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. 2022 Jan 21;53:5. doi: 10.1186/s13567-022-01023-2

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Identification of pET28a-PhoE by restriction enzyme digestion and detection of purified PhoE by SDS-PAGE and Western blot analysis. A The recombinant plasmid was subjected to endonuclease digestion and identified by agarose gel electrophoresis; M: 1 kb DNA marker Ι, 1: the pET28a-PhoE plasmid was double digested with restriction endonucleases BamHI and XhoI. B SDS-PAGE analysis of purified PhoE protein (38.8 kDa). M: Pre-stained protein size maker; expected PhoE protein is indicated in lane 1. C. Western blot analysis of purified PhoE protein. The primary antibody was an anti-His tag monoclonal antibody, and the secondary antibody was an HRP-conjugated goat anti-mouse IgG. M: Pre-Stained Protein maker; the specific band of PhoE was present in lane 2, and lane 1 was the lysate of the strain carrying the empty pET28a vector.