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Human Polyclonal EGLN1 Primary Antibody for FACS, ICC - ABIN151071
Elvidge, Glenny, Appelhoff, Ratcliffe, Ragoussis, Gleadle: Concordant regulation of gene expression by hypoxia and 2-oxoglutarate-dependent dioxygenase inhibition: the role of HIF-1alpha, HIF-2alpha, and other pathways. in The Journal of biological chemistry 2006
Show all 66 Pubmed References
Human Polyclonal EGLN1 Primary Antibody for ICC, IF - ABIN250635
Mikhaylova, Ignacak, Barankiewicz, Harbaugh, Yi, Maxwell, Schneider, Van Geyte, Carmeliet, Revelo, Wyder, Greis, Meller, Czyzyk-Krzeska: The von Hippel-Lindau tumor suppressor protein and Egl-9-Type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress. in Molecular and cellular biology 2008
Show all 23 Pubmed References
Human Polyclonal EGLN1 Primary Antibody for EM, FACS - ABIN151072
Baek, Mahon, Oh, Kelly, Krishnamachary, Pearson, Chan, Giaccia, Semenza: OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. in Molecular cell 2005
Show all 16 Pubmed References
Human Monoclonal EGLN1 Primary Antibody for IHC, IHC (p) - ABIN440716
Stolze, Tian, Appelhoff, Turley, Wykoff, Gleadle, Ratcliffe: Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected]. in The Journal of biological chemistry 2004
Show all 4 Pubmed References
Human Polyclonal EGLN1 Primary Antibody for ELISA, WB - ABIN565755
Aprelikova, Pandolfi, Tackett, Ferreira, Salnikow, Ward, Risinger, Barrett, Niederhuber: Melanoma antigen-11 inhibits the hypoxia-inducible factor prolyl hydroxylase 2 and activates hypoxic response. in Cancer research 2009
oxygen via Phd2 has a decisive influence on the formation of the vascular network during vertebrate embryogenesis.
comparative analysis of phd1 (show EGLN2 Antibodies), 2, and 3 expression in Xenopus laevis
PHD-2 knockdown mesenchymal stromal cells overexpressed HIF-1alpha (show HIF1A Antibodies) 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-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/VEGF pathway.
Phd2 is the dominant HIF-hydroxylase in neutrophils under normoxic conditions; intrinsic regulation of glycolysis and glycogen (show GYS1 Antibodies) stores is linked to the resolution of neutrophil-mediated inflammatory responses
Epo (show EPO Antibodies) transcription in brain pericytes was HIF-2 dependent and cocontrolled by PHD2 and PHD3 (show EGLN3 Antibodies), oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
Notch ligand (show JAG2 Antibodies) genes Jag1 (show JAG1 Antibodies), Jag2 (show JAG2 Antibodies), and Dll1 (show DLL1 Antibodies) and target Hes1 became downregulated upon aging HIF-2alpha (show EPAS1 Antibodies) 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.
We conclude that the activation of the HIF pathway induced by PHD2 deficiency enhances the effect of running training
deleting Phd1 (show EGLN2 Antibodies)-3 genes in osteoblasts increased osteoclast formation in vitro and in bone.
A mechanism of PHD2 regulation that involves the mTOR (show FRAP1 Antibodies) and PP2A (show PPP2R4 Antibodies) pathways.
These data unravel B55alpha (show PPP2R2A Antibodies) as a PHD2 substrate and highlight a role for PHD2-B55alpha (show PPP2R2A Antibodies) in the response to nutrient deprivation.
Genetic variants in HIF-1alpha (show HIF1A Antibodies) and PHD2 genes exist in Caucasians but do not appear to alter 30-day mortality in sepsis
The role of PHD-2 in breast cancer [review]
Sulfur mustard negatively affects hypoxia-stimulated HIF-1alpha (show HIF1A Antibodies) signaling in keratinocytes and fibroblasts and thus possibly contributes to delayed wound healing in SM-injured patients, which could be treated with PHD-2 inhibitors.
The HIFalpha subunit is usually prolyl-hydroxylated by EglN family members under normoxic conditions, causing its rapid degradation. Study confirmed that triple-negative breast cancer cells secrete glutamate (show GRIN1 Antibodies), which is both necessary and sufficient for the paracrine induction of HIF1alpha (show HIF1A Antibodies) in such cells under normoxic conditions.
Disulfide bond-mediated PHD2 dimerization and inactivation result in the activation of HIF-1alpha (show HIF1A Antibodies) and aerobic glycolysis in response to oxidative stress.
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