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Use of in vivo biotinylated GST fusion proteins to select recombinant antibodies
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Cedric Blanc, Madeleine Zufferey, and Pierre Cosson
Department of Cell Physiology and Metabolism, Centre Médical Universitaire, University of Geneva, Geneva, Switzerland
Over the last 20 years, continuous advances in the field of molecular biology have led to the development of new strategies to discover and produce monoclonal antibodies, notably by phage display. Here we describe a simple procedure for antibody selection that considerably reduces the undesired selection of non-specific antibodies based on the use of biotinylated GST proteins fused to a target antigenic sequence. This procedure was tested on a collection of 7 different targets and resulted in the selection of a high percentage (71%) of antibodies specific for each target. This simple and effective in vitro procedure has great potential to replace animal immunization for the development of specific antibodies.
Keywords: antibody, phage display, glutathione S-transferase (GST), biotinylation
ALTEX 31(1), 37–42