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020 _a9781592593019
024 7 _a10.1385/1592593011
_2doi
040 _aES-MaUEC
_bspa
_cES-MaUEC
245 1 0 _aE. coli Gene Expression Protocols
_cedited by Peter E. Vaillancourt.
250 _a1st edition 2003
264 1 _aTotowa, NJ
_bHumana Press
_c2003
300 _a1 recurso en línea (XI, 347 páginas)
_b129 ilustraciones
336 _atexto
_btxt
_2rdacontent
337 _aelectrónico
_bc
_2rdamedia
338 _arecurso electrónico
_bcr
_2rdacarrier
347 _aarchivo de texto
_bPDF
490 0 _aMethods in Molecular Biology
_x1940-6029
_v205
505 0 _aCold-Inducible Promoters for Heterologous Protein Expression -- Dual-Expression Vectors for Efficient Protein Expression in Both E. coli and Mammalian Cells -- A Dual-Expression Vector Allowing Expression in E. coli and P. pastoris, Including New Modifications -- Purification of Recombinant Proteins from E. coli by Engineered Inteins -- Calmodulin as an Affinity Purification Tag -- Calmodulin-Binding Peptide as a Removable Affinity Tag for Protein Purification -- Maltose-Binding Protein as a Solubility Enhancer -- Thioredoxin and Related Proteins as Multifunctional Fusion Tags for Soluble Expression in E. coli -- Discovery of New Fusion Protein Systems Designed to Enhance Solubility in E. coli -- Assessment of Protein Folding/Solubility in Live Cells -- Improving Heterologous Protein Folding via Molecular Chaperone and Foldase Co-Expression -- High-Throughput Purification of PolyHis-Tagged Recombinant Fusion Proteins -- Co-Expression of Proteins in E. coli Using Dual Expression Vectors -- Small-Molecule Affinity-Based Matrices for Rapid Protein Purification -- Use of tRNA-Supplemented Host Strains for Expression of Heterologous Genes in E. coli -- Screening Peptide/Protein Libraries Fused to the ? Repressor DNA-Binding Domain in E. coli Cells -- Studying Protein-Protein Interactions Using a Bacterial Two-Hybrid System -- Using Bio-Panning of FLITRX Peptide Libraries Displayed on E. coli Cell Surface to Study Protein-Protein Interactions -- Use of Inteins for the In Vivo Production of Stable Cyclic Peptide Libraries in E. coli -- Hyperphage -- Combinatorial Biosynthesis of Novel Carotenoids in E. coli -- Using Transcriptional-Based Systems for In Vivo Enzyme Screening -- Identification of Genes Encoding Secreted Proteins Using Mini-OphoA Mutagenesis.
520 _aGene expression using E. coli as a host is carried out over a wide range of disciplines in academic and industrial laboratories. In E. coli Gene Expression Protocols, 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. Described in step-by-step detail to ensure robust, trouble-free results, each proven method has been written by a hands-on expert and includes extensive notes and practical tips for avoiding pitfalls. Even highly skilled researchers will find many time-saving techniques. Authoritative and highly practical, E. coli Gene Expression Protocols provides a state-of-the-art collection of tested methods for this powerful gene expression technology, offering today's investigators proven tools for success in the emerging fields of functional genomics and proteomics.
700 1 _aVaillancourt, Peter E
_eeditor literario
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
776 0 8 _iPrinted edition:
_z9781617373022
776 0 8 _iPrinted edition:
_z9781489927972
776 0 8 _iPrinted edition:
_z9781588290083
856 4 0 _uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592593011
_zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942 _2lcc
_cLE
988 _aSpringer_Protocols_2003
999 _c392884
_d392884