that were additionally deficient for both Hif1a (show HIF1A Proteins) and Hif2a (show EPAS1 Proteins)
expression of PHD2 in endothelial cells plays a critical role in preventing pulmonary arterial remodeling in mice
PHD-2 knockdown mesenchymal stromal cells overexpressed HIF-1alpha (show HIF1A Proteins) and multiple angiogenic factors compared to control. Wounds treated with PHD-2 knockdown mesenchymal stromal cells healed at a significantly accelerated rate compared with wounds treated with shScramble mesenchymal stromal cells.
data identify the PHD2:HIF-2alpha:EPO axis as a so far unknown regulator of osteohematology by controlling bone homeostasis.
miR (show MLXIP Proteins)-21 contributes to the protection of delayed ischemic preconditioning against renal ischemia reperfusion injury in mice, which is at least in part mediated by targeting of PHD2 and subsequently up-regulating HIF-1alpha (show HIF1A Proteins)/VEGF (show VEGFA Proteins) pathway.
Phd2 is the dominant HIF-hydroxylase in neutrophils under normoxic conditions; intrinsic regulation of glycolysis and glycogen (show GYS1 Proteins) stores is linked to the resolution of neutrophil-mediated inflammatory responses
Epo (show EPO Proteins) transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 and PHD3 (show EGLN3 Proteins), oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
Notch ligand (show JAG2 Proteins) genes Jag1 (show JAG1 Proteins), Jag2 (show JAG2 Proteins), and Dll1 (show DLL1 Proteins) and target Hes1 became downregulated upon aging HIF-2alpha (show EPAS1 Proteins) dependently.
Results identified a critical role of PHD2 for a reversible glycolytic reprogramming in macrophages with a direct impact on their function.
Results found that loss of endothelial PHD2 induced pulmonary arterial hypertension and vascular remodeling in a HIF-2-dependent fashion.
the expression of prolyl hydroxylase domain 2 (PHD2) is selectively increased in CKD-AT-MSCs and its inhibition can restore the expression of HIF-1alpha (show HIF1A Proteins) and the wound healing function of CKD-AT-MSCs. These results indicate that more studies about the functions of MSCs from CKD patients are required before they can be applied in the clinical setting
Functionally active PHD2 SNP rs516651 , located in the key pathway for the hypoxic-inflammatory response, is associated with increased 30-day mortality in Acute Respiratory Distress Syndrome (ARDS) patients. In contrast, the PHD2 SNP rs480902 is not. Furthermore, the HIF-2alpha (show EPAS1 Proteins) SNP [ch2 (show Acyp1 Proteins): 46441523(hg18)] GG-genotype was neither present in our ARDS patients of Caucasian heritage nor in healthy Caucasian blood donors.
We genotyped 347 Tibetan individuals from varying altitudes for both the Tibetan-specific EGLN1 haplotype and 10 candidate SNPs in the EPAS1 haplotype and correlated their association with hemoglobin levels.
PHD2 is a direct binding partner of EGFR (show EGFR Proteins) and show that PHD2 regulates EGFR (show EGFR Proteins) stability as well as its subsequent signaling in breast carcinoma cells.
A mechanism of PHD2 regulation that involves the mTOR (show FRAP1 Proteins) and PP2A (show PPP2R4 Proteins) pathways.
These data unravel B55alpha (show PPP2R2A Proteins) as a PHD2 substrate and highlight a role for PHD2-B55alpha (show PPP2R2A Proteins) in the response to nutrient deprivation.
Genetic variants in HIF-1alpha (show HIF1A Proteins) and PHD2 genes exist in Caucasians but do not appear to alter 30-day mortality in sepsis
The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3).
egl nine homolog 1 (C. elegans)
, egl nine homolog 1
, egl nine homolog 1-like
, egl nine homolog 2
, HIF-prolyl hydroxylase 2
, hypoxia-inducible factor prolyl hydroxylase 2
, prolyl hydroxylase domain-containing protein 2
, HIF prolyl hydroxylase 2
, egl nine-like protein 1
, zinc finger MYND domain-containing protein 6