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. 2015 Apr 8;15:23. doi: 10.1186/s12896-015-0136-x

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© Yang 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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PAGE and immunoblotting analysis of the purification process of recombinant HP-NAP expressed in E. coli . The whole cell lysate (W) and soluble fraction (S) of E. coli BL21(DE3) expressing HP-NAP, the pooled fraction (P) of the unbound fraction and wash fractions containing HP-NAP from DEAE Sephadex chromatography, the dialyzed HP-NAP solution (D), and the filtrated HP-NAP solution (F) were analyzed by SDS-PAGE (A), native-PAGE (B), and immunoblotting (C). Molecular weights (M) in kDa are indicated on the left of the stained gels and the blot. Data were representative of at least three independent experiments.