Info
- Utilizzare la checkbox di selezione a fianco di ciascun documento per attivare le funzionalità di stampa, invio email, download nei formati disponibili del (i) record.
Antibodies : a laboratory manual / edited by Ed Harlow, David Lane
| Antibodies : a laboratory manual / edited by Ed Harlow, David Lane |
| Pubbl/distr/stampa | Cold Spring Harbor : Cold Spring Harbor Laboratory Press, c1988 |
| Descrizione fisica | ix, 709 p. : ill. ; 28 cm |
| Disciplina | 571.967 |
| Altri autori (Persone) |
Harlow, Ed
Lane, David |
| Soggetto topico |
Immunochemistry - Laboratory manuals
Immunoglobulins - Laboratory manuals |
| ISBN | 0879693142 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNISALENTO-991003422589707536 |
| Cold Spring Harbor : Cold Spring Harbor Laboratory Press, c1988 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. del Salento | ||
| ||
Antibody glycosylation / / edited by Marija Pezer
| Antibody glycosylation / / edited by Marija Pezer |
| Pubbl/distr/stampa | Cham, Switzerland : , : Springer, , [2021] |
| Descrizione fisica | 1 online resource (585 pages) |
| Disciplina | 571.967 |
| Collana | Experientia Supplementum Ser |
| Soggetto topico |
Biochemical markers
Pharmacology Immunology Enginyeria de proteïnes Enginyeria bioquímica |
| Soggetto genere / forma | Llibres electrònics |
| ISBN | 3-030-76912-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Intro -- Foreword -- Contents -- Editor and Contributors -- Chapter 1: Micro-Heterogeneity of Antibody Molecules -- 1.1 Introduction -- 1.2 Disulfide Bond-Related Modifications -- 1.3 N- and C-Terminal Modifications -- 1.3.1 N-Terminal Modifications -- 1.3.2 C-Terminal Modifications -- 1.4 Chemical Modifications of Main-Chain Amino Acid Residues -- 1.4.1 Deamidation -- 1.4.2 Glycation -- 1.4.3 Oxidation -- 1.5 Aggregation -- 1.6 Glycosylation -- 1.6.1 IgG-Fc Oligosaccharide Chain -- 1.6.2 Fab Oligosaccharide Chain -- 1.7 Conclusion -- References -- Part I: Analytical Methods -- Chapter 2: Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 2.1 Introduction -- 2.1.1 Glycosylation -- 2.1.2 Immunoglobulins -- 2.2 Liquid Chromatography -- 2.2.1 Immunoglobulin Purification by Liquid Chromatography -- 2.2.1.1 Affinity Chromatography -- 2.2.1.2 Melon Gel Chromatography -- 2.2.1.3 Size-Exclusion Chromatography (SEC) -- 2.2.1.4 Ion-Exchange Chromatography (IEX) -- 2.2.2 N-Glycan Analysis by Liquid Chromatography -- 2.2.2.1 Glycan Release -- 2.2.2.2 Fluorescent Labeling Methods -- 2.2.2.3 Reducing Agent -- 2.2.2.4 Clean-Up Strategies -- 2.2.2.5 Detection of Labeled Glycans with (U)HPLC -- 2.2.2.6 N-Glycan Sequencing by Exoglycosidases -- 2.2.3 O-Glycan Analysis by Liquid Chromatography -- 2.2.4 Liquid Chromatography Coupled to Mass Spectrometry -- 2.2.4.1 Proteolytic Cleavage -- 2.2.4.2 Glycopeptide and Glycan Enrichment -- 2.2.4.3 Glycopeptide and Glycan Analysis by LC-MS -- 2.2.4.4 Analysis of Ig Glycosylation on the Subunit and Whole Protein Level -- 2.3 Lectin Techniques -- 2.3.1 Lectin Chromatography -- 2.3.2 Lectin Microarrays -- 2.4 Perspectives -- References -- Chapter 3: Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis -- 3.1 Basic Principles of Mass Spectrometry.
