Data presenting a modified bacterial expression vector for expressing and purifying Nus solubility-tagged proteins

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• 作者：Nidhi Gupta¹ ; Heng Wu ; Jonathan R. Terman ; ^{jonathan.terman@utsouthwestern.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Mical ; Plexin ; Semaphorin ; Repulsion ; Axon guidance ; Redox
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：September 2016
• 年：2016
• 卷：8
• 期：Complete
• 页码：1227-1231
• 全文大小：626 K

文摘

Bacteria are the predominant source for producing recombinant proteins but while many exogenous proteins are expressed, only a fraction of those are soluble. We have found that a new actin regulatory enzyme Mical is poorly soluble when expressed in bacteria but the use of a Nus fusion protein tag greatly increases its solubility. However, available vectors containing a Nus tag have been engineered in a way that hinders the separation of target proteins from the Nus tag during protein purification. We have now used recombinant DNA approaches to overcome these issues and reengineer a Nus solubility tag-containing bacterial expression vector. The data herein present a modified bacterial expression vector useful for expressing proteins fused to the Nus solubility tag and separating such target proteins from the Nus tag during protein purification.