Unique Antibody Engineering Using Phage Display Technology: Isolation of Camel Phage Displayed Functional Single Domain Antibody Fragments Against Mouse TNF-α and Chicken Lysozyme

 
9783848441167: Unique Antibody Engineering Using Phage Display Technology: Isolation of Camel Phage Displayed Functional Single Domain Antibody Fragments Against Mouse TNF-α and Chicken Lysozyme
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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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About the Author:

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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Book Description Condition: New. Publisher/Verlag: LAP Lambert Academic Publishing | Isolation of Camel Phage Displayed Functional Single Domain Antibody Fragments Against Mouse TNF- and Chicken Lysozyme | 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. | Format: Paperback | Language/Sprache: english | 155 gr | 220x150x5 mm | 104 pp. Seller Inventory # K9783848441167

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Book Description LAP Lambert Academic Publishing Jun 2012, 2012. Taschenbuch. Condition: 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. 104 pp. Englisch. Seller Inventory # 9783848441167

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Book Description LAP Lambert Academic Publishing Jun 2012, 2012. Taschenbuch. Condition: 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. 104 pp. Englisch. Seller Inventory # 9783848441167

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Book Description LAP Lambert Academic Publishing. Paperback. Condition: New. 104 pages. Dimensions: 8.6in. x 5.8in. x 0.3in.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. This item ships from multiple locations. Your book may arrive from Roseburg,OR, La Vergne,TN. Paperback. Seller Inventory # 9783848441167

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Book Description LAP Lambert Academic Publishing, Germany, 2012. Paperback. Condition: New. Aufl.. Language: English. Brand new Book. 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. Seller Inventory # AAV9783848441167

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Book Description LAP Lambert Academic Publishing Jun 2012, 2012. Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand 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. 104 pp. Englisch. Seller Inventory # 9783848441167

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