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. 2015 Aug 20;6(30):29847–29859. doi: 10.18632/oncotarget.4913

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Copyright: © 2015 Lu et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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A. Western blot and B. immunofluorescence showing expression and localization of NDRG1 and β-catenin in Hep3B and HepG2 cells, under normoxia and hypoxia (400× magnification; scale bars: 5 μm). C. Western blot showing that suppression of NDRG1 decreased cytoplasmic and nuclear β-catenin levels, with corresponding changes in GSK-3β 9ser, Nur77, and Cyclin D1. GAPDH and Histone3 are used as loading controls. D. The changes in NDRG1 and β-catenin protein levels and their cellular localizations (after NDRG1 suppression) were confirmed by immunofluorescence staining (400× magnification; scale bars: 5 μm). E. The changes in protein levels of NDRG1, β-catenin, GSK-3β 9ser, Nur77, and Cyclin D1 caused by suppression of NDRG1 under hypoxia were detected by Western blot. GAPDH and Histone3 are used as loading controls. F. The changes in NDRG1 and β-catenin protein levels and their cellular localizations (after NDRG1 suppression) were confirmed by immunofluorescence staining of HCC cells cultured under hypoxia (400× magnification; scale bars: 5 μm).