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. 2018 Oct 13;46(22):12139–12153. doi: 10.1093/nar/gky925

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Binding assay. (A) The electrophoretic pattern of SMAD2 (Trx-SMAD2C-2E) and MAN1 (His-Trx-MAN1(762–890)-SDED and its mutants) after a His-tag pull-down assay. The sizes of the protein markers (lane M) are indicated on the left side of the panel. (B) The relative affinities of the MAN1 mutants. Data are mean ± SEM from triplicate experiments. Bars sharing the same letter are not significantly different (one-way analysis of variance (ANOVA) with Tukey's multiple comparison test, P < 0.05). (C) The electrophoretic pattern of SMAD2 (His-Trx-SMAD2C-2E and its mutants) and MAN1 (Trx-MAN1(762–890)-SDED) after a His-tag pull-down assay. (D) The relative affinities of SMAD2 mutants. Data are mean ± SEM from triplicate experiments. Bars sharing the same letter are not significantly different (one-way ANOVA with Tukey's multiple comparison test, P < 0.05). (E) The electrophoretic pattern of SMAD1 (His-GST-SMAD1C-2E and its mutant) and MAN1 (Trx-MAN1(762–890)-SDED after a His-tag pull-down assay. (F) The relative affinity of a SMAD1 mutant. Data are mean ± SEM from triplicate experiments. *P < 0.05 compared to wild type (WT) by two-tailed Student's t-test. (G, H) Interaction of SMAD2 (Trx-SMAD2C-2E) with MAN1 (Trx-MAN1(762–890)-SDED) and SKI (His-Trx-SKI(16–40)-SDED) (G) or CBP (His-Trx-CBP(1941-1973)-SDED) (H). After the His-tag pull-down assay, the proteins were separated by SDS-PAGE. The gel images are representative of triplicate experiments.