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. 2017 Apr 21;7:1005. doi: 10.1038/s41598-017-00691-x

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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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Decreased STAT1 activation, but enhanced STAT3 DNA-binding, upon NOD1 silencing. (a/b) Immature DCs were generated and transfected with a control siRNA or siRNA directed against NOD1 or NOD2. STAT activation was analysed by Western Blot. Transfected iDCs were stimulated with IL-10 for the indicated time points and tyrosine phosphorylation of STAT1 and STAT3 was detected by specific antibodies. To control for equal loading, total STAT protein and β-actin were detected. One of two independent experiments (a) and quantification of two experiments (b) are shown. Data represent mean and SD. (c) IL-10 (30 ng/ml)-induced STAT3 binding was analysed after 60 minutes by means of a STAT3 binding assay. STAT3 binding was normalised to total STAT3 protein in the cytosolic fraction, which was measured by Western Blot analysis. Data represent mean and SD of three independent experiments. For statistical analysis a one-way ANOVA with Tukey’s post hoc test was performed.