| Literature DB >> 10096296 |
G A Huls1, I A Heijnen, M E Cuomo, J C Koningsberger, L Wiegman, E Boel, A R van der Vuurst de Vries, S A Loyson, W Helfrich, G P van Berge Henegouwen, M van Meijer, J de Kruif, T Logtenberg.
Abstract
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.Entities:
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Year: 1999 PMID： 10096296 DOI： 10.1038/7023
Source DB: PubMed Journal: Nat Biotechnol ISSN： 1087-0156 Impact factor: 54.908