Abstract
Phage display involves expression of a large library of diverse molecules as fusion proteins on the surface of filamentous bacteriophage. In this form, they may be subjected to biological or molecular selection to isolate molecules with the desired binding properties (1) (see review in ref. 2). Initially, the system was used for mapping antibody epitopes by expression of large libraries (107–108) of random peptides (3–5). However, the approach has proved readily applicable to many types of molecular interaction, including the production or manipulation of antibodies (6–10), enzymes, and their substrates (11–13), general protein-protein interactions (14–15) and DNA binding proteins (16–17).
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© 1998 Humana Press Inc., Totowa, NJ
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Hexham, J.M. (1998). Production of Human Fab Antibody Fragments from Phage Display Libraries. In: Pound, J.D. (eds) Immunochemical Protocols. Methods in Molecular Biology™, vol 80. Humana Press. https://doi.org/10.1007/978-1-59259-257-9_46
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DOI: https://doi.org/10.1007/978-1-59259-257-9_46
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