Use of in vivo biotinylated GST fusion proteins to select recombinant antibodies

Main Article Content

Cedric Blanc
Madeleine Zufferey
Pierre Cosson

Abstract

 


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.

Article Details

How to Cite
Blanc, C., Zufferey, M. and Cosson, P. (2014) “Use of in vivo biotinylated GST fusion proteins to select recombinant antibodies”, ALTEX - Alternatives to animal experimentation, 31(1), pp. 37-42. doi: 10.14573/altex.1307081.
Section
Articles

Most read articles by the same author(s)