Lorence Recombinant Gene Expression

3rd Auflage 2012
ISBN: 978-1-61779-433-9
Verlag: Humana Press
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band 824, 649 Seiten, eBook

Reihe: Methods in Molecular Biology

Studies related to recombinant gene expression have brought new advance such as  the emergence of the “omics” technologies. While Escherichia coli, Sacharomyces cerevisiae and insect cells continue to be the dominant production platforms of recombinant proteins. In Recombinant Gene Expression: Review and Protocols, Third Edition , expert researchers in the field detail many of the methods now commonly used to study recombinant gene expression. These include methods and techniques for bacteria, lower eukaryotes, fungi, plants and plant cells, and animals and animal cells. Written in the highly successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.   Authoritative and practical, Recombinant Gene Expression: Review and Protocols, Third Edition seeks to aid scientists in the further study of this crucially important research into recombinant gene expression.

Zielgruppe

Professional/practitioner

Autoren/Hrsg.

Lorence, Argelia

Inhaltsverzeichnis

Using Folding Promoting Agents in Recombinant Protein Production: A Review.-Routine Identity Confirmation of Recombinant Proteins by MALDI-TOF Mass Spectrometry.-A Matter of Packaging: Influence of Nucleosome Positioning on Heterologous Gene Expression.-Tools of the Trade: Developing Antibody-Based Detection Capabilities for Recombinant Proteins.-Heat-shock Protein Fusion Vectors for Improved Expression of Soluble Recombinant Proteins in Escherichia coli.-The use of a Flagellar Export Signal for the Secretion of Recombinant Proteins in Salmonella.-Optimization of Purification Protocols Based on the Step-by-step Monitoring of the Protein Aggregates in the Soluble Fractions.-Heterologous Protein Expression by Lactococcus lactis.-An Extended Suite of Genetic Tools for Use in Bacteria of the Halomonadaceae: An Overview.-Regulated Recombinant Protein Production in the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125.-A Novel Strategy for the Construction of Genomic Mutants of the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125.-A New Bacterial Co-expression System for Over-expressing Soluble Protein and Validating Protein-protein Interaction.-Heterologous High-level Gene Expression in the Photosynthetic Bacterium Rhodobacter capsulatus.-Plasmid DNA Production for Therapeutic Applications.-Recombinant Protein Production in the Eukaryotic Protozoan Parasite Leishmania tarentolae: A Review.-Expression of Multi-subunit Proteins in Leishmania tarentolae.-Recombinant Protein Production in Yeasts.-Yeasts as Tool for Heterologous Gene Expression.-The Cre/lox system: A Practical Tool to Efficiently Eliminate Selectable Markers in Fungal Endophytes.-Aptamer-regulated Expression of Essential Genes in Yeast.-Cloning and Expression of Hemicellulases from Aspergillus nidulans in Pichia pastoris.-A Thiamine-regulatable Epitope-tagged Protein Expression System in Fission.-Heterologous Gene Expression by Chromosomal Integration in Fission Yeast.-Genetic Engineering of Industrial Strains of Saccharomyces cerevisiae.-Recombinant Protein Production in Plants: Challenges and Solutions.-A Novel Plant Cell Bioproduction Platform for High-yield Secretion of Recombinant Proteins.-Super-promoter:TEV, a Powerful Gene Expression System for Tobacco Hairy Roots.-Bioseparation of Recombinant Proteins from Plant Extract with Hydrophobin Fusion Technology.-Quality Assessment of Recombinant Proteins Produced in Plants.-Cell-free Protein Synthesis as a Promising Expression System for Recombinant Proteins.-The use of Bacterial Artificial Chromosomes for Recombinant Protein Production in Mammalian Cell Lines.-Engineering the Chaperone Network of CHO Cells for Optimal Recombinant Protein Production and Authenticity.-High-throughput Baculovirus Expression in Insect Cells.-Recombinant Protein Expression in Milk of Livestock Species.