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. 2017 Oct 25;7:13979. doi: 10.1038/s41598-017-14277-0

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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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Analysis of refolded and purified Zipbody mAb produced in E. coli. Refolded and purified anti-V. parahaemolyticus Zipbody clone G22 produced in E. coli SHuffle T7 Express was used. The purified fraction in these analyses was obtained by Ni-affinity chromatography. The left-hand lane in panels a and b indicates molecular size markers. Arrows show the expected size of the Zipbody proteins (which overlap). (a) Coomassie Brilliant Blue staining after SDS-PAGE. One microgram of the purified fraction was loaded. (b) Western blotting detecting Hc and Lc, with anti-HA tag-HRP and anti-His tag-HRP conjugated antibodies, respectively. Loaded protein amount = 0.1 µg. (c) Blitz sensorgram at various Zipbody mAb concentrations against inactivated V. parahaemolyticus cells, corrected with 0 nM Zipbody as the reference.