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Making the most of affinity tags

  1. Author:
    Waugh, D. S.

  2. Author Address

    NCI, Prot Engn Sect, Macromol Crystallog Lab, Canc Res Ctr, Frederick, MD 21701 USA Waugh, DS, NCI, Prot Engn Sect, Macromol Crystallog Lab, Canc Res Ctr, POB B, Frederick, MD 21701 USA
    1. Year: 2005
    2. Date: JUN
  2. Journal: Trends in Biotechnology
    1. 23
    2. 6
    3. Pages: 316-320
  4. Type of Article: Review
  1. Abstract:

    Proteins do not naturally lend themselves to high-throughput 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

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  2. DOI: 10.1016/j.tibtech.2005.03.012
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