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. 2017 Aug 21;7:8360. doi: 10.1038/s41598-017-08641-3

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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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The purification of BsAb (CD3×HER2). (a) Purification workflow. In the first step, unreacted fragment A was removed by capturing on Sepharose affinity column through the His-tag. In the second step, the product was isolated from the rest of reaction mixture by protein A affinity chromatography to remove fragment B. (b) The chromatography of protein A purification of trans-spliced BsAb (CD3×HER2), Using pH gradient elution from pH 5.0 to pH 2.8. (c,d) SDS–PAGE (4 – 20%) analysis of the protein A elutions. Lanes: 1, Sample after the trans-splicing reaction of fragments A (CD3) and B (HER2); 2, Ni column Elution; 3, Ni column flow through; 4 to 14, fractions of protein A elution from 1 to 11 respectively.