Bernard Marasa (10 results)
- Softcover
Seller: Ria Christie Collections, Uxbridge, United KingdomRia Christie Collections
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Language: English
Published by LAP LAMBERT Academic Publishing 2012-06-16, 2012
- Softcover
Seller: Chiron Media, Wallingford, United KingdomChiron Media
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More images- Softcover
Seller: preigu, Osnabrück, Germanypreigu
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Taschenbuch. Condition: Neu. Unique Antibody Engineering Using Phage Display Technology | Isolation of Camel Phage Displayed Functional Single Domain Antibody Fragments Against Mouse TNF-¿ and Chicken Lysozyme | Bernard S. Marasa | Taschenbuch | 104 S. | Englisch | 2012 | LAP LAMBERT Academic Publishing | EAN 9783848441167 | Ver…antwortliche Person für die EU: OmniScriptum GmbH & Co. KG, Bahnhofstr. 28, 66111 Saarbrücken, info[at]akademikerverlag[dot]de | Anbieter: preigu.
- Softcover
Seller: Mispah books, Redhill, SURRE, United KingdomMispah books
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- Softcover
- Print on Demand
Seller: PBShop.store US, Wood Dale, IL, U.S.A.PBShop.store US
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PAP. Condition: New. New Book. Shipped from UK. THIS BOOK IS PRINTED ON DEMAND. Established seller since 2000.
- Softcover
- Print on Demand
Seller: PBShop.store UK, Fairford, GLOS, United KingdomPBShop.store UK
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PAP. Condition: New. New Book. Delivered from our UK warehouse in 4 to 14 business days. THIS BOOK IS PRINTED ON DEMAND. Established seller since 2000.
Language: English
Published by LAP LAMBERT Academic Publishing Apr 2012, 2012
- Softcover
- Print on Demand
Seller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermanyBuchWeltWeit Ludwig Meier e.K.
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Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - 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.
- Softcover
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Seller: moluna, Greven, Germanymoluna
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Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Marasa Bernard S.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 D…isplay and HIV- vaccine Immunog.
Language: English
Published by LAP LAMBERT Academic Publishing Apr 2012, 2012
- Softcover
- Print on Demand
Seller: buchversandmimpf2000, Emtmannsberg, BAYE, Germanybuchversandmimpf2000
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Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. 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 dAb…s) 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.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 104 pp. Englisch.
- Softcover
- Print on Demand
Seller: AHA-BUCH GmbH, Einbeck, GermanyAHA-BUCH GmbH
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Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - 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.
