{"product_id":"single-domain-antibodies-methods-and-protocols-paperback","title":"Single Domain Antibodies: Methods and Protocols - Paperback","description":"\u003cp\u003eby \u003cb\u003eDirk Saerens\u003c\/b\u003e (Editor), \u003cb\u003eSerge Muyldermans\u003c\/b\u003e (Editor)\u003c\/p\u003e\u003cp\u003e\u003c\/p\u003e\u003cp\u003ePart I: Overview of Single Domain Antibodies\u003c\/p\u003e\u003cp\u003e1. From Whole Monoclonal Antibodies to Single Domain Antibodies: Think Small\u003c\/p\u003e\u003cp\u003e Jean-Luc Teillaud\u003c\/p\u003e\u003cp\u003e2. Introduction to Heavy Chain Antibodies and Derived Nanobodies\u003c\/p\u003e\u003cp\u003e Cécile Vincke and Serge Muyldermans\u003c\/p\u003e\u003cp\u003e3. Overview and Discovery of IgNARs and Generation of VNARs \u003c\/p\u003e\u003cp\u003e Stewart D. Nuttall\u003c\/p\u003e\u003cp\u003ePart II: Single Domain Antibody Library Construction\u003c\/p\u003e\u003cp\u003e4. Creation of the Large and Highly Functional Synthetic Repertoire of Human VH and Vκ Domain Antibodies \u003c\/p\u003e\u003cp\u003e Olga Ignatovich, Laurent Jespers, Ian M, Tomlinson, and Ruud M.T. de Wildt\u003c\/p\u003e\u003cp\u003e5. Preparation of a Naïve Library of Camelid Single Domain Antibodies \u003c\/p\u003e\u003cp\u003e Aurelien Olichon and Ario de Marco\u003c\/p\u003e\u003cp\u003ePart III: Selection of Single Domain Antibodies\u003c\/p\u003e\u003cp\u003e6. Selection by Phage Display of Single Domain Antibodies Specific to Antigens in Their Native Conformation \u003c\/p\u003e\u003cp\u003e Peter Verheesen and Toon Laeremans\u003c\/p\u003e\u003cp\u003e7. Semi-Automated Panning of Naive \u003ci\u003eCamelidae\u003c\/i\u003e Libraries and Selection of Single-Domain Antibodies Against Peptide Antigens \u003c\/p\u003e\u003cp\u003e Jyothi Kumaran, Roger MacKenzie, and Mehdi Arbabi-Ghahroudi\u003c\/p\u003e\u003cp\u003e8. Pichia Surface Display: A Tool for Screening Single Domain Antibodies \u003c\/p\u003e\u003cp\u003e Kristof De Schutter and Nico Callewaert\u003c\/p\u003e\u003cp\u003e9. Bacterial Two Hybrid: A Versatile One-Step Intracellular Selection Method \u003c\/p\u003e\u003cp\u003e Mireille Pellis, Serge Muyldermans, and Cécile Vincke\u003c\/p\u003e\u003cp\u003e10. Intracellular Antibody Capture (IAC) Methods for Single Domain Antibodies \u003c\/p\u003e\u003cp\u003e Tomoyuki Tanaka and Terence H. Rabbitts\u003c\/p\u003e\u003cp\u003e \u003c\/p\u003e\u003cp\u003e11. Selection of Functional Single Domain Antibody Fragments for Interfering with Protein-Protein Interactions Inside Cells: A \"One Plasmid\" Mammalian Two-Hybrid System \u003c\/p\u003e\u003cp\u003e Tomoyuki Tanaka and Terence H. Rabbitts\u003c\/p\u003e\u003cp\u003e12. Cell-Free Selection of Domain Antibodies by In Vitro Compartmentalization \u003c\/p\u003e\u003cp\u003e Armin Sepp and Andrew Griffiths\u003c\/p\u003e\u003cp\u003e13. Selection of VHHs Under Application Conditions \u003c\/p\u003e\u003cp\u003e Edward Dolk, Theo Verrips, and Hans de Haard\u003c\/p\u003e\u003cp\u003e14. Isolation and Characterization of \u003ci\u003eClostridium difficile\u003c\/i\u003e Toxin-Specific Single-Domain Antibodies \u003c\/p\u003e\u003cp\u003e Greg Hussack, Mehdi Arbabi-Ghahroudi, C. Roger MacKenzie, and Jamshid Tanha\u003c\/p\u003e\u003cp\u003e15. Selection of VHH Antibody Fragments that Recognize Different Aβ Depositions Using Complex Immune Libraries \u003c\/p\u003e\u003cp\u003e Rinse Klooster, Kim S. Rutger, and Sylvère van der