Efficient one-step direct labelling of recombinant antibodies with technetium-99m
- 1 November 1995
- journal article
- research article
- Published by Springer Nature in European Journal of Nuclear Medicine and Molecular Imaging
- Vol. 22 (11) , 1326-1329
- https://doi.org/10.1007/bf00801622
Abstract
High-affinity bacterially expressed antibody fragments can nowadays be cloned from established hybridomas or, more conveniently, isolated directly from antibody libraries displayed on filamentous phage. Such antibodies can be tagged with C-terminal peptide tags containing one cysteine residue, which represents a convenient functionalisation site for a number of applications, including technetium-99m labelling. Here we describe a simple one-step method for99m-Tc labelling of cysteine-tagged recombinant antibodies with more than 50% radionuclide incorporation. The labelled antibodies displayed full retention of immuoreactivity and good stability.Keywords
This publication has 12 references indexed in Scilit:
- Engineering recombinant antibodies for immunotherapyCell Biochemistry and Biophysics, 1995
- A single chain Fv derived from a filamentous phage library has distinct tumour targeting advantages over one derived from a hybridomaInternational Journal of Cancer, 1995
- High-affinity Antigen Binding by Chelating Recombinant Antibodies (CRAbs)Journal of Molecular Biology, 1995
- IMPROVED TUMOR TARGETING WITH CHEMICALLY CROSS-LINKED RECOMBINANT ANTIBODY FRAGMENTS1994
- In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity.Proceedings of the National Academy of Sciences, 1994
- Making Antibodies by Phage Display TechnologyAnnual Review of Immunology, 1994
- Microautoradiographic analysis of the normal organ distribution of radioiodinated single-chain Fv and other immunoglobulin forms.1993
- By–Passing Immunization: Building High Affinity Human Antibodies by Chain ShufflingNature Biotechnology, 1992
- Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chainsNucleic Acids Research, 1991