3.1.1 Ionization -- 3.1.2 Gas-Phase Separation and Detection -- 3.1.3 Tandem MS -- 3.2 Levels of IgG N-Glycosylation Analysis -- 3.3 Sample Preparation for IgG Glycosylation Analysis -- 3.3.1 Protein A, G, and L Affinity Chromatography for IgG Enrichment from Biological Samples -- 3.3.1.1 Protein A -- 3.3.1.2 Protein G -- 3.3.1.3 Protein L -- 3.3.1.4 Recombinant Fusion Proteins and Alternative Scaffolds -- 3.3.2 Sample Preparation for Released IgG Glycan Analysis -- 3.3.2.1 Chemical and Enzymatic Glycan Release -- 3.3.3 Fluorescent and Isotopic Glycan Labeling -- 3.3.4 Sample Preparation for Glycopeptide Mapping and Subclass-Specific IgG Fc Glycosylation Analysis -- 3.3.4.1 Enzymatic Digestion -- 3.3.4.2 Stable Isotope Glycopeptide Labeling -- 3.3.4.3 Glycan and Glycopeptide Enrichment and Purification Strategies -- 3.4 Deciphering the IgG Glycan Structure -- 3.4.1 Fragmentation -- 3.4.2 Fragmentation Nomenclature -- 3.4.3 Fragmentation Candidates -- 3.4.3.1 Fragmentation of Glycopeptides -- 3.4.3.2 Fragmentation of Released Glycans -- 3.4.4 Ionization Polarity of MS Analysis -- 3.4.4.1 Example of Positive Ion Mode Fragmentation -- 3.4.4.2 Example of Negative Ion Mode Fragmentation -- 3.4.5 Exoglycosidase Digestion Monitored by MS -- 3.5 Selected Approaches for IgG Glycosylation Analysis -- 3.5.1 MALDI-MS -- 3.5.1.1 Intact Proteins and Glycopeptides -- 3.5.1.2 Released N-Glycans -- 3.5.1.3 Sialic Acid Stability -- 3.5.1.4 Matrix Substances for MALDI-MS -- 3.5.1.5 MALDI-MS for High-Throughput and Quantitative Analysis -- 3.5.2 LC-MS for IgG Glycosylation Analysis -- 3.5.2.1 Coupling LC to MS for Enhanced Separation and Structural Characterization -- 3.5.2.2 HILIC-UHPLC-MS -- 3.5.2.3 RP-LC-MS -- 3.5.2.4 PGC for Enhanced Isomeric Glycan Separation -- 3.5.2.5 Anion Exchange LC-MS -- 3.5.2.6 Challenges of Miniaturization. 3.5.3 Capillary Electrophoresis-Mass Spectrometry -- 3.6 Perspectives -- References -- Chapter 4: Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 4.1 Historical Background -- 4.2 Background: Principles of Capillary (Gel) Electrophoresis (C(G)E) -- 4.3 Performance, Benefits, and Potentials of Capillary (Gel) Electrophoresis C(G)E -- 4.4 Data Analysis and Interpretation -- 4.5 Exoglycosidase Sequencing of Glycans -- 4.6 Coupling Capillary Electrophoresis with Mass Spectrometry -- 4.7 Latest Developments: Miniaturization of CE Systems-Microchip CE -- 4.8 Application of C(G)E for Immunoglobulin Analysis -- 4.9 Conclusion -- References -- Chapter 5: Automation of Immunoglobulin Glycosylation Analysis -- 5.1 Introduction -- 5.1.1 Biopharmaceutical Glycomics -- 5.1.2 Clinical Glycomics -- 5.1.3 Towards High-Throughput Glycomics -- 5.1.4 Robotics: The Ultimate High-Throughput Solution? -- 5.2 Automation of Glycomics Sample Preparation -- 5.2.1 Sample Origins and Protein Purification -- 5.2.1.1 Serum and Plasma -- 5.2.1.2 Therapeutic Antibody Glycoproteins -- 5.2.2 Preparing Glycans for Analysis: Glycan Release, Derivatization and Clean-Up -- 5.2.2.1 Plasma and Serum -- Automated Methods for N-Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.2.2 Therapeutic Antibody Glycoproteins -- Automated Methods for N-Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.3 Automated Methods for Glycopeptide Preparation -- 5.3 Commentary -- 5.4 Future Perspectives -- 5.5 Conclusions -- References -- Chapter 6: Bioinformatics in Immunoglobulin Glycosylation Analysis -- 6.1 Introduction. 