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Therapeutic Fc-fusion proteins / / edited by Steven M. Chamow [and three others]
| Therapeutic Fc-fusion proteins / / edited by Steven M. Chamow [and three others] |
| Pubbl/distr/stampa | Weinheim : , : Wiley-VCH Verlag GmbH, , [2014] |
| Descrizione fisica | 1 online resource (400 p.) |
| Disciplina | 613.5 |
| Altri autori (Persone) | ChamowSteven Mark |
| Soggetto topico |
Proteins - Therapeutic use
Protein drugs |
| ISBN |
3-527-67527-2
3-527-67528-0 3-527-67529-9 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Therapeutic Fc-Fusion Proteins; Contents; Preface; List of Contributors; 1 Introduction: Antibody Structure and Function; 1.1 Introduction to Antibodies; 1.2 General Domain and Structure of IgG; 1.2.1 Structural Aspects Important for Fc Fusion(s); 1.2.1.1 Fc Protein-Protein Interactions; 1.2.1.2 Fc Glycosylation; 1.2.1.3 Hinge and Interchain Disulfide Bonds; 1.3 The Neonatal Fc Receptor; 1.3.1 FcRn Function and Expression; 1.3.2 Species Difference in FcRn; 1.3.3 Engineering to Modulate Pharmacokinetics; 1.3.3.1 Fc Engineering
1.3.3.2 Other Engineering Efforts to Modify PK of an IgG or Fc Fusion1.4 Introduction to FcgR- and Complement-Mediated Effector Functions; 1.4.1 Cell Lysis and Phagocytosis Mediation; 1.4.2 FcgR-Mediated Effector Functions; 1.4.2.1 FcgR Biology; 1.4.2.2 Expression Profiles; 1.4.2.3 Therapeutic Relevancy; 1.4.3 Complement; 1.4.3.1 C1q Biology; 1.4.3.2 Therapeutic Relevancy; 1.4.4 Modifying Effector Functions; 1.4.4.1 FcgR-Dependent Effector Function; 1.4.4.2 Engineering; 1.4.4.3 Glycoengineering; 1.4.4.4 Reducing and Silencing Effector Function; 1.5 Current Trends in Antibody Engineering 1.5.1 Bispecific1.5.2 Drug Conjugates; References; Part One: Methods of Production for Fc-Fusion Proteins; 2 Fc-Fusion Protein Expression Technology; 2.1 Introduction; 2.2 Expression Systems Used for Fc-Fusion Proteins; 2.2.1 Expression Using Mammalian Cell Lines; 2.2.1.1 Host Cells; 2.2.1.2 Codon Optimization; 2.2.1.3 Vectors; 2.2.1.4 Stable versus Transient Expression; 2.2.1.5 Viral Transduction and Transfection Methods; 2.2.2 Expression Using Prokaryotic Cells; 2.2.2.1 Vectors; 2.2.3 Expression Using Baculovirus/Insect Cells; 2.2.3.1 Host Cells; 2.2.3.2 Vectors 2.2.3.3 Additional Considerations2.3 Summary; References; 3 Cell Culture-Based Production; 3.1 Introduction; 3.2 Basic Aspects of Industrial Cell Culture; 3.2.1 The Central Role of the Production Cell Line; 3.2.2 Production Systems; 3.2.3 Production Mode: Fed-Batch or Perfusion?; 3.2.4 Scale-Up; 3.2.5 Raw Materials and Process Control; 3.2.6 How to Develop or Optimize a Culture Production Process for Fc-Fusion Molecules; 3.3 Speci.c Process Considerations for Fc-Fusion Molecules; 3.3.1 Product Quality Challenges; 3.3.2 Process Strategies and Process Parameters 3.3.2.1 Temperature and Misfolding3.3.2.2 Other Process Parameters; 3.3.2.3 Glycosylation; 3.4 Case Studies; 3.4.1 LTBr-Fc (Baminercept); 3.4.2 rFVIIIFc; 3.5 Conclusions; References; 4 Downstream Processing of Fc-Fusion Proteins; 4.1 Introduction and Overview of Fc-Fusion Proteins; 4.2 Biochemistry of Fc-Fusion Proteins; 4.3 Purification of Fc-Fusion Proteins from Mammalian Cells; 4.3.1 Platform Approaches for Downstream Purification; 4.3.2 Comparison of Protein A Chromatography, Viral Inactivation, and Polishing Steps; 4.4 Purification of Fc-Fusion Protein from Microbial Systems 4.5 Future Innovations in Fc-Fusion Protein Downstream Processing |
| Record Nr. | UNINA-9910138970203321 |
