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Recombinant Protein Expression, Part A, Volume 659 in the Methods in Enzymology series, highlights new advances in the field with this new volume presenting interesting chapters on Multiplexed analysis protein: Protein interactions of polypeptides translated in Leishmania cell-free system, MultiBac system and its applications, performance and recent, Production of antibodies in Shuffle, Designing hybrid-promoter architectures by engineering cis-acting DNA sites to enhance transcription in yeast, Designing hybrid-promoter architectures by engineering cis-acting DNA sites to deregulate transcription in yeast, Antibody or protein-based vaccine production in plants, Cell-free protein synthesis, Plant-based expression of biologic drugs, and much more.

Additional sections cover the Use of native mass spectrometry to guide detergent-based rescue of non-native oligomerization by recombinant proteins, Advancing overexpression and purification of recombinant proteins by pilot optimization through tandem affinity-buffer exchange chromatography online with native mass spectrometry, Method for High-Efficiency Fed-batch cultures of recombinant Escherichia coli, Method to transfer Chinese hamster ovary (CHO) shake flask experiments to the ambr® 250, and Expression of recombinant antibodies in Leishmania tarentolae.

  • Provides the authority and expertise of leading contributors from an international board of authors
  • Presents the latest release in the Methods in Enzymology serial
  • Updated release includes the latest information on Recombinant Protein Expression

1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Series Page - p. iii 5. Copyright - p. iii 6. Contributors - p. iii 7. Preface - p. xix 8. Section I: Bacterial hosts - p. xxiii 9. Chapter One: Starting a new recombinant protein production project in Escherichia coli - p. 3 10. Chapter Two: From the notebook to recombinant protein production in Escherichia coli: Design of expression vectors and gene cloning - p. 19 11. Chapter Three: Use of tandem affinity–buffer exchange chromatography online with native mass spectrometry for optimizing overexpression and purification of recombinant proteins - p. 37 12. Chapter Four: Purification, reconstitution, and mass analysis of archaeal RNase P, a multisubunit ribonucleoprotein enzyme - p. 71 13. Chapter Five: Production of antibodies in SHuffle Escherichia coli strains - p. 109 14. Chapter Six: Improved folding of recombinant protein via co-expression of exogenous chaperones - p. 145 15. Chapter Seven: Fusing an insoluble protein to GroEL apical domain enhances soluble expression in Escherichia coli - p. 171 16. Chapter Eight: Method for high-efficiency fed-batch cultures of recombinant Escherichia coli - p. 189 17. Chapter Nine: Fed-batch production of deuterated protein in Escherichia coli for neutron scattering experimentation - p. 219 18. Section II: Archaeal hosts - p. 240 19. Chapter Ten: Thermococcus kodakarensis provides a versatile hyperthermophilic archaeal platform for protein expression - p. 243 20. Chapter Eleven: Recombinant protein expression in Sulfolobus islandicus - p. 275 21. Chapter Twelve: High-level synthesis and secretion of laccase, a metalloenzyme biocatalyst, by the halophilic archaeon Haloferax volcanii - p. 297 22. Chapter Thirteen: Expression and tandem affinity purification of 20S proteasomes and other multisubunit complexes in Haloferax volcanii - p. 315 23. Chapter Fourteen: Purification and characterization of ribonucleoprotein effector complexes of Sulfolobus islandicus CRISPR-Cas systems - p. 327 24. Section III: Cell-free systems - p. 347 25. Chapter Fifteen: Guidelines for nucleic acid template design for optimal cell-free protein synthesis using an Escherichia coli reconstituted system or a lysate-based system - p. 351 26. Chapter Sixteen: Cell-free protein synthesis of CRISPR ribonucleoproteins (RNP) - p. 371 27. Chapter Seventeen: Leishmania tarentolae cell-free based approach for rapid anitbody–antigen interaction analysis - p. 391 28. Chapter Eighteen: Cell-free protein synthesis using Chinese hamster ovary cells - p. 411

