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. 2017 Apr 17;10:185. doi: 10.1186/s13071-017-2127-3

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© The Author(s). 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 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.

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Fig. 1 — Expression of recombinant rLmlRAB and rLmlRABC in E. coli. Recombinant rLmlRAB as well as its carboxyl terminal part rLmlRABC were synthesized in BL21, purified by affinity chromatography over Ni-NTA resin. Western blot analysis shows the reactivity of the polyclonal anti-LmlRAB against the insoluble fraction of E. coli expressing both proteins rLmlRAB (a Lane 1) and LmlRABC (b Lane 1). The purified proteins rLmlRAB (a Lane 2) and rLmlRAB (b Lane 2) were also analyzed