6.2 Glycomic Data Collection and Processing -- 6.2.1 Reference Databases -- 6.2.2 Identification and Quantification Software Tools -- 6.3 Glycoproteomics Data Collection and Processing -- 6.3.1 Reference Databases -- 6.3.2 Identification Software Tools -- 6.3.3 Quantification Software Tools -- 6.4 Data Integration with Other Omics -- 6.5 Practical Examples -- 6.5.1 Glycomic Data Processing -- 6.5.1.1 Software Required -- 6.5.1.2 Glycan Composition Determination -- 6.5.1.3 Annotation of MS and MS/MS Glycomics Spectra -- 6.5.1.4 Convert Raw Mass Spectrometry Data to mzXML -- 6.5.1.5 Skyline for Glycomics Quantitation -- 6.5.1.6 Setting Up Transition List -- 6.5.2 Glycopeptide Data Processing for Enriched Immunoglobulins -- 6.5.2.1 Software Required -- 6.5.2.2 Glycosylation Site Identification Based on MS2 -- 6.5.2.3 Glycoform Identification Based on MS1 -- 6.5.2.4 Targeted Glycopeptide Quantification -- 6.5.3 Visualizing Profiles -- 6.5.3.1 Structural Dependencies Brought Out by GlyConnect Compozitor -- 6.5.3.2 Comparing Profiles with Glynsight -- 6.6 Conclusion -- References -- Part II: Biosynthesis and Regulation -- Chapter 7: N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome -- 7.1 Introduction -- 7.2 Biosynthesis of N-Glycans in the Endoplasmic Reticulum -- 7.2.1 Building Blocks for N-Glycan Synthesis -- 7.2.2 Precursor Synthesis and Its Attachment to Nascent Polypeptide Chains -- 7.2.3 N-Glycan Processing in the ER and Quality Control -- 7.3 N-Glycan Processing in the Golgi Apparatus -- 7.3.1 N-Glycosylation of Immunoglobulins -- 7.4 Golgi Microenvironment Is Important for Normal Processing and Maturation of N-Glycans -- 7.4.1 Golgi pH Homeostasis -- 7.4.2 Golgi Ion Homeostasis -- 7.4.3 Golgi Redox State -- 7.5 Concluding Remarks -- References -- Chapter 8: Genetic Regulation of Immunoglobulin G Glycosylation. 8.1 Introduction -- 8.2 Heritability of the Human IgG N-Glycome -- 8.3 Linkage Studies of Mouse N-glycome -- 8.4 Genome-Wide Association Studies of Human N-Glycome -- 8.4.1 Genomic Loci Associated with IgG N-Glycosylation -- 8.4.1.1 Chromosome 1 -- 8.4.1.2 Chromosome 3 -- 8.4.1.3 Chromosome 5 -- 8.4.1.4 Chromosome 6 -- 8.4.1.5 Chromosome 7 -- 8.4.1.6 Chromosome 9 -- 8.4.1.7 Chromosome 11 -- 8.4.1.8 Chromosome 14 -- 8.4.1.9 Chromosome 17 -- 8.4.1.10 Chromosome 21 -- 8.4.1.11 Chromosome 22 -- 8.4.2 Suggestive Associations -- 8.4.3 Functional Network of Loci Associated with IgG Glycosylation -- 8.5 Pleiotropy with Complex Traits and Diseases -- 8.6 Conclusions -- References -- Chapter 9: Epigenetics of Immunoglobulin G Glycosylation -- 9.1 Introduction -- 9.2 Regulation of Glycosyltransferases by Transcription Factors -- 9.3 Epigenetic Regulation of IgG Glycosylation -- 9.4 The Role of miRNAs in Protein N-Glycosylation -- 9.5 Conclusions -- References -- Chapter 10: Immunoglobulin G Glycosylation Changes in Aging and Other Inflammatory Conditions -- 10.1 Premise -- 10.2 IgG Glycosylation -- 10.3 Changes in IgG Asn297 Glycans Associated with Inflammatory Diseases -- 10.4 IgG Glycosylation as a Predictor of Disease Onset, Progression, and Therapy Response -- 10.4.1 Prediction of Disease Onset -- 10.4.2 Prediction of Progression and Therapy Response -- 10.5 IgG Glycosylation in Aging -- 10.6 The Inflammaging Is a Link Between Aging and Inflammation -- 10.7 How Altered IgG Glycosylation Drives Inflammation -- 10.7.1 Activation of Complement Through the Lectin or the Classical Pathways -- 10.7.2 Binding to Fcγ Receptors -- 10.7.3 Binding on Lectin Receptors of Antigen-Presenting Cells: Role in the Intravenous Administration of High Doses IgG (IVIG) -- 10.7.4 Anti IgG Autoantibodies -- 10.8 Molecular Bases of N-Glycosylation Changes -- 10.9 Conclusions. References. |
