کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8359775 | 1542321 | 2016 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Investigation of TtrD, an expressing recombinant fusion tag, in Escherichia coli
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Escherichia coli is widely used for expressing recombinant proteins, and several tags have been developed to improve protein solubility. However, expressing and purifying protein from other organisms is not always successful. In this study, we investigated the possibility of using TtrD as an expressing fusion tag in E. coli. Twenty RING finger domain containing human genes were expressed in E. coli grown at 37 °C and 18 °C and tested with four other fusion tags, namely His, SUMO, GST and MBP, for comparison. The results indicated that the soluble expressing ability of the tags was MBP, GST, TtrD, SUMO, and His in descending order. A one-column refolding process was used to purify the expressed proteins in inclusion bodies, and TtrD showed the strongest refolding ability. The results suggested that the TtrD tag enhanced recombinant protein solubility and refolding ability and might be a useful tag for protein expression in E. coli.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 120, April 2016, Pages 65-71
Journal: Protein Expression and Purification - Volume 120, April 2016, Pages 65-71
نویسندگان
Anqi Chen, Li Zhang, Shaohua Gu, Rong Tang, Yi Xie, Chaoneng Ji,