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. 2017 Aug 16;40(4):1165–1171. doi: 10.3892/ijmm.2017.3100

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Copyright: © Zhu et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Transforming growth factor-β1 (TGF-β1) stimulation enhances the interaction between partitioning-defective protein 6 (Par6) and Cdc42-interacting protein-4 (CIP4). NRK-52E cells were untreated (control) or incubated with TGF-β1 (20 ng/ml) for 72 h, and CIP4 interacted with Par6 in vitro. Cell lysates were prepared from control cells and TGF-β1-stimulated cells. Cell lysates were immunoprecipitated with anti-Par6 antibody. Immunopellets were analyzed by immunoblot analysis using anti-CIP4 antibody. IB, immunoblotting; IP, immunoprecipitation.