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. 2017 Sep 20;7:12030. doi: 10.1038/s41598-017-12364-w

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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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Functional analysis of cell-free synthesized antibody constructs by ELISA. (a) Autoradiograph derived from SDS-PAGE gel showing cell-free synthesized target proteins in the microsomal fraction (MF) and the supernatant fraction (SN2) after detergent-based release of target proteins from the lumen of microsomal vesicles. (b) ELISA analysis showing the specific binding of LC/HC (IgG) and scFv-Fc to its antigen SMAD2-P, but not to CXCR5 (non-related antigen). Samples analyzed by ELISA were treated likewise and tested in parallel in triplicate analysis. Starting concentrations in dilution 1:2 of LC/HC, scFv-Fc and HC control were 0.2 µg/mL each (total protein yield according to quantification via incorporation of ¹⁴C-leucine). Standard deviations were calculated from triplicate analysis. LC: antibody light chain; HC: antibody heavy chain; scFv-Fc: single-chain variable fragment Fc fusion; NTC: No template control.