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Updated: Sep 26, 2026
Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
Published on: January 6, 2015
Cloning, expression and two-step purification of recombinant His-tag enhanced green fluorescent protein
W Dieryck1, A M Noubhani, D Coulon
1Ecole Supérieure de Technologie des Biomolécules de Bordeaux (ESTBB), UMR 5544, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Cedex, Bordeaux, France.
Abstract:
In this report, we describe a two-step chromatographic procedure for the purification of His-tag EGFP by immobilized metal affinity expanded bed adsorption (IMAEBA) as the capture step and size exclusion chromatography as the polishing step. The use of proteins including a histidine-tag facilitates their subsequent purification after expression in many microorganisms. This meets the needs of scientific researchers as well as industrialists in purifying recombinant proteins. The procedure described allowed the obtention of 230 mg pure EGFP from 1 l simple batch culture with a recovery of 90%.
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