E. coli Gene Expression Protocols [Hardcover]

Peter E. Vaillancourt presents a collection of popular and emerging methodologies that take advantage of E. coli's ability to quickly and inexpensively express recombinant proteins. The authors focus on two areas of interest: the use of E. coli vectors and strains for production of pure, functional protein, and the use of E. coli as host for the functional screening of large collections of proteins and peptides. Among the cutting-edge techniques demonstrated are those for rapid high-level expression and purification of soluble and functional recombinant protein and those essential to functional genomics, proteomics, and protein engineering.Peter E. Vaillancourt presents a collection of popular and emerging methodologies that take advantage of E. coli's ability to quickly and inexpensively express recombinant proteins. The authors focus on two areas of interest: the use of E. coli vectors and strains for production of pure, functional protein, and the use of E. coli as host for the functional screening of large collections of proteins and peptides. Among the cutting-edge techniques demonstrated are those for rapid high-level expression and purification of soluble and functional recombinant protein and those essential to functional genomics, proteomics, and protein engineering.Cold-Inducible Promoters for Heterologous Protein ExpressionFran?ois Baneyx and Mirna MujacicDual-Expression Vectors for Efficient Protein Expression in Both E. coli and Mammalian CellsRebecca L. Mullinax, David T. Wong, Heidi A. Davis, Kerstein A. Padgett, and Joseph A. SorgeA Dual-Expression Vector Allowing Expression in E. coli and P. pastoris, Including New ModificationsAngelika Lueking, Sabine Horn, Hans Lehrach, and Dolores J. CahillPurification of Recombinant Proteins from E. coli by Engineered InteinsMing-Qun Xu and Thomas C. Evans, JrCalmodulin as an Affinity Purification TagSamu Melkko and Dario NeriCalmodulin-Binding Peptide as a Removable Affinity Tag for Protein PurificationWolfganglS.