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Unique Antibody Engineering Using Phage Display Technology: Isolation of Camel Phage Displayed Functional Single Domain Antibody Fragments Against ... Against Mouse TNF-¿ and Chicken Lysozyme - Softcover
Inhaltsangabe
The absolute target of molecular engineers has been to minimize the size of the antigen binding protein without compromising its functional affinity. Smaller fragments like Fabs, Fvs and single domain antibody fragments (also called dAbs) derived from the conventional bivalent IgG antibodies have been met with limited success due to problems in solubility, low expression yields in bacteria, instability and purification difficulties. The discovery of functional heavy chain antibodies devoid of light chains in camelid sera (Hamers-Casterman et al., 1993) revolutionized development of platforms from which the variable domains (VHHs) regarded as the smallest naturally intact antigen binding domains are derived from with significantly high affinities, comparable to those of Fvs. The camelid derived VHHs have several advantages such as; their small size facilitating their use in tumor imaging and therapy apart from being perfect targeting agents of toxic molecules to specific tissue due to ability to penetrate deep into tissues and bioclearence. This book highlights the methodology for isolation camel phage displayed single domain antibodies against murine TNF-α and chicken lysozyme.
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Reseña del editor
The absolute target of molecular engineers has been to minimize the size of the antigen binding protein without compromising its functional affinity. Smaller fragments like Fabs, Fvs and single domain antibody fragments (also called dAbs) derived from the conventional bivalent IgG antibodies have been met with limited success due to problems in solubility, low expression yields in bacteria, instability and purification difficulties. The discovery of functional heavy chain antibodies devoid of light chains in camelid sera (Hamers-Casterman et al., 1993) revolutionized development of platforms from which the variable domains (VHHs) regarded as the smallest naturally intact antigen binding domains are derived from with significantly high affinities, comparable to those of Fvs. The camelid derived VHHs have several advantages such as; their small size facilitating their use in tumor imaging and therapy apart from being perfect targeting agents of toxic molecules to specific tissue due to ability to penetrate deep into tissues and bioclearence. This book highlights the methodology for isolation camel phage displayed single domain antibodies against murine TNF-α and chicken lysozyme.
Biografía del autor
Dr. Bernard Marasa is currently a Molecular Biologist at Catholic University of America (CUA) in Washington, DC. He is a leading expert in RNA Interference,Antibody engineering, Phage Display and HIV- vaccine Immunogen design. Dr. Marasa has a PhD in Molecular Medicine from University of Maryland, Baltimore and M.Sc from Vrije Universiteit Brussels
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Unique Antibody Engineering Using Phage Display Technology: Isolation of Camel Phage Displayed Functional Single Domain Antibody Fragments Against Mouse TNF-? and Chicken Lysozyme
Verlag:
LAP LAMBERT Academic Publishing, 2012
ISBN 10: 3848441160
ISBN 13: 9783848441167
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Softcover
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Unique Antibody Engineering Using Phage Display Technology
Verlag:
LAP LAMBERT Academic Publishing Apr 2012, 2012
ISBN 10: 3848441160
ISBN 13: 9783848441167
Neu
Taschenbuch
Anbieter: buchversandmimpf2000, Emtmannsberg, BAYE, Deutschland
Verkäuferbewertung 5 von 5 Sternen
Taschenbuch. Zustand: Neu. Neuware -The absolute target of molecular engineers has been to minimize the size of the antigen binding protein without compromising its functional affinity. Smaller fragments like Fabs, Fvs and single domain antibody fragments (also called dAbs) derived from the conventional bivalent IgG antibodies have been met with limited success due to problems in solubility, low expression yields in bacteria, instability and purification difficulties. The discovery of functional heavy chain antibodies devoid of light chains in camelid sera (Hamers-Casterman et al., 1993) revolutionized development of platforms from which the variable domains (VHHs) regarded as the smallest naturally intact antigen binding domains are derived from with significantly high affinities, comparable to those of Fvs. The camelid derived VHHs have several advantages such as; their small size facilitating their use in tumor imaging and therapy apart from being perfect targeting agents of toxic molecules to specific tissue due to ability to penetrate deep into tissues and bioclearence. This book highlights the methodology for isolation camel phage displayed single domain antibodies against murine TNF-¿ and chicken lysozyme.Books on Demand GmbH, Überseering 33, 22297 Hamburg 104 pp. Englisch. Artikel-Nr. 9783848441167
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