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. 2019 Oct 29;9:15507. doi: 10.1038/s41598-019-51947-7

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© The Author(s) 2019

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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Expression and purification of MaMIF. (A) SDS-PAGE analysis of purified MaMIF suggesting an approximate molecular mass of ~12.5 kDa for the monomer. (B) Superdex 75 10/300 GL analytical size-exclusion chromatography profile of MaMIF suggesting an apparent molecular mass of ~39 kDa in solution, corresponding to the size of a trimeric form. (C) CD spectrum of MaMIF confirming a properly folded protein. The pie chart in the inset shows the secondary structure make-up of the protein. (D) Western blot analysis with polyclonal anti-His and anti-MIF antibodies confirming the expressed protein to be MaMIF. (E) Western blot analysis with isotype-matched primary antibody shows the background level of antibody binding to the protein.