title: Bacterial expression and purification of biologically active mouse c-Fos proteins by selective codon optimization.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville 32610-0245, USA. tdeng@biochem.med.ufl.edu
authors.forename: T
authors.initials: T
authors.lastname: Deng
mesh_terms: D000818:Animals; D001120:Arginine / Q000235:genetics; D003062:Codon / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D005822:Genetic Vectors / Q000378:metabolism*; D051379:Mice; D016254:Mutagenesis, Insertional; D016760:Proto-Oncogene Proteins c-fos / Q000096:biosynthesis* / Q000235:genetics* / Q000302:isolation & purification
chemical_list: D003062:Codon; D016760:Proto-Oncogene Proteins c-fos; D001120:Arginine