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Cell-free protein expression systems, also known as in vitro translation systems, are alternatives to cell-based protein expression methods. They provide a quick access to recombinant proteins with advantages include (1) no requirement for cell culture making them faster and easier to use (2) the ability to express proteins that are difficult or toxic to express in cell culture (3) an open format that allows for the addition of auxiliary components such as labels that can facilitate downstream detection or applications such as structural analyses and (4) the possibility of parallel synthesis of many proteins for screening. The template of cell-free protein synthesis can be DNA or RNA, where DNA based systems provide a much simplified approach by eliminating the in vitro RNA synthesis step. In this presentation, we will describe four DNA based cell-free protein expression systems prepared from different organisms (S30 extract from E. coli, insect cell extract, wheat germ extract and rabbit reticulocyte lysate) for protein expression and functional analysis.
We will demonstrate functional protein kinase expression and studies of protein-protein interactions in these systems in combination with HaloTag� fusion protein technology.

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