ABSTRACT
The bacterium Escherichia coli is a well-characterized and extremely robust host for recombinant protein expression. Among other advantages, expression in E. coli permits efcient mutagenesis and DNA manipulation, rapid establishment and growth of expression cultures, and in ideal cases, high yields of puried proteins. Thus, the ability to express and purify antibody fragments from E. coli has been of great utility both for basic research into antibody structure and function and for the development of antibody reagents and therapeutics. However, because of the complex nature of the immunoglobulin molecule, the development of efcient expression protocols in bacteria faced signicant challenges, which have nonetheless been gradually surmounted through the efforts of many researchers.
