Recombinant protein production data after expression in the bacterium Escherichia coli

被引：4

作者：

Enrique Cantu-Bustos, J. ^{[1
]}

Cano del Villar, Kevin D. ^{[1
]}

Vargas-Cortez, Teresa ^{[1
]}

Ruben Morones-Ramirez, Jose ^{[1
]}

Balderas-Renteria, Isaias ^{[1
]}

Zarate, Xristo ^{[1
]}

机构：

[1] Univ Autonoma Nuevo Leon, Fac Ciencias Quim, Ave Univ S-N,Ciudad Univ, San Nicolas De Los Garza 66451, Nuevo Leon, Mexico

来源：

DATA IN BRIEF | 2016年 / 7卷

关键词：

Fusion protein; Affinity tag; Escherichia coli; CusF; GST;

D O I：

10.1016/j.dib.2016.02.074

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Fusion proteins have become essential for the expression and purification of recombinant proteins in Escherichia coil. The metal binding protein CusF has shown several features that make it an attractive fusion protein and affinity tag: "Expression and purification of recombinant proteins in Escherichia coil tagged with the metal binding protein CusF" (Cantu-Bustos et al., 2016 I). Here we present accompanying data from protein expression experiments; we tested different protein tags, temperatures, expression times, cellular compartments, and concentrations of inducer in order to obtain soluble protein and low formation of inclusion bodies. Additionally, we present data from the purification of the green fluorescent protein (GFP) tagged with CusF, using Ag(I) metal affinity chromatography. (C) 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/40).

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收藏

页码：502 / 508

页数：7

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