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. 2015 Mar 24;15:147. doi: 10.1186/s12879-015-0906-z

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© Mossallam et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. 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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Illustration of the created plasmids and purified antigens described in the study. (A) Schematic representation of the construction of pQE31-FSm14/29, pQE31-Sm14 and pQE31-Sm29. Amp: β-lactamase coding sequence; ColE1: ColE1 origin of replication; PT5: T5 promoter; lac O: lac operator element; RBS: Ribosomal Binding Site; H: Hexahistidine tag; MCS: Multiple Cloning Site; T: Terminator; B: BamHI recognition site; K: KpnI recognition site; P: PstI recognition site. (B) SDS-PAGE of antigens purified from corresponding induced E. coli M15 (pREP4) strains. Lane 1, protein ladder; lanes 2 and 3, two successive elutions of the fusion antigen FSm14/29; lanes 4 and 5, two successive elutions of Sm14 antigen; lanes 6 and 7, two successive elutions of Sm29 antigen. Buffer E (pH 4.5) was used for elutions under denaturing conditions following induction with 0.3 mM IPTG at 25°C for 16 h.