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Updated: Jun 28, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
Use of magnetic carboxyl beads to purify a cationic peptide in a batch system
Fabrice Bayard1, Amélie Raveneau, Aurélie Letourneau
1EA 4135, Ecole Supérieure de Technologie des Biomolécules de Bordeaux, Université Victor Segalen Bordeaux2, 146 rue Leo Saignat, 33076 Bordeaux Cedex, France.
Abstract:
Antimicrobial peptides (AMPs) are cationic molecules that are good leads for new antiinfective drugs. To obtain sufficient amounts, recombinant AMPs are generally produced as fusion proteins in Escherichia coli. Fusion partners facilitate purification of recombinant proteins. Fusion proteins are then cleaved by specific proteases, and cationic peptides are purified by size exclusion chromatography or ion exchange chromatography, neither of which is easily applicable to small volumes of diluted peptide samples. We developed a small-scale system that is easily adaptable for high-throughput screening and uses carboxyl magnetic beads to purify a cationic peptide from its fusion partner.
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