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. 2017 Nov 23;7:16139. doi: 10.1038/s41598-017-16167-x

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© The Author(s) 2017

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Purification of hFGF21 from soluble MBP-hFGF21 expressed in E. coli BL21(DE3). (A) The flowchart of the purification process. (B) The fusion protein and hFGF21 after tag cleavage were both purified by IMAC. M, molecular weight makers; lane 1, total cell protein before IPTG induction as a negative control; lane 2, whole-cell lysate after IPTG induction; lane 3, the soluble fraction after cell sonication; lane 4, the MBP-hFGF21 fusion protein purified by IMAC (64.4 kDa); lane 5, the MBP tag was cleaved by TEV protease: the MBP tag (40.3 kDa), hFGF21 (19.45 kDa); lane 6, the final hFGF21 product (19.45 kDa).