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FEBS Lett. 1997 Jun 9;409(2):269-72.

Bacterial expression and purification of biologically active mouse c-Fos proteins by selective codon optimization.

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  • Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville 32610-0245, USA. tdeng@biochem.med.ufl.edu


A simple strategy using selective codon optimization was devised to express mouse c-Fos protein in high levels in E. coli. Ten arginine codons located in the basic region were optimized to achieve high levels of protein expression. The c-Fos protein was purified to near homogeneity and was demonstrated to be biologically active by assaying its several biological activities.

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