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

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Published in ALTEX. 2014, vol. 31, no. 1, p. 37-42
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 reduces considerably 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 a strong potential to replace animal immunization for the development of specific antibodies.
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PMID: 24100547
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Article (Published version) (636 Kb) - document accessible for UNIGE members only Limited access to UNIGE
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Research group Phagocytose (140)
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BLANC, Cédric, ZUFFEREY, Madeleine, COSSON, Pierre. Use of in vivo biotinylated GST fusion proteins to select recombinant antibodies. In: ALTEX, 2014, vol. 31, n° 1, p. 37-42. https://archive-ouverte.unige.ch/unige:39509

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Deposited on : 2014-08-19

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