Recombinant protein production data after expression in the bacterium Escherichia coli
J. Enrique Cantu-Bustos, Kevin D. Cano del Villar, Teresa Vargas-Cortez and 3 more
Data in Brief · 2016
doi:10.1016/j.dib.2016.02.074 (opens in a new tab)
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Abstract
Fusion proteins have become essential for the expression and purification of recombinant proteins in Escherichia coli. 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 coli tagged with the metal-binding protein CusF'' (Cantu-Bustos et al., 2016 [1]). 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. Keywords: Fusion protein, Affinity tag, Escherichia coli, CusF, GST
Abstract licence: CC BY-NC
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