| Record Nr. | UNINA-9910506382203321 |
| Cham, Switzerland : , : Springer, , [2021] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Catalytic antibodies [[electronic resource] /] / edited by Ehud Keinan
| Catalytic antibodies [[electronic resource] /] / edited by Ehud Keinan |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
| Descrizione fisica | 1 online resource (618 p.) |
| Disciplina |
571.967
616.0798 |
| Altri autori (Persone) | KeinanEhud |
| Soggetto topico |
Monoclonal antibodies
Antibody-enzyme conjugates |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-52020-5
9786610520206 3-527-60366-2 3-527-60505-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Catalytic Antibodies; Foreword; Table of Contents; Preface; List of Contributors; 1 Immunological Evolution of Catalysis; 1.1 Introduction; 1.2 Parallels between Antibody and Enzyme Evolution; 1.3 Evolution of Catalytic Antibodies; 1.4 Ferrochelatase Antibody 7G12 - Evolution of the Strain Mechanism; 1.5 Esterase Antibody 48G7 - Effect of Distant Mutations on Catalysis; 1.6 Sulfur Oxidase Antibody 28B4 - Incremental Changes in Evolution; 1.7 Oxy-Cope Antibody AZ28 - Evolution of Conformational Diversity in Catalysis
1.8 Diels-Alderase Antibody 39A11 - Evolution of a Polyspecific Antibody combining Site1.9 Conclusions; References; 2 Critical Analysis of Antibody Catalysis; 2.1 Introduction; 2.2 Exploiting Antibodies as Catalysts; 2.3 Catalytic Efficiency; 2.4 Hapten Design; 2.5 Representative Catalytic Antibodies; 2.5.1 Proximity Effects; 2.5.1.1 Sigmatropic Rearrangements; 2.5.1.2 Cycloadditions; 2.5.2 Strain; 2.5.2.1 Ferrochelatase Mimics; 2.5.2.2 Other Systems; 2.5.3 Electrostatic Catalysis; 2.5.3.1 Acyl Transfer Reactions; 2.5.4 Functional Groups; 2.5.4.1 Aldolases; 2.6 Perspectives 2.6.1 General Lessons from Comparisons of Enzymes and Antibodies2.6.2 How efficient does catalysis need to be?; 2.6.3 Strategies for Optimizing Efficiency; 2.6.3.1 Better Haptens; 2.6.3.2 Screening; 2.6.3.3 Engineering; 2.6.3.4 Selection; 2.6.3.5 Other Scaffolds; 2.7 Conclusions; References; 3 Theoretical Studies of Antibody Catalysis; 3.1 Introduction; 3.2 Questions Subject to Theoretical Elucidation; 3.2.1 Predicting Antibody Structure from Sequence; 3.2.2 Predicting Binding Modes and Binding Energies; 3.2.3 Understanding Antibody Catalysis [14]; 3.2.4 General Considerations 3.3 Hydrolytic Antibodies3.3.1 Gas and Solution Phase Hydrolysis of Aryl Esters; 3.3.2 Hapten Fidelity; 3.3.3 Theoretical Exploration of Antibody Catalysis; 3.3.3.1 16G3; 3.3.3.2 6D9; 3.3.3.3 43C9; 3.3.3.4 CNJ206; 3.3.3.5 48G7; 3.3.3.6 17E8 and 29G11; 3.4 Cationic Cyclizations; 3.4.1 Antibody Catalysis of Solvolysis; 3.4.2 Antibody-Catalyzed Hydroxyepoxide Cyclization; 3.5 Antibody-Catalyzed Diels-Alder and retro-Diels-Alder Reactions; 3.5.1 The Most Efficient endo-Diels-Alderase 1E9; 3.5.2 endo-Diels-Alderase 39A11 and its Germline Precursor; 3.5.3 exo-Diels-Alderase 13G5 3.5.4 