| Autor: |
Huls GA; Department of Immunology, University Hospital Utrecht, The Netherlands., Heijnen IA, Cuomo ME, Koningsberger JC, Wiegman L, Boel E, van der Vuurst de Vries AR, Loyson SA, Helfrich W, van Berge Henegouwen GP, van Meijer M, de Kruif J, Logtenberg T |
| Jazyk: |
angličtina |
| Zdroj: |
Nature biotechnology [Nat Biotechnol] 1999 Mar; Vol. 17 (3), pp. 276-81. |
| DOI: |
10.1038/7023 |
| Abstrakt: |
A single-chain Fv antibody fragment specific for the tumor-associated Ep-CAM molecule was isolated from a semisynthetic phage display library and converted into an intact, fully human IgG1 monoclonal antibody (huMab). The purified huMab had an affinity of 5 nM and effectively mediated tumor cell killing in in vitro and in vivo assays. These experiments show that nonimmunized phage antibody display libraries can be used to obtain high-affinity, functional, and clinically applicable huMabs directed against a tumor-associated antigen. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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