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. 2017 Jul 26;7:6607. doi: 10.1038/s41598-017-06993-4

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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 oligomeric TNFR2 selective TNF muteins (A) Schematic representation and size exclusion chromatography analysis of the differently oligomerized TNF muteins sc-mTNF_R2, EHD2-sc-mTNF_R2, p53-sc-mTNF_R2 and GCN4-sc-mTNF_R2. (B) Coomassie staining of sc-mTNF_R2, EHD2-sc-mTNF_R2, p53-sc-mTNF_R2 and GCN4-sc-mTNF_R2. Purified TNF variants were analyzed by 8% SDS-PAGE under reducing (+2-ME) or non-reducing (−2-ME) conditions and stained with Coomassie. (C) Size exclusion chromatography analysis of the differently oligomerized TNF muteins sc-mTNF_R2, EHD2-sc-mTNF_R2, p53-sc-mTNF_R2 and GCN4-sc-mTNF_R2. (D,E) Binding of the TNF muteins to mouse (D) TNFR1 and (E) TNFR2 was analyzed by ELISA. Soluble recombinant mouse TNF (sTNF) was used as a positive control for binding to TNFR1 (n = 3 ± SEM).