E. coli Gene Expression Protocols

1. Cold-Inducible Promoters for Heterologous Protein Expression
2. Dual-Expression Vectors for Efficient Protein Expression in Both E. coliand Mammalian Cells
3. ADual-Expression Vector Allowing Expression in E. coli and P. pastoris, Including New Modifications
4. Purification of Recombinant Proteins from E. coli by Engineered Intein
5. Calmodulin as an Affinity Purification Tag
6. Calmodulin-Binding Peptide as a Removable Affinity Tag for Protein Purification
7. Maltose-Binding Protein as a Solubility Enhancer
8. Thioredoxin and Related Proteins as Multifunctional Fusion Tags for Soluble Expression in E. col
9. Discovery of New Fusion Protein Systems Designed to Enhance Solubility inE. coli
10. Assessment of Protein Folding/Solubility in Live Cells
11. Improving Heterologous Protein Folding via Molecular Chaperone and Foldase Co-Expression
12. High-Throughput Purification of PolyHis-Tagged Recombinant Fusion Proteins
13. Co-Expression of Proteins in E. coliUsing Dual Expression Vector
14. Small-Molecule Affinity-Based Matrices for Rapid Protein Purificatio
15. Use of tRNA-Supplemented Host Strains for Expression of Heterologous Genes in E. coli
16. Screening Peptide/Protein Libraries Fused to the λ Repressor DNA-Binding Domain in E. coliCells
17. Studying Protein–Protein Interactions Using a Bacterial Two-Hybrid System
18. Using Bio-Panning of FLITRX Peptide Libraries Displayed on E. coli Cell Surface to Study Protein–Protein Interactions
19. Use of Inteins for the In Vivo Production of Stable Cyclic Peptide Libraries in E. coli
20. Hyperphage: Improving Antibody Presentation in Phage Display
21. Combinatorial Biosynthesis of Novel Carotenoids in E. col
22. Using Transcriptional-Based Systems for In Vivo Enzyme Screening
23. Identification of Genes Encoding Secreted Proteins Using Mini-OphoAMutagenesis

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.