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Recombinant protein production data after expression in the bacterium Escherichia coli.


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.

SUBMITTER: Cantu-Bustos JE 

PROVIDER: S-EPMC4792856 | biostudies-other | 2016 Jun

REPOSITORIES: biostudies-other

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Recombinant protein production data after expression in the bacterium Escherichia coli.

Cantu-Bustos J Enrique JE   Cano Del Villar Kevin D KD   Vargas-Cortez Teresa T   Morones-Ramirez Jose Ruben JR   Balderas-Renteria Isaias I   Zarate Xristo X  

Data in brief 20160304


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, temperat  ...[more]

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