Abstract
Monoclonal antibodies (MAbs) (1), because of their binding specificity and stability both in vivo and in vitro, are extremely useful tools in medicine, biology, and organic chemistry. The combination of hybridoma technology and recombinant DNA techniques have given access, not only to full-size molecules, but also to various recombinant antibody fragments (RAbs) and fusion proteins (2), thus broadening the range of possible applications. Recent improvements in heterologous gene expression systems (3) and the development of phage display technologies (2) have made it possible to design and express RAbs against almost any given antigen, and to fine-tune these molecules with respect to improved performance. Furthermore, incorporation of affinity tags has simplified the purification of heterologously expressed recombinant proteins (4,5).
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© 1998 Humana Press Inc., Totowa, NJ
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Drossard, J., Liao, YC., Fischer, R. (1998). Production of Recombinant Antibodies in Plant Suspension Cultures. In: Cunningham, C., Porter, A.J.R. (eds) Recombinant Proteins from Plants. Methods in Biotechnology, vol 3. Humana Press. https://doi.org/10.1007/978-1-60327-260-5_11
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DOI: https://doi.org/10.1007/978-1-60327-260-5_11
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Print ISBN: 978-0-89603-390-0
Online ISBN: 978-1-60327-260-5
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