| Weinheim : , : Wiley-VCH Verlag GmbH, , [2014] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Therapeutic Fc-fusion proteins / / edited by Steven M. Chamow [and three others]
| Therapeutic Fc-fusion proteins / / edited by Steven M. Chamow [and three others] |
| Pubbl/distr/stampa | Weinheim : , : Wiley-VCH Verlag GmbH, , [2014] |
| Descrizione fisica | 1 online resource (400 p.) |
| Disciplina | 613.5 |
| Altri autori (Persone) | ChamowSteven Mark |
| Soggetto topico |
Proteins - Therapeutic use
Protein drugs |
| ISBN |
3-527-67527-2
3-527-67528-0 3-527-67529-9 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Therapeutic Fc-Fusion Proteins; Contents; Preface; List of Contributors; 1 Introduction: Antibody Structure and Function; 1.1 Introduction to Antibodies; 1.2 General Domain and Structure of IgG; 1.2.1 Structural Aspects Important for Fc Fusion(s); 1.2.1.1 Fc Protein-Protein Interactions; 1.2.1.2 Fc Glycosylation; 1.2.1.3 Hinge and Interchain Disulfide Bonds; 1.3 The Neonatal Fc Receptor; 1.3.1 FcRn Function and Expression; 1.3.2 Species Difference in FcRn; 1.3.3 Engineering to Modulate Pharmacokinetics; 1.3.3.1 Fc Engineering
1.3.3.2 Other Engineering Efforts to Modify PK of an IgG or Fc Fusion1.4 Introduction to FcgR- and Complement-Mediated Effector Functions; 1.4.1 Cell Lysis and Phagocytosis Mediation; 1.4.2 FcgR-Mediated Effector Functions; 1.4.2.1 FcgR Biology; 1.4.2.2 Expression Profiles; 1.4.2.3 Therapeutic Relevancy; 1.4.3 Complement; 1.4.3.1 C1q Biology; 1.4.3.2 Therapeutic Relevancy; 1.4.4 Modifying Effector Functions; 1.4.4.1 FcgR-Dependent Effector Function; 1.4.4.2 Engineering; 1.4.4.3 Glycoengineering; 1.4.4.4 Reducing and Silencing Effector Function; 1.5 Current Trends in Antibody Engineering 1.5.1 Bispecific1.5.2 Drug Conjugates; References; Part One: Methods of Production for Fc-Fusion Proteins; 2 Fc-Fusion Protein Expression Technology; 2.1 Introduction; 2.2 Expression Systems Used for Fc-Fusion Proteins; 2.2.1 Expression Using Mammalian Cell Lines; 2.2.1.1 Host Cells; 2.2.1.2 Codon Optimization; 2.2.1.3 Vectors; 2.2.1.4 Stable versus Transient Expression; 2.2.1.5 Viral Transduction and Transfection Methods; 2.2.2 Expression Using Prokaryotic Cells; 2.2.2.1 Vectors; 2.2.3 Expression Using Baculovirus/Insect Cells; 2.2.3.1 Host Cells; 2.2.3.2 Vectors 2.2.3.3 Additional Considerations2.3 Summary; References; 3 Cell Culture-Based Production; 3.1 Introduction; 3.2 Basic Aspects of Industrial Cell Culture; 3.2.1 The Central Role of the Production Cell Line; 3.2.2 Production Systems; 3.2.3 Production Mode: Fed-Batch or Perfusion?; 3.2.4 Scale-Up; 3.2.5 Raw Materials and Process Control; 3.2.6 How to Develop or Optimize a Culture Production Process for Fc-Fusion Molecules; 3.3 Speci.c Process Considerations for Fc-Fusion Molecules; 3.3.1 Product Quality Challenges; 3.3.2 Process Strategies and Process Parameters 3.3.2.1 Temperature and Misfolding3.3.2.2 Other Process Parameters; 3.3.2.3 Glycosylation; 3.4 Case Studies; 3.4.1 LTBr-Fc (Baminercept); 3.4.2 rFVIIIFc; 3.5 Conclusions; References; 4 Downstream Processing of Fc-Fusion Proteins; 4.1 Introduction and Overview of Fc-Fusion Proteins; 4.2 Biochemistry of Fc-Fusion Proteins; 4.3 Purification of Fc-Fusion Proteins from Mammalian Cells; 4.3.1 Platform Approaches for Downstream Purification; 4.3.2 Comparison of Protein A Chromatography, Viral Inactivation, and Polishing Steps; 4.4 Purification of Fc-Fusion Protein from Microbial Systems 4.5 Future Innovations in Fc-Fusion Protein Downstream Processing |
| Record Nr. | UNINA-9910813438303321 |
| Weinheim : , : Wiley-VCH Verlag GmbH, , [2014] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||