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. 2019 Dec 21;50:111. doi: 10.1186/s13567-019-0729-9

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© The Author(s) 2019

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

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Prokaryotic expression of mpIL-11. A Phylogenetic analysis and B amino acid (aa) sequence homologies of pIL-11 in comparison with other mammalian IL-11 molecules (monkey, human, mouse, bovine, chicken and sheep). Phylogenetic analysis based on the aa sequence of the IL-11 was constructed using MEGA version 5.0 software, utilizing the neighbor-joining method and bootstrapping for 1000 replicates with a value > 70%, in order to determine the percentage reliability of each internal node. The amino acid (aa) sequence homologies among the species were analyzed using the MegAlign program of DNAstar (DNAstar Inc.). C The protein mpIL-11 containing 600 bp was amplified specifically from mRNA of pig intestines and cloned into E. coli-expressing vector pET-32a. D SDS-PAGE analysis of the expression and purification of mpIL-11 from E. coli BL21(DE3)/pET-32a. 1: total protein of empty pET-30a vector; 2: protein supernatant including His-Trx-pIL-11; 3: affinity-purified His-Trx-pIL-11 protein; 4: unlabeled pIL-11 protein after enterokinase digestion. E A similar protein sample order to that of D was determined through Western blotting using a monoclonal antibody against His protein.