Demystified… recombinant antibodies
- 1Division of Cell and Molecular Medicine, Postgraduate Medical Institute, University of Hull, Cottingham Rd, Hull HU6 7RX, UK
- 2Molecular Immunology Research Group, Research Institute in Healthcare Science, School of Applied Sciences, University of Wolverhampton, Wulfruna Street, Wolverhampton WV1 1SB, UK
- 3Department of Pathology, Division of Cancer Studies, The Medical School, University of Birmingham B15 2TT, UK
- Correspondence to: Dr K A Smith Division of Cell and Molecular Medicine, Postgraduate Medical Institute, University of Hull, Cottingham Rd, Hull HU6 7RX, UK; k.a.smithhull.ac.uk
- Accepted 7 January 2004
Abstract
Recombinant antibodies are important tools for biomedical research and are increasingly being used as clinical diagnostic/therapeutic reagents. In this article, a background to humanised antibodies is given, together with details of the generation of antibody fragments—for example, single chain Fv fragments. Phage antibody fragments are fast becoming popular and can be generated by simple established methods of affinity enrichment from libraries derived from immune cells. Phage display methodology can also be used for the affinity enrichment of existing antibody fragments to provide a reagent with a higher affinity. Here, phage antibodies are demystified to provide a greater understanding of the potential of these reagents and to engage clinicians and biomedical scientists alike to think about potential applications in pathology and clinical settings.
- C, constant region
- CDR, complementarity determining region
- CEA, carcinoembryonic
- Fab, fragment antigen binding
- Fc, fragment crystallisable
- H, heavy chain
- HAMA, human anti-murine antibody response
- L, light chain
- MAb, monoclonal antibody
- scFv, single chain heavy and light chain variable regions
- V, variable
- VEGF, vascular endothelial growth factor
