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. 2016 May 17;9:286. doi: 10.1186/s13071-016-1568-4

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© Long et al. 2016

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. 3 — Purification and identification of recombinant Ac-cathB-2. a SDS-PAGE analysis of all fractions through Nickel resin for purification. Lanes: Marker, molecular weight marker; 1, concentrated culture supernatant in binding buffer; 2, column flow-through; 3, binding buffer wash; 4 and 5, successive eluate fractions. b Identification of the purified rAc-cathB-2 by Western blot with an antiserum against Ac-cathB-2 expressed in E. coli and an anti-His antibody