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. 2018 Aug 7;8:11813. doi: 10.1038/s41598-018-30216-z

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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CDX2 binds all the predicted binding-sites within the ST14 and SPINT1 enhancers in Caco-2 cells in vitro. Gel shift analysis of double-stranded [γ³²]ATP-labeled oligonucleotides wtCDX2-A (a) wtCDX2-B (b) wtCDX2-C (c) wtCDX2-D (d) wtCDX2-E (e) covering the putative CDX2 binding sites within the ST14 enhancer and one within the SPINT1 enhancer (f) [γ³²] ATP-labeled probes were incubated with Caco-2 nuclear cell extracts, and all resulted in shifted DNA/protein complexes, depicting that binding has taken place (lane 1). Competition by excess of unlabeled unspecific oligonucleotides (lane 2), unlabeled wild-type oligonucleotides (wt) (lane 3) and unlabeled mutated oligonucleotides (mut) (lane 4 (for C lanes 4 and 5)), were used for validating the specificity of the shifted DNA/protein complexes. Addition of anti-human CDX2 antibody was used for the supershift assays (lane 5 (for C lane 6)), and non-immune serum was used as negative control (lane 6 (for C lane 7)). Supershifted complexes are indicated by red arrows. Gels are representative of three independent EMSA assay experiments.