retro-Diels-Alderase 10F113.6 Other Antibody-Catalyzed Pericyclic Reactions; 3.6.1 Oxy-Cope Rearrangement Catalyzed by Antibody AZ-28; 3.6.2 1,3-Dipolar Cycloaddition Catalyzed by Antibody 29G12; 3.6.3 Chorismate-Prephenate Claisen Rearrangement Catalyzed by Antibody 1F7; 3.7 Antibody-Catalyzed Carboxybenzisoxazole Decarboxylation; 3.8 Summary; References; 4 The Enterprise of Catalytic Antibodies: A Historical Perspective; 4.1 Introduction; 4.2 Methods; 4.3 Results; 4.3.1 The Conceptual Origins of Catalytic Antibodies; 4.3.2 Tapping the Immune System for Catalysts; 4.4 Conclusions References |
| Record Nr. | UNINA-9910143966603321 |
| Weinheim, : Wiley-VCH | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Catalytic antibodies [[electronic resource] /] / edited by Ehud Keinan
| Catalytic antibodies [[electronic resource] /] / edited by Ehud Keinan |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
| Descrizione fisica | 1 online resource (618 p.) |
| Disciplina |
571.967
616.0798 |
| Altri autori (Persone) | KeinanEhud |
| Soggetto topico |
Monoclonal antibodies
Antibody-enzyme conjugates |
| ISBN |
1-280-52020-5
9786610520206 3-527-60366-2 3-527-60505-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Catalytic Antibodies; Foreword; Table of Contents; Preface; List of Contributors; 1 Immunological Evolution of Catalysis; 1.1 Introduction; 1.2 Parallels between Antibody and Enzyme Evolution; 1.3 Evolution of Catalytic Antibodies; 1.4 Ferrochelatase Antibody 7G12 - Evolution of the Strain Mechanism; 1.5 Esterase Antibody 48G7 - Effect of Distant Mutations on Catalysis; 1.6 Sulfur Oxidase Antibody 28B4 - Incremental Changes in Evolution; 1.7 Oxy-Cope Antibody AZ28 - Evolution of Conformational Diversity in Catalysis
1.8 Diels-Alderase Antibody 39A11 - Evolution of a Polyspecific Antibody combining Site1.9 Conclusions; References; 2 Critical Analysis of Antibody Catalysis; 2.1 Introduction; 2.2 Exploiting Antibodies as Catalysts; 2.3 Catalytic Efficiency; 2.4 Hapten Design; 2.5 Representative Catalytic Antibodies; 2.5.1 Proximity Effects; 2.5.1.1 Sigmatropic Rearrangements; 2.5.1.2 Cycloadditions; 2.5.2 Strain; 2.5.2.1 Ferrochelatase Mimics; 2.5.2.2 Other Systems; 2.5.3 Electrostatic Catalysis; 2.5.3.1 Acyl Transfer Reactions; 2.5.4 Functional Groups; 2.5.4.1 Aldolases; 2.6 Perspectives 2.6.1 General Lessons from Comparisons of Enzymes and Antibodies2.6.2 How efficient does catalysis need to be?; 2.6.3 Strategies for Optimizing Efficiency; 2.6.3.1 Better Haptens; 2.6.3.2 Screening; 2.6.3.3 Engineering; 2.6.3.4 Selection; 2.6.3.5 Other Scaffolds; 2.7 Conclusions; References; 3 Theoretical Studies of Antibody Catalysis; 3.1 Introduction; 3.2 Questions Subject to Theoretical Elucidation; 3.2.1 Predicting Antibody Structure from Sequence; 3.2.2 Predicting Binding Modes and Binding Energies; 3.2.3 Understanding Antibody Catalysis [14]; 3.2.4 General Considerations 3.3 Hydrolytic Antibodies3.3.1 Gas and Solution Phase Hydrolysis of Aryl Esters; 3.3.2 Hapten Fidelity; 3.3.3 Theoretical Exploration of Antibody Catalysis; 3.3.3.1 16G3; 3.3.3.2 6D9; 3.3.3.3 43C9; 3.3.3.4 CNJ206; 3.3.3.5 48G7; 3.3.3.6 17E8 and 29G11; 3.4 Cationic Cyclizations; 3.4.1 Antibody Catalysis of Solvolysis; 3.4.2 Antibody-Catalyzed Hydroxyepoxide Cyclization; 3.5 Antibody-Catalyzed Diels-Alder and retro-Diels-Alder Reactions; 3.5.1 The Most Efficient