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. 2017 Jul 3;7:4524. doi: 10.1038/s41598-017-04767-6

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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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Schematic representation of the postulated model for sRecE-dimer assembly from immobilized monomers. (1) sRecE is chelated to Ni²⁺-coated plates. The immobilization of sRecE at its C-terminal end presumably locks the protein in a specific conformation. (2) The plates are subsequently blocked and (3) reloaded with sRecE at high protein concentrations. (4) This enables interaction of the immobilized sRecE with the reloaded proteins and generates quaternary epitopes that can be recognized by E-dimer epitope dependent mAbs.