Marasa bernard (9 resultados)
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Librería: Ria Christie Collections, Uxbridge, Reino UnidoRia Christie Collections
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EUR 47,85
Envío por EUR 14,01Se envía de Reino Unido a Estados Unidos de AmericaCantidad disponible: Más de 20 disponibles
Condición: New. In.
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Librería: Chiron Media, Wallingford, Reino UnidoChiron Media
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EUR 45,11
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Paperback. Condición: New.
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Librería: Mispah books, Redhill, SURRE, Reino UnidoMispah books
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EUR 125,31
Envío por EUR 29,25Se envía de Reino Unido a Estados Unidos de AmericaCantidad disponible: 1 disponibles
Paperback. Condición: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
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Librería: PBShop.store US, Wood Dale, IL, Estados Unidos de AmericaPBShop.store US
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EUR 51,12
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PAP. Condición: New. New Book. Shipped from UK. THIS BOOK IS PRINTED ON DEMAND. Established seller since 2000.
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Librería: PBShop.store UK, Fairford, GLOS, Reino UnidoPBShop.store UK
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EUR 50,08
Envío por EUR 3,85Se envía de Reino Unido a Estados Unidos de AmericaCantidad disponible: Más de 20 disponibles
PAP. Condición: New. New Book. Delivered from our UK warehouse in 4 to 14 business days. THIS BOOK IS PRINTED ON DEMAND. Established seller since 2000.
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Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, AlemaniaBuchWeltWeit Ludwig Meier e.K.
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EUR 49,00
Envío por EUR 23,00Se envía de Alemania a Estados Unidos de AmericaCantidad disponible: 2 disponibles
Taschenbuch. Condición: 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.
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Librería: moluna, Greven, Alemaniamoluna
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EUR 41,05
Envío por EUR 48,99Se envía de Alemania a Estados Unidos de AmericaCantidad disponible: Más de 20 disponibles
Condición: 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.
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Librería: buchversandmimpf2000, Emtmannsberg, BAYE, Alemaniabuchversandmimpf2000
Contactar con el vendedorVendedor de 5 estrellasCondición: Nuevo
EUR 49,00
Envío por EUR 60,00Se envía de Alemania a Estados Unidos de AmericaCantidad disponible: 1 disponibles
Taschenbuch. Condición: 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.
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Librería: AHA-BUCH GmbH, Einbeck, AlemaniaAHA-BUCH GmbH
Contactar con el vendedorVendedor de 5 estrellasCondición: Nuevo
EUR 49,00
Envío por EUR 60,87Se envía de Alemania a Estados Unidos de AmericaCantidad disponible: 1 disponibles
Taschenbuch. Condición: 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.