endo-Diels-Alderase 1E9; 3.5.2 endo-Diels-Alderase 39A11 and its Germline Precursor; 3.5.3 exo-Diels-Alderase 13G5 3.5.4 retro-Diels-Alderase 10F113.6 Other Antibody-Catalyzed Pericyclic Reactions; 3.6.1 Oxy-Cope Rearrangement Catalyzed by Antibody AZ-28; 3.6.2 1,3-Dipolar Cycloaddition Catalyzed by Antibody 29G12; 3.6.3 Chorismate-Prephenate Claisen Rearrangement Catalyzed by Antibody 1F7; 3.7 Antibody-Catalyzed Carboxybenzisoxazole Decarboxylation; 3.8 Summary; References; 4 The Enterprise of Catalytic Antibodies: A Historical Perspective; 4.1 Introduction; 4.2 Methods; 4.3 Results; 4.3.1 The Conceptual Origins of Catalytic Antibodies; 4.3.2 Tapping the Immune System for Catalysts; 4.4 Conclusions References |
| Record Nr. | UNINA-9910829843303321 |
| Weinheim, : Wiley-VCH | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
DNA deamination and the immune system [[electronic resource] ] : AID in health and disease / / editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou
| DNA deamination and the immune system [[electronic resource] ] : AID in health and disease / / editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou |
| Pubbl/distr/stampa | London, : Imperial College Press, 2011 |
| Descrizione fisica | 1 online resource (232 p.) |
| Disciplina | 571.967 |
| Altri autori (Persone) |
FugmannSebastian
DiazMarilyn PapavasiliouNina |
| Collana | Molecular medicine and medicinal chemistry |
| Soggetto topico |
DNA
Immune system |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-283-14344-5
9786613143440 1-84816-593-5 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Preface; Contents; List of Tables; List of Figures; Chapter 1 Introduction; Chapter 2 Switch Regions, ChromatinAccessibility and AID Targeting; Chapter 3 Cis-Regulatory Elements that Target AID to Immunoglobulin Loci; Chapter 4 Partners in Diversity: The Search for AID Co-Factors; Chapter 5 Resolution of AID Lesions in Class Switch Recombination; Chapter 6 Error-Prone and Error-Free Resolution of AID Lesions in SHM; Chapter 7 Regulatory Mechanisms of AID Function; Chapter 8 AID in Immunodeficiency and Cancer; Chapter 9 AID in Aging and in Autoimmune Disease; Index |
| Record Nr. | UNINA-9910461619003321 |
| London, : Imperial College Press, 2011 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
DNA deamination and the immune system [[electronic resource] ] : AID in health and disease / / editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou
| DNA deamination and the immune system [[electronic resource] ] : AID in health and disease / / editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou |
| Pubbl/distr/stampa | London, : Imperial College Press, 2011 |
| Descrizione fisica | 1 online resource (232 p.) |
| Disciplina | 571.967 |
| Altri autori (Persone) |
FugmannSebastian
DiazMarilyn PapavasiliouNina |
| Collana | Molecular medicine and medicinal chemistry |
| Soggetto topico |
DNA
Immune system |
| ISBN |
1-283-14344-5
9786613143440 1-84816-593-5 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Preface; Contents; List of Tables; List of Figures; Chapter 1 Introduction; Chapter 2 Switch Regions, ChromatinAccessibility and AID Targeting; Chapter 3 Cis-Regulatory Elements that Target AID to Immunoglobulin Loci; Chapter 4 Partners in Diversity: The Search for AID Co-Factors; Chapter 5 Resolution of AID Lesions in Class Switch Recombination; Chapter 6 Error-Prone and Error-Free Resolution of AID Lesions in SHM; Chapter 7 Regulatory Mechanisms of AID Function; Chapter 8 AID in Immunodeficiency and Cancer; Chapter 9 AID in Aging and in Autoimmune Disease; Index |
