Recombinant Human HIF Prolyl Hydroxylases protein is a Human Full Length protein, in the 1 to 563 aa range, expressed in Wheat germ and suitable for ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
PH4, P4HTM, Transmembrane prolyl 4-hydroxylase, P4H-TM, Hypoxia-inducible factor prolyl hydroxylase 4, HIF-PH4, HIF-prolyl hydroxylase 4, HPH-4
Recombinant Human HIF Prolyl Hydroxylases protein is a Human Full Length protein, in the 1 to 563 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
Glycosylated.
HIF prolyl hydroxylases also known as EglN or prolyl hydroxylase domain proteins (PHDs) are enzymes that modulate the stability of hypoxia-inducible factors (HIFs). These enzymes primarily facilitate the hydroxylation of prolyl residues on HIF-α subunits which marks them for degradation via the ubiquitin-proteasome pathway. Mammals express three isoforms: PHD1 PHD2 and PHD3 with PHD2 being the most widely studied. PHDs are expressed ubiquitously with higher levels observed in the liver kidneys and lung. The molecular mass of these enzymes is typically around 40 kDa.
HIF prolyl hydroxylases play an essential role in oxygen sensing and homeostasis by regulating the activity of HIF-α subunits. Under normoxic conditions the hydroxylation of HIF-α by these hydroxylases permits recognition by the von Hippel-Lindau (VHL) protein leading to proteasomal degradation. In hypoxic conditions the decreased activity of HIF prolyl hydroxylases allows HIF-α stabilization and heterodimerization with HIF-β facilitating transcription of target genes involved in angiogenesis and metabolism. PHD2 is predominantly responsible for targeting HIF-1α.
HIF prolyl hydroxylases integrate into the hypoxia response pathway. Oxygen-dependent regulation of HIF by these hydroxylases affects processes such as angiogenesis and erythropoiesis through interaction with several proteins including endothelial growth factor (VEGF) and erythropoietin (EPO). Beyond the hypoxia pathway they participate in metabolic pathways influencing cellular energy homeostasis thereby impacting proteins involved in metabolic regulation.
HIF prolyl hydroxylases associate with cancer and ischemic diseases. Dysregulation of these hydroxylases can lead to excessive stabilization of HIF-α which promotes tumor growth and metastasis due to enhanced angiogenesis and altered metabolism associated with cancer cells. In ischemic conditions reduced prolyl hydroxylases activity can offer protection by inducing adaptive responses through HIF-α stabilization. Their connectivity to the VHL protein further links them to von Hippel-Lindau disease characterized by tumor development in multiple organs.
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ab162816 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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