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. 2017 Jul 26;7:6519. doi: 10.1038/s41598-017-06685-z

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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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Identification of a mutagenic candidate of EphA4 Fc. (A) SDS-PAGE analysis of reduced, protein A purified single, double and triple mutants (N > Q) and wild type EphA4 Fc proteins. (B) Sandwich ELISA of single, double and triple mutants (N > Q) and wild type EphA4 Fc protein clearance in Mus musculus (a) with calculated AUC_last values (b). Protein conformation and stability of the triple mutant compared to wild type EphA4 Fc proteins using SEC (C) and SV-AUC (D). The profiles reveal single predominant peaks for the triple mutant and wild type EphA4 Fc proteins indicating the absence of significantly different sized protein species. The chromatogram for the molecular weight standards has been included in the SEC profile with the mass of the standards noted above the respective peak. (E) Deconvoluted MS spectrum of the intact triple mutant of EphA4 Fc showing the masses of the predominate species.