| Record Nr. | UNINA-9910789405503321 |
| London, : Imperial College Press, 2011 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
DNA deamination and the immune system : AID in health and disease / / editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou
| DNA deamination and the immune system : AID in health and disease / / editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | London, : Imperial College Press, 2011 |
| Descrizione fisica | 1 online resource (232 p.) |
| Disciplina | 571.967 |
| Altri autori (Persone) |
FugmannSebastian
DiazMarilyn PapavasiliouNina |
| Collana | Molecular medicine and medicinal chemistry |
| Soggetto topico |
DNA
Immune system |
| ISBN |
1-283-14344-5
9786613143440 1-84816-593-5 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Preface; Contents; List of Tables; List of Figures; Chapter 1 Introduction; Chapter 2 Switch Regions, ChromatinAccessibility and AID Targeting; Chapter 3 Cis-Regulatory Elements that Target AID to Immunoglobulin Loci; Chapter 4 Partners in Diversity: The Search for AID Co-Factors; Chapter 5 Resolution of AID Lesions in Class Switch Recombination; Chapter 6 Error-Prone and Error-Free Resolution of AID Lesions in SHM; Chapter 7 Regulatory Mechanisms of AID Function; Chapter 8 AID in Immunodeficiency and Cancer; Chapter 9 AID in Aging and in Autoimmune Disease; Index |
| Record Nr. | UNINA-9910809152503321 |
| London, : Imperial College Press, 2011 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Polyklonale Antikörper [[electronic resource] ] : Eine Einführung in die Theorie und Praxis der Antikörperherstellung / / von Elvira Schecklies
| Polyklonale Antikörper [[electronic resource] ] : Eine Einführung in die Theorie und Praxis der Antikörperherstellung / / von Elvira Schecklies |
| Autore | Schecklies Elvira |
| Pubbl/distr/stampa | Weinheim, Germany, : VCH, 1996 |
| Descrizione fisica | 1 online resource (138 p.) |
| Disciplina |
571.967
616.0798 |
| Soggetto topico | Immunoglobulins |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-282-02144-3
9786612021442 3-527-62410-4 3-527-62411-2 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | ger |
| Nota di contenuto |
Polyklonale Antikörper; Inhalt; VORWORT; 1 EINLEITUNG; 2 IMMUNOLOGISCHE GRUNDLAGEN; 2.1 Was ist ein Antikörper?; 2.2 Wie entsteht ein Antikörper?; 3 ZIELSETZUNG; 3.1 Qualität und Quantität; 3.1.1 Antigen; 3.1.2 Antikörper; 3.2 Zeitplanung; 3.2.1 Beginn der Antikörperproduktion; 3.2.2 Dauer der Antikörperproduktion; 3.3 Antikörperanwendung; 3.3.1 Immunoblotting; 3.3.2 Affinitätschromatographie; 3.3.3 Enzymimmunoassays; 4 WAHL DES ANTIKÖRPERS; 4.1 Polyklonale Antikörper; 4.1.1 Vorteile; 4.1.2 Nachteile; 4.2 Monoklonale Antikörper; 4.2.1 Vorteile; 4.2.2 Nachteile; 5 WAHL DES TIERES; 5.1 Ziege
