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References
| Screening antibody-antigen interactions in parallel using Biacore A100 |
| P. Safsten, S. L. Klakamp, A. W. Drake, R. Karlsson and D. G. Myszka |
| Anal Biochem 353: 181-90 (2006) |
| High-quality data with increased throughput on Biacore A100 in the characterization of monoclonal antibodies for therapeutic and diagnostic applications. Antibodies with optimal kinetic profiles were selected from 386 crude hybridoma samples in a 12 h automated run. Selected antibodies were further characterized by higher resolution analysis, and binding interactions were studied under a range of buffer conditions. |
| Link to abstract |
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| Ultra-potent antibodies against respiratory syncytial virus: effects of binding kinetics and binding valence on viral neutralization |
| H. Wu, D. S. Pfarr, Y. Tang, L. L. An, N. K. Patel, J. D. Watkins, W. D. Huse, P. A. Kiener and J. F. Young |
| J Mol Biol 350: 126-44 (2005) |
| Excellent paper on understanding the value of kinetics. Fab phage display was used to discover beneficial mutations of an anti-viral antibody. Mutations that slowed dissociation in selected Fabs failed to improve potencies of full IgG counterparts but when Fab mutants were selected according to association rates, potencies of IgGs increased. The paper highlights the development of a unique ELISA to screen for association rates; however, information from Biacore was essential for characterization and interpretation of the results. |
| Link to abstract |
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| Measurement of antibody-membrane interactions by surface plasmon resonance |
| A. Klimka, M. K. Tur, M. Huhn, U. Bierfreund, E. Terrada, R. Fischer, R. Finnern and S. Barth |
| Int J Mol Med 14: 765-8 (2004) |
This paper demonstrates Biacore’s capabilities to evaluate the binding of antibodies derived from phage display libraries. To overcome the limitations, based on ELISA methods, the authors develop a new method to visualize direct antibody-cell membrane interactions using Biacore.
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| Link to abstract |
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