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. 2018 Aug 10;8:11967. doi: 10.1038/s41598-018-30435-4

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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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Expression, protein trans splicing, and purification of eGFP- NpuDnaE_ΔC16 in E. coli prior to light triggered release. (A) WB using anti-polyhistidine antibody for the detection in the soluble fraction of E. coli lysate. Lanes: (1) molecular weight markers; (2) eGFP- NpuDnaE_ΔC16 (not induced: negative control); (3) eGFP- NpuDnaE_ΔC16 + peptide 1; (4) eGFP- NpuDnaE_ΔC16 + peptide 3 + 1 mM ZnCl₂; (5) eGFP- NpuDnaE_ΔC16 + peptide 3 + 1 mM TCEP. (*) indicate the mass of eGFP-His6. (B) Elution of the soluble protein fractions after Ni-NTA affinity chromatography, using UV-light for visualization, of the products of the protein trans splicing of eGFP- NpuDnaE_ΔC16 peptide 1. (C) SDS-PAGE stained with CBB of the first four washing steps and the elution steps. The uncropped images can be seen in Fig. S7.