The development of effective overproduction and purification approaches for ExuR transcription factor of Escherichia coli using affine chromatography

Abstract

A method for isolation and purification of the recombinant ExuR protein from Escherichia coli was
developed. Process includes cloning of the exuR gene into pGEMEX1 vector, followed by overproduction of
soluble protein in BL21 *(DE3) E. coli cells and a series of affine chromatography cycles on a column with
Ni-NTA agarose charged with nickel sulfate. This approach allows obtaining of electrophoretically
homogenious and functionally active ExuR protein for further investigation.