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. 2017 Aug 3;7:7240. doi: 10.1038/s41598-017-07655-1

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© The Author(s) 2017

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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Confirmation of MRE on DYRK1A promoter by EMSA and ChIP. (A) The consensus MEF2 oligonucleotides were labelled with infrared fluorescence IRDye® 700 and used as probes. EMSA was performed as described in methods. DY-MRE is the oligonucleotide of −282 bp to −251 bp from DYRK1A promoter. Numbers of competitor indicates the molar excess of labelled oligonucleotides. (B) DY-MRE was labelled with infrared fluorescence IRDye® 700 IRDye. EMSA was performed as described in methods. Anti-MEF2D antibody was used in supershift. (C) ChIP was used to confirm the binding of MEF2D with DYRK1A promoter region. Anti-MEF2D antibody, anti-RNA Polymerase II and normal mouse IgG were used in chromatin immunoprecipitation from HEK293 cells. Primers to amplify a short DNA sequence spanning the putative DY-MRE site in DYRK1A promoter region and GAPDH were used for PCR. IgG and H₂O were used as the negative controls. (D) Western blot showed that the anti-MEF2D antibody actually immunoprecipitated MEF2D protein. The lower bands were antibody heavy chain.