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| Progress in the Application of Affinity Tags for the Expression and Purification of Recombinant Proteins |
| CHEN Ai-chun1, PENG Wei1, WANG Sheng-peng1,2 |
1. School of Biology and Chemical Engineering, Jiangsu University of Science and Technology, Zhenjiang 212018, China;
2. Key Laboratory of Silkworm and Mulberry Genetic Improvement, Ministry of Agriculture, Sericultural Research Institute, Chinese Academy of Agricultural Sciences, Zhenjiang 212018, China |
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Abstract Affinity-tag fusion technology provides a simple and convenient tool for the purification of arbitrary recombinant proteins through genetic engineering, which is obviously characterized with high binding specificity, mild elution conditions employed, high generality and hundred- or even thousand-fold purification. The affinity tags widely used for the expression and purification of recombinant proteins is discussed, together with several novel purification tags in recent years. The positive effects of affinity tags on the fusion proteins are presented, which can increase the yield, enhance the solubility and promote the folding of recombinant proteins. An overview of the tag design that combines different affinity tags is introduced, which His6-MBP combinatorial tag has advantages of the two integral parts and tandem affinity purification can purify protein complexes under physiological conditions. Finally, future outlook is also discussed briefly, and purification tag systems that are characterized with more superior performance and more notable purification efficiency are still needed to be developed.
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Received: 09 July 2012
Published: 25 December 2012
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