5.1.1 Alter5.1.2 Größe; 5.1.3 Antikörper; 5.1.4 Tierhaltung; 5.2 Huhn; 5.2.1 Alter; 5.2.2 Größe; 5.2.3 Antikörper; 5.2.4 Tierhaltung; 5.3 Kaninchen; 5.3.1 Alter; 5.3.2 Größe; 5.3.3 Antikörper; 5.3.4 Tierhaltung; 6 ANTIGENE; 6.1 Niedermolekulare Haptene; 6.1.1 Wahl der Kopplungsgruppe; 6.1.2 Wahl des Trägermoleküls; 6.2 Peptide; 6.2.1 Molekulargewicht unter 1500; 6.2.2 Molekulargewicht über 1500; 6.3 Proteine; 6.4 Zellen; 6.5 Polysaccharide; 7 IMMUNISIERUNGSVORBEREITUNG; 7.1 Puffer; 7.2 Adjuvanzien; 7.3 Antigenkonzentration; 7.3.1 Hohe Immunogenität des Antigens 7.3.2 Niedrige Immunogenität des Antigens8 APPLIKATION; 8.1 Ziege; 8.1.1 Vorimmunisierung; 8.1.2 Boostinjektionen; 8.2 Huhn; 8.2.1 Vorimmunisierung; 8.2.2 Boostinjektionen; 8.3 Kaninchen; 8.3.1 Vorimmunisierung; 8.3.2 Boostinjektionen; 9 NEBENWIRKUNGEN DER IMMUNISIERUNG; 9.1 Ziege; 9.2 Huhn; 9.3 Kaninchen; 10 BLUTENTNAHME; 10.1 Vene; 10.2 Arterie; 10.2.1 Kaninchen; 10.2.2 Ziege; 10.3 Entbluten; 11 ANTlKÖRPERGEWINNUNG; 11.1 Serumgewinnung; 11.2 Antikörperisolierung; 11.2.1 Serum; 11.2.2 Dotter; LITERATUR; SACHWORTREGISTER |
| Record Nr. | UNINA-9910144394603321 |
Schecklies Elvira
|
||
| Weinheim, Germany, : VCH, 1996 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Polyklonale Antikörper [[electronic resource] ] : Eine Einführung in die Theorie und Praxis der Antikörperherstellung / / von Elvira Schecklies
| Polyklonale Antikörper [[electronic resource] ] : Eine Einführung in die Theorie und Praxis der Antikörperherstellung / / von Elvira Schecklies |
| Autore | Schecklies Elvira |
| Pubbl/distr/stampa | Weinheim, Germany, : VCH, 1996 |
| Descrizione fisica | 1 online resource (138 p.) |
| Disciplina |
571.967
616.0798 |
| Soggetto topico | Immunoglobulins |
| ISBN |
1-282-02144-3
9786612021442 3-527-62410-4 3-527-62411-2 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | ger |
| Nota di contenuto |
Polyklonale Antikörper; Inhalt; VORWORT; 1 EINLEITUNG; 2 IMMUNOLOGISCHE GRUNDLAGEN; 2.1 Was ist ein Antikörper?; 2.2 Wie entsteht ein Antikörper?; 3 ZIELSETZUNG; 3.1 Qualität und Quantität; 3.1.1 Antigen; 3.1.2 Antikörper; 3.2 Zeitplanung; 3.2.1 Beginn der Antikörperproduktion; 3.2.2 Dauer der Antikörperproduktion; 3.3 Antikörperanwendung; 3.3.1 Immunoblotting; 3.3.2 Affinitätschromatographie; 3.3.3 Enzymimmunoassays; 4 WAHL DES ANTIKÖRPERS; 4.1 Polyklonale Antikörper; 4.1.1 Vorteile; 4.1.2 Nachteile; 4.2 Monoklonale Antikörper; 4.2.1 Vorteile; 4.2.2 Nachteile; 5 WAHL DES TIERES; 5.1 Ziege
5.1.1 Alter5.1.2 Größe; 5.1.3 Antikörper; 5.1.4 Tierhaltung; 5.2 Huhn; 5.2.1 Alter; 5.2.2 Größe; 5.2.3 Antikörper; 5.2.4 Tierhaltung; 5.3 Kaninchen; 5.3.1 Alter; 5.3.2 Größe; 5.3.3 Antikörper; 5.3.4 Tierhaltung; 6 ANTIGENE; 6.1 Niedermolekulare Haptene; 6.1.1 Wahl der Kopplungsgruppe; 6.1.2 Wahl des Trägermoleküls; 6.2 Peptide; 6.2.1 Molekulargewicht unter 1500; 6.2.2 Molekulargewicht über 1500; 6.3 Proteine; 6.4 Zellen; 6.5 Polysaccharide; 7 IMMUNISIERUNGSVORBEREITUNG; 7.1 Puffer; 7.2 Adjuvanzien; 7.3 Antigenkonzentration; 7.3.1 Hohe Immunogenität des Antigens 7.3.2 Niedrige Immunogenität des Antigens8 APPLIKATION; 8.1 Ziege; 8.1.1 Vorimmunisierung; 8.1.2 Boostinjektionen; 8.2 Huhn; 8.2.1 Vorimmunisierung; 8.2.2 Boostinjektionen; 8.3 Kaninchen; 8.3.1 Vorimmunisierung; 8.3.2 Boostinjektionen; 9 NEBENWIRKUNGEN DER IMMUNISIERUNG; 9.1 Ziege; 9.2 Huhn; 9.3 Kaninchen; 10 BLUTENTNAHME; 10.1 Vene; 10.2 Arterie; 10.2.1 Kaninchen; 10.2.2 Ziege; 10.3 Entbluten; 11 ANTlKÖRPERGEWINNUNG; 11.1 Serumgewinnung; 11.2 Antikörperisolierung; 11.2.1 Serum; 11.2.2 Dotter; LITERATUR; SACHWORTREGISTER |
| Record Nr. | UNINA-9910829845903321 |
|
Schecklies Elvira
|
||
| Weinheim, Germany, : VCH, 1996 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||