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. 2018 Apr 26;8:6612. doi: 10.1038/s41598-018-24961-4

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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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Production and characterization of C7-Fc. (a) Schematic representation of C7-Fc. scFv of the C7 phage was fused with human IgG₁ Fc. The recombinant proteins were secreted from mammalian cells using the signal sequence of laminin γ2. (b) C7-Fc and Fc were purified from conditioned media using Protein A Sepharose. The proteins were separated on a 12.5% gel under reducing conditions. (c) ELISA using the C7-Fc antibody demonstrates binding to the recombinant extracellular domain of CD239 (Sol-Lu). (d) The binding affinity of C7-Fc was investigated using SPR. The sensorgrams represent the association and dissociation of the injected C7-Fc at different concentrations (as indicated) with and from (respectively) the immortalized recombinant CD239 (Lu-Fc). (e) Summary of kinetic parameters, k_a and k_d and the K_d of C7-Fc and mouse anti-CD239 mAbs.