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. 2022 Mar 12;23:199. doi: 10.1186/s12864-022-08419-6

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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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Fig. 1 — SDS-PAGE gel and western blot showing purification of RAD51A1. An SDS-PAGE gel is shown on the left, and a western blot probed with an α-ZmRAD51 antibody from rabbit is shown on the right. Gel lanes represent (1) supernatant, (2) pellet, (3) flow through, (4) wash, (5) marker, and (6) eluted protein. In the western blot on the right, lane (6) contains the eluted RAD51 protein probed with an α-ZmRAD51 antibody from rabbit. The RAD51A1 dimer band (92 KDa), indicated by an arrow, can be seen more clearly than the monomer band (46 KDa)