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. 2019 Jan 28;9:800. doi: 10.1038/s41598-018-37280-5

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© The Author(s) 2019

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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Purified recombinant fusion proteins (after transient Expi293 transfection, protein A affinity chromatography and desalting) were analysed by SDS/PAGE under non-reducing conditions. Five µg of protein were applied to each lane. Several independent batches of each protein were tested (IL-2/Fc in lanes 2–4 and K35E IL-2/Fc in lanes 5–8). Black arrow indicates the major band corresponding to the fusion protein homodimer. Grey arrows highlight the presence of denaturation-resistant aggregates with lower electrophoretic mobility in all samples of non-mutated IL-2/Fc.