{"product_id":"single-domain-antibodies-dirk-saerens-9781493959150","title":"Single Domain Antibodies: Methods and Protocols","description":"\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 C馗ile 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 Na?e 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 C馗ile 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 Sylv鑽e 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\u003cbr\u003e\u003cbr\u003e\u003cb\u003eAuthor:\u003c\/b\u003e Dirk Saerens\u003cbr\u003e\u003cb\u003eISBN-10:\u003c\/b\u003e 1493959158\u003cbr\u003e\u003cb\u003eISBN-13:\u003c\/b\u003e 9781493959150\u003cbr\u003e\u003cb\u003ePublisher:\u003c\/b\u003e Humana\u003cbr\u003e\u003cb\u003eLanguage:\u003c\/b\u003e English\u003cbr\u003e\u003cb\u003ePublished:\u003c\/b\u003e 08\/23\/2016\u003cbr\u003e\u003cb\u003ePages:\u003c\/b\u003e 580\u003cbr\u003e\u003cb\u003eFormat:\u003c\/b\u003e Paperback\u003cbr\u003e\u003cb\u003eWeight:\u003c\/b\u003e 2.25lbs\u003cbr\u003e\u003cb\u003eSize:\u003c\/b\u003e 10.00h x 7.00w x 1.21d","brand":"Dirk Saerens","offers":[{"title":"Paperback","offer_id":44064768622847,"sku":"9781493959150","price":119.99,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0662\/2982\/9887\/files\/img_b8aa7720-abad-482d-a0f3-c6d90949577a.jpg?v=1685397451","url":"https:\/\/www.whiterainbookhouse.com\/products\/single-domain-antibodies-dirk-saerens-9781493959150","provider":"WR Book House","version":"1.0","type":"link"}