Affinty Tag Essay

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Review TRENDS in Biotechnology Vol.23 No.6 June 2005 Making the most of affinity tags David S. Waugh Protein Engineering Section, Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, MD 21702-1201, USA Proteins do not naturally lend themselves to highthroughput analysis because of their diverse physiochemical properties. Consequently, affinity tags have become indispensable tools for structural and functional proteomics initiatives. Although originally developed to facilitate the detection and purification of recombinant proteins, in recent years it has become clear that affinity tags can have a positive impact on the yield, solubility and even the folding of their fusion partners. However, no single affinity tag is optimal with respect to all of these parameters; each has its strengths and weaknesses. Therefore, combinatorial tagging might be the only way to harness the full potential of affinity tags in a high-throughput setting. Introduction As we enter the post-genomic era, the focus is shifting from high-throughput analysis of genome sequences to functional and structural studies of the proteins they encode. However, proteins are much more chemically and structurally diverse than nucleic acids, making them intrinsically unsuitable for generic methodology. As a result, the use of genetically engineered affinity tags is the only means of achieving high-throughput protein purification. The variable yield and poor solubility of many recombinant proteins are also major impediments to highthroughput production. However, the yield of recombinant proteins can often be improved by the judicious use of affinity tags and some tags can enhance the solubility, and even promote the proper folding, of their fusion partners. No single tag is ideally suited for all of these purposes. Instead,

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