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. 2017 Mar 3;292(17):6895–6909. doi: 10.1074/jbc.M116.769091

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© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 7. — Direct interaction of nectin-4 with the prolactin receptor. A, schematics of the domain structures of nectin-4, the PRLR, and their mutants. B, interaction of nectin-4 with PRLR. Ba, purity of the recombinant proteins used in this assay. Each purified recombinant protein (1 μg of protein each) was resolved by SDS-PAGE and stained with CBB. Bb, direct interaction of FLAG-Nectin-4-ΔCP with PRLR-ΔCP-Fc. The protein A-beads were conjugated with 50 pmol of Fc tag, PRLR-EC-Fc, and PRLR-ΔCP-Fc and mixed with 5 μm FLAG-Nectin-4-ΔCP or FLAG-Nectin-4-EC in a total volume of 30 μl at 4 °C for 2 h with gentle rotation. Each Fc-fusion protein was precipitated, and each interacted protein was subjected to silver staining and Western blotting using the anti-FLAG Ab. The results are representative of three independent experiments. SP, signal peptide; EC, extracellular; TM, transmembrane; CP, cytoplasmic; IB, immunoblotting; IP, immunoprecipitation.