Maarel\u003c\/p\u003e\u003cp\u003ePart IV: Expression of Single Domain Antibodies and Derivatives\u003c\/p\u003e\u003cp\u003e16. Expression of Single-Domain Antibodies in Bacterial Systems \u003c\/p\u003e\u003cp\u003e Toya Nath Baral and Mehdi Arbabi-Ghahroudi\u003c\/p\u003e\u003cp\u003e17. Expression of VHHs in \u003ci\u003eS. cerevisiae\u003c\/i\u003e \u003c\/p\u003e\u003cp\u003e Andrea Gorlani, Hans de Haard, \u003csup\u003e \u003c\/sup\u003eand Theo Verrips\u003c\/p\u003e\u003cp\u003e18. Stable Expression of Chimeric Heavy Chain Antibodies in CHO Cells \u003c\/p\u003e\u003cp\u003e Vishal Agrawal, Igor Slivac, Sylvie Perret, Louis Bisson, Gilles St-Laurent, Yanal Murad, Jianbing Zhang, and Yves Durocher\u003c\/p\u003e\u003cp\u003e19. Production of Camel-Like Antibodies in Plants \u003c\/p\u003e\u003cp\u003e Sylvie De Buck, Vikram Virdi, Thomas De Meyer, Kirsten De Wilde, Robin Piron, Jonah Nolf, Els Van Lerberge, Annelies De Paepe, and Ann Depicker\u003c\/p\u003e\u003cp\u003ePart V: Improvement and Applications of Single Domain Antibodies\u003c\/p\u003e\u003cp\u003e20. Selecting and Purifying Autonomous Human Variable Heavy (VH) Domains \u003c\/p\u003e\u003cp\u003e Raffi Tonikian and Sachdev S. Sidhu\u003c\/p\u003e\u003cp\u003e21. Solubility and Stability Engineering of Human VH Domains \u003c\/p\u003e\u003cp\u003e Dae Young Kim, Wen Ding, and Jamshid Tanha\u003c\/p\u003e\u003cp\u003e22. Improvement of Proteolytic Stability through In Silico Engineering \u003c\/p\u003e\u003cp\u003e Lucy Rutten, Hans de Haard, and Theo Verrips\u003c\/p\u003e\u003cp\u003e23. Selection of Human VH Single Domains with Improved Biophysical Properties by Phage Display \u003c\/p\u003e\u003cp\u003e Kip Dudgeon, Romain Rouet, Kristoffer Famm, and Daniel Christ\u003c\/p\u003e\u003ch3\u003eBack Jacket\u003c\/h3\u003e\u003cp\u003eThe development of the hybridoma technology created the possibility to obtain unlimited amounts of monoclonal antibodies (mAb) with high specificity and affinity for any target and to introduce mAbs in a wide range of applications; however, the bulky size of mAbs, costly production, and cumbersome engineering hampered regularly their streamlined development in some applications. In \u003ci\u003eSingle Domain Antibodies: Methods and Protocols\u003c\/i\u003e, expert researchers examine single variable domain antibody fragments, referred to as VH, VL, VHH or VNAR. These fragments are the smallest intact antigen-binding fragments that can be produced recombinantly at low cost. Written in the highly successful \u003ci\u003eMethods in Molecular Biology\u003c\/i\u003e(TM) series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.\u003c\/p\u003e\u003cdiv\u003e\n\u003cstrong\u003eNumber of Pages:\u003c\/strong\u003e 580\u003c\/div\u003e\u003cdiv\u003e\n\u003cstrong\u003eDimensions:\u003c\/strong\u003e 1.21 x 10 x 7 IN\u003c\/div\u003e\u003cdiv\u003e\n\u003cstrong\u003eIllustrated:\u003c\/strong\u003e Yes\u003c\/div\u003e\u003cdiv\u003e\n\u003cstrong\u003ePublication Date:\u003c\/strong\u003e August 23, 2016\u003c\/div\u003e","brand":"Books by splitShops","offers":[{"title":"Default Title","offer_id":42716916285503,"sku":"9781493959150","price":233.26,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0105\/8226\/1823\/files\/93e2b590f4e8b57d09274e60dc896d3f.webp?v=1765076640","url":"https:\/\/dhlswag.com\/products\/single-domain-antibodies-methods-and-protocols-paperback","provider":"BBB","version":"1.0","type":"link"}