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. 2017 May 3;7:1416. doi: 10.1038/s41598-017-01641-3

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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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Characterization of the p.G202V protein in vitro. Transiently transfected Hela cells with plasmids harboring either the wild type HAND2 or the p.G202V variant were fixed and stained with an anti-Flag antibody. The secondary fluorescent antibody showed no change in the nuclear staining (in red) for both proteins as compared to the Hoechst staining (Magnification X40) (A). Western blot using the same anti-Flag antibody shows equal expression of both the wild type (wt) and mutated (mut) proteins in Hek293 cells, as well as the transiently overexpressed E47/Pan protein (B). Gel Shift analyses with increasing doses from the same nuclear extracts as in (C) were used on a consensus HAND binding site showed similar pattern of binding for both the wild type and mutant HAND2 proteins (D). The same pattern was observed when mixing the same amount of the HAND2 proteins with E47/Pan. The panel was separated by dotted lines to highlight the fact that the presented figure is a merge of two different gels run simultaneously.