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. 2009 May;65(1):108-13.
doi: 10.1016/j.pep.2008.11.008. Epub 2008 Dec 3.

Universal and Rapid Method for Purification of GFP-like Proteins by the Ethanol Extraction

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Universal and Rapid Method for Purification of GFP-like Proteins by the Ethanol Extraction

Olga N Samarkina et al. Protein Expr Purif. .

Abstract

GFP-like fluorescent proteins (FPs) are crucial in biological and biomedical studies. The majority of FP purification techniques either include multiple time-consuming chromatography steps with a low yield of the desired product or require prior protein modification (addition of special tags). In the present work, we propose an alternative ethanol extraction-based technique previously used for GFP purification and then modified for diverse FPs originated from different sources. The following recombinant FPs were expressed using Escherichia coli M15 (pREP4) strain as a host transformed with pQE30 plasmid bearing one of the target FP genes: TagCFP, TagGFP, TagYFP, TagRFP, TurboGFP, TurboRFP, Dendra2, TurboFP602 and KillerRed. Despite their diversity, all tested recombinant FPs were successfully purified and yielded a highly homogeneous product. The method is easily scalable for purification of any amount of protein and requires no expensive reagents and equipment.

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