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.
| Original language | English |
|---|---|
| Pages (from-to) | 276-281 |
| Number of pages | 6 |
| Journal | Nature Biotechnology |
| Volume | 17 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1999 |
Keywords
- Ep-CAM
- Immunotherapy
- Phage display
- Recombinant antibodies
- Single-chain Fv