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The protein encoded by EGLN1 catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Additionally we are shipping Egl Nine Homolog 1 (C. Elegans) Antibodies (105) and Egl Nine Homolog 1 (C. Elegans) Kits (6) and many more products for this protein.
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comparative analysis of phd1 (show EGLN2 Proteins), 2, and 3 expression in Xenopus laevis
HIF-P4H-2 inhibition may be a novel strategy for protecting against the development of atherosclerosis.
findings show hypoxia and loss of PHD2 revert cancer-associated fibroblast (CAF (show LAMA2 Proteins)) activation; this reversion is associated with loss of matrix stiffening and consequently reduction in spontaneous metastases to lungs and liver
Data (including data from studies in transgenic/knockout mice) suggest that expression of Phd2/Egln1 in chondrocytes plays key role in chondrogenesis, osteogenesis, and developmental gene expression regulation.
a genetic link between EGLN1 and VWF (show VWF Proteins) in a constitution specific manner which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia, is reported.
PHD2 in the liver has a role in survival in lactic acidosis by activating the Cori cycle
Regulatory link was discovered between mitochondrial Txnrd and the JNK (show MAPK8 Proteins)-PHD2-Hif-1alpha (show HIF1A Proteins) axis, which highlights how the loss of Txnrd2 (show TXNRD2 Proteins) and the resulting altered mitochondrial redox balance impairs tumor growth as well as tumor-related angiogenesis.
combined deletion of Phd2 and Phd3 (show EGLN3 Proteins) dramatically decreased expression of phospholamban (PLN (show PLN Proteins)), resulted in sustained activation of calcium/calmodulin (show Calm2 Proteins)-activated kinase II (CaMKII (show CAMK2G Proteins)), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury
PHD2 activity is a critical contributor to the high fat-diet-induced cardiac dysfunction.
Phd2 plays an important role in regulating bone formation in part by modulating expression of Osx (show SP7 Proteins) and bone formation marker genes.
Hif-p4h-2-deficient mice, whether fed normal chow or a high-fat diet, had less adipose tissue, smaller adipocytes, and less adipose tissue inflammation than their littermates.
the levels of both miR-182 and HIF1alpha were elevated, while the expression PHD2 and FIH1 was downregulated in a mouse model of prostate cancer.
findings show hypoxia and loss of PHD2 revert cancer-associated fibroblast (CAF (show KAT2B Proteins)) activation
In this article, UTMD/PEI mediated gene transfection was investigated and the US parameters were optimized. Furthermore, the biological effects of PHD2 shRNA were investigated in H9C2 cells.
Data show that dimethyl-2-ketoglutarate (DKG) inhibits hypoxia-inducible factor 1alpha (HIF-1alpha (show HIF1A Proteins)) proline hydroxylation and degradation mediated by prolyl-4-hydroxylase PHD2.
The kinetic properties of PHD2 and FIH (show CASR Proteins) with respect to oxygen reflect their cellular hypoxia-sensing ability.
Germ-line PHD1 (show EGLN2 Proteins) and PHD2 mutations detected in patients with pheochromocytoma/paraganglioma-polycythemia
The association between EGLN1 and HIF-1AN single nucleotide polymorphisms and acute mountain sickness in a Han Chinese population, was examined.
Compared to those with high PHD2 expressions, patients with low PHD2 expression had significantly longer DFS (show FST Proteins) and OS periods.
PHD2 inhibits the adaptation of glioblastoma cells to hypoxia by regulating the expression of HIF-alpha subunits.
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