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. 2018 Oct 22;9:4381. doi: 10.1038/s41467-018-06756-3

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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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Fig. 3 — The C-terminal of CYPJ interacts with TAB2 and TAB3. a Effects of CYPJ on NF-κB reporter activation induced by individually transfected components of the NF-κB signal pathway (N = 3). b, c Reciprocal co-IP assays determine the interaction between HA-CYPJ and Flag-TAB2 or Flag-TAB3 in 293T cells. d Endogenous co-IP assays evaluate the interaction between CYPJ and TAB2/TAB3 with or without TNF treatment for different time points in 293T cells. e Immunofluorescence microscopy observing the colocalization of pEGFP-CYPJ and Flag-TAB2 in HeLa cells. Scale bars, 20 μm. f Multiple sequence alignments of CYPJ proteins from different species. The three fragments of CYPJ are marked. g GST pull-down assays were performed using E.coli-expressed GST and GST-CYPJ fragments and lysates of 293T cells transfected with Flag-TAB2 or Flag-TAB3. h Co-IP assays detecting the interaction between Flag-TAB2/3 with HA-tagged FL or fragment-3 deleted CYPJ, # indicates a nonspecific band. Error bars indicate S.D.; n.s. no significance, * p < 0.05, ** p < 0.01 (two-tailed Student’s t-test)