Catalog No.S2919 Synonyms: JICL38
Molecular Weight(MW): 352.34
IOX2 is a potent inhibitor of HIF-1α prolyl hydroxylase-2 (PHD2) with IC50 of 21 nM in a cell-free assay, >100-fold selectivity over JMJD2A, JMJD2C, JMJD2E, JMJD3, or the 2OG oxygenase FIH.
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NHEK and NHDF are cultivated under normoxic (N) and hypoxic (H) conditions in the presence of IOX2 (50 μM), or vehicle control (DMSO). b HIF-1α levels are analyzed in cell extracts of NHEK (4 h) and NHDF (24 h) by immunoblotting with cellular β-actin as loading control. c Subcellular localization of HIF-1α is examined by immunoblotting analysis of HIF-1α in nuclear (Nu) and cytoplasmic (Cy) fractions with β-tubulin as cytosolic loading control.
Arch Toxicol, 2016, 90(5):1141-50. IOX2 purchased from Selleck.
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|Description||IOX2 is a potent inhibitor of HIF-1α prolyl hydroxylase-2 (PHD2) with IC50 of 21 nM in a cell-free assay, >100-fold selectivity over JMJD2A, JMJD2C, JMJD2E, JMJD3, or the 2OG oxygenase FIH.|
IOX2 potently inhibits PHD2 (IC50 of 21 nM) with over 100-fold selectivity compared to inhibition of JMJD2A, JMJD2C, JMJD2E, JMJD3, or the 2OG oxygenase FIH (IC50s <100 μM). IOX2 is active in cells, inhibiting HIF-1α hydroxylation in RCC4 cells at 50 μM.  Hypoxia Inducible Factor (HIF) is regulated by the hydroxylation of prolyl residues in oxygen-dependent degradation domains in the HIF-1α subunit, which mark it for degradation by the proteosome. 1,2 HIF prolyl hydroxylation is catalyzed by prolyl hydroxylase domain enzymes (PHD1, 2, and 3), members of the Fe(II) and 2-oxoglutarate (2OG) oxygenase family. They require dioxygen as a cosubstrate, thus acting as the hypoxia-sensing component of the HIF system. The activity of PHD is suppressed by hypoxia, increasing both the abundance and activity of the HIF transcriptional complex. 
|In vitro||DMSO||7 mg/mL (19.86 mM)|
|In vivo||Add solvents individually and in order:
5% DMSO+30% PEG 300+ddH2O
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