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. 2020 Sep 29;18:371. doi: 10.1186/s12967-020-02544-0

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Analysis of the interaction of CREB with HLA-G. a In silico analysis of the HLA-G promoter sequence for predicted CREB binding sites. b The protein levels of HLA-G and of CREB were analyzed in RCC cell lines by Western blot. JEG-3 cells served as positive control. c The bar diagram shows the qPCR data expressed as means of three biological replicates of the chromatin immunoprecipitation. In comparison to the unspecific IgG control, the usage of anti-CREB antibody enriched HLA-G promoter regions as well as the internal positive control of the known CREB-bound RRM2 promoter sequence. The lower agarose gel exemplarily shows the enrichment of one HLA-G promoter fragment with the anti-CREB pull down in comparison to the isotype control of the antibody