Expression of functional full-length hSRC-1 in eukaryotic cells using modified vaccinia virus Ankara and baculovirus

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• 作者：Judit Osz ; Karine Pradeau-Aubreton ; Robert Drillien ; Nathalie Troffer-Charlier ; Isabelle Kolb-Cheynel ; Arnaud Poterszman ; Marc Ruff ; Dino Moras ; Natacha Rochel ; ^{rochel@igbmc.fr}
• 关键词：Recombinational cloning ; Protein purification ; Phosphoproteins ; Steroid receptor coactivator 1 ; Baculovirus expression system ; Mammalian expression system ; Modified vaccinia virus Ankara
• 刊名：Analytical Biochemistry
• 出版年：2012
• 出版时间：15 July, 2012
• 年：2012
• 卷：426
• 期：2
• 页码：106-108
• 全文大小：337 K

文摘

Purified protein expression level and quality are contingent upon specific host expression systems. This differential production is particularly observed for proteins of high molecular weight, hampering further structural studies. We developed an expression method aimed at producing proteins in Escherichia coli, insect, and mammalian systems. Our novel protocol was used to produce in large scale the full-length 160-kDa steroid receptor coactivator 1 (SRC-1), a coregulator of nuclear receptors. The results indicate that we can produce biologically active human SRC-1 in mammalian and insect cells in large scale.