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. 2020 Jan 28;10:1376. doi: 10.1038/s41598-020-57669-5

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© The Author(s) 2020

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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Panels A and B: Samples of CRTI protein purified from recombinant E. coli (Lot No. M20454-02) were incubated in the presence of SGF pH 1.2 containing pepsin for 0 min (lane 2) and 0.5, 1, 2, 5, 10, 20, 30 or 60 min at 37 °C (lanes 4–11) and then analyzed by SDS-PAGE. Gels were either stained for protein with colloidal blue G250 (panel A) or subjected to western immunoblot analysis (panel B) using rabbit anti-CRTI immunoglobulin (1:1000) and horseradish peroxidase-conjugated goat anti-rabbit IgG followed by precipitating substrate development. Control samples included CRTI protein diluted in gastric control fluid without pepsin (lane 1) and SGF solution containing pepsin (lane 12). Molecular weight standards are shown in lane 3 (adapted from GR2E-FFP submitted study reports).