Antibody Phage Display

Hust, Michael; Frenzel, André; Tomszak, Florian; Kügler, Jonas; Dübel, Stefan

doi:10.1002/9780470485408.ch8

Cited by 5 publications

References 189 publications

(29 reference statements)

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Antibody Production: Human, Recombinant

Dübel

2010

Encyclopedia of Industrial Biotechnology

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Recombinant antibodies are not only the largest, but also the most rapidly growing group of protein therapeutics. In fact, only the development of an increasing number of recombinant technologies was the trigger for the broad success of monospecific antibodies in the clinics, which started in the last decade. By now, 24 antibodies are approved for clinical use, the vast majority of them having been modified toward a more “human” primary sequence. In addition to various humanization methods for mouse hybridoma‐derived monoclonal antibodies, in particular, novel methods for the generation of fully human antibodies were developed. Most importantly, approaches allowing in vitro selection, that is, the isolation of specific interactions outside of, and independent from a living immune system, gained increasing importance to generate clinically useful human antibodies. The most widely used method here is phage display. This method is based on the selection of antibody genes by their encoded antigen‐binding function in an affinity‐based enrichment step. After getting a recombinant antibody clone, the fusion of other proteins/protein domains lends itself to the development of new characteristics in recombinant antibodies, which nature cannot provide. Furthermore, through the production of recombinant antibodies in different organisms, new possibilities for commercial mass production have arisen.

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