Expression and purification of bioactive high-purity human S100A6 in Escherichia coli

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• 作者：Honglin He^a ; Tingxu Yang^b ; Shixiang Jia^c ; Ruliang Zhang^c ; Ping Tu^c ; Jin Gao^d ; Yunsheng Yuan^a ; Wei Han^d ; ^{weihan@sjtu.edu.cn} ; Yan Yu^a ; ^{yanyu@sjtu.edu.cn}
• 关键词：S100 protein ; S100A6 ; Prokaryotic expression ; Protein purification
• 刊名：Protein Expression and Purification
• 出版年：2012
• 期刊代码：184_10465928
• 类别：bio
• 出版时间：May, 2012
• 卷：83
• 期：1
• 页码：98-103
• 文件大小：752 K

摘要

S100A6, as a member of S100 protein family, have biological functions in cell proliferation, differentiation, morphology, cytoskeletal organization and apoptosis. In the last three decades, S100A6 has been caught more and more attention. Here, we introduced a simple and efficient method for producing high-purity recombinant human S100A6 from Escherichia coli culture with low level of endotoxin. We further demonstrated its biological activities for triggering SH-SY5Y cells apoptosis in vitro. These results can facilitate the study of physiological and pathological roles of S100A6 and other members of S100 family proteins.