Descripcion
Descripción

Recombinant Protein Expression, Part A, Volume 659 in the Methods in Enzymology series, highlights new advances in the field with this new volume presenting interesting chapters on Multiplexed analysis protein: Protein interactions of polypeptides translated in Leishmania cell-free system, MultiBac system and its applications, performance and recent, Production of antibodies in Shuffle, Designing hybrid-promoter architectures by engineering cis-acting DNA sites to enhance transcription in yeast, Designing hybrid-promoter architectures by engineering cis-acting DNA sites to deregulate transcription in yeast, Antibody or protein-based vaccine production in plants, Cell-free protein synthesis, Plant-based expression of biologic drugs, and much more.

Additional sections cover the Use of native mass spectrometry to guide detergent-based rescue of non-native oligomerization by recombinant proteins, Advancing overexpression and purification of recombinant proteins by pilot optimization through tandem affinity-buffer exchange chromatography online with native mass spectrometry, Method for High-Efficiency Fed-batch cultures of recombinant Escherichia coli, Method to transfer Chinese hamster ovary (CHO) shake flask experiments to the ambr® 250, and Expression of recombinant antibodies in Leishmania tarentolae.

  • Provides the authority and expertise of leading contributors from an international board of authors
  • Presents the latest release in the Methods in Enzymology serial
  • Updated release includes the latest information on Recombinant Protein Expression

1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Series Page - p. iii 5. Copyright - p. iii 6. Contributors - p. iii 7. Preface - p. xix 8. Section I: Bacterial hosts - p. xxiii 9. Chapter One: Starting a new recombinant protein production project in Escherichia coli - p. 3 10. Chapter Two: From the notebook to recombinant protein production in Escherichia coli: Design of expression vectors and gene cloning - p. 19 11. Chapter Three: Use of tandem affinity–buffer exchange chromatography online with native mass spectrometry for optimizing overexpression and purification of recombinant proteins - p. 37 12. Chapter Four: Purification, reconstitution, and mass analysis of archaeal RNase P, a multisubunit ribonucleoprotein enzyme - p. 71 13. Chapter Five: Production of antibodies in SHuffle Escherichia coli strains - p. 109 14. Chapter Six: Improved folding of recombinant protein via co-expression of exogenous chaperones - p. 145 15. Chapter Seven: Fusing an insoluble protein to GroEL apical domain enhances soluble expression in Escherichia coli - p. 171 16. Chapter Eight: Method for high-efficiency fed-batch cultures of recombinant Escherichia coli - p. 189 17. Chapter Nine: Fed-batch production of deuterated protein in Escherichia coli for neutron scattering experimentation - p. 219 18. Section II: Archaeal hosts - p. 240 19. Chapter Ten: Thermococcus kodakarensis provides a versatile hyperthermophilic archaeal platform for protein expression - p. 243 20. Chapter Eleven: Recombinant protein expression in Sulfolobus islandicus - p. 275 21. Chapter Twelve: High-level synthesis and secretion of laccase, a metalloenzyme biocatalyst, by the halophilic archaeon Haloferax volcanii - p. 297 22. Chapter Thirteen: Expression and tandem affinity purification of 20S proteasomes and other multisubunit complexes in Haloferax volcanii - p. 315 23. Chapter Fourteen: Purification and characterization of ribonucleoprotein effector complexes of Sulfolobus islandicus CRISPR-Cas systems - p. 327 24. Section III: Cell-free systems - p. 347 25. Chapter Fifteen: Guidelines for nucleic acid template design for optimal cell-free protein synthesis using an Escherichia coli reconstituted system or a lysate-based system - p. 351 26. Chapter Sixteen: Cell-free protein synthesis of CRISPR ribonucleoproteins (RNP) - p. 371 27. Chapter Seventeen: Leishmania tarentolae cell-free based approach for rapid anitbody–antigen interaction analysis - p. 391 28. Chapter Eighteen: Cell-free protein synthesis using Chinese hamster ovary cells - p. 411

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