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Expression of Soluble Native Human Proteins in Cell-Free
Extracts
Michael R. Slater, Ph.D., Robin Hurst, M.S., Becky
Pferdehirt, B.S., Doug White, M.S., Andrew Niles, M.S., Natalie
Betz, Ph.D., and Elaine Schenborn, Ph.D.
Promega Corporation
This article compares soluble native protein expression from Wheat Germ
Extract Plus and two E. coli expression systems using Flexi®
Vector plasmids encoding 55 different human proteins. While only three
of the proteins were expressed in the soluble fraction of E. coli
cells, the number of proteins expressed using the E. coli T7 S30
Extract System for Circular DNA increased to 42. However, only 10 of
those proteins were in the soluble fraction. In contrast, all 55
proteins were expressed in the soluble fraction of Wheat Germ Extract
Plus, and nearly fourfold higher yields were achieved using the Wheat
Germ Extract Plus in dialysis mode compared to batch mode.
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