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Removal of Affinity Tags with TEV Protease.

  1. Author:
    Raran-Kurussi, Sreejith
    Cherry, Scott
    Zhang, Di
    Waugh, David

  2. Author Address

    Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, B, Frederick, MD, 21702-1201, USA., Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, B, Frederick, MD, 21702-1201, USA. waughd@mail.nih.gov.,
    1. Year: 2017
  2. Journal: Methods in molecular biology (Clifton, N.J.)
    1. 1586
    2. Pages: 221-230
  4. Type of Article: Article
  1. Abstract:

    Although affinity tags are highly effective tools for the expression and purification of recombinant proteins, they generally need to be removed prior to structural and functional studies. This chapter describes a simple method for overproducing a soluble form of a stable variant of tobacco etch virus (TEV) protease in Escherichia coli and a protocol for purifying it to homogeneity so that it can be used as a reagent for removing affinity tags from recombinant proteins by site-specific endoproteolysis. Further, we cleave a model substrate protein (MBP-NusG) in vitro using the purified TEV protease to illustrate a protease cleavage protocol that can be employed for simple pilot experiments and large-scale protein preparations.

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External Sources

  1. View Full Text
  2. DOI: 10.1007/978-1-4939-6887-9_14
  3. PMID: 28470608
  4. View record in Web of Science®
  5. WOS: 000428324900015

Library Notes

  1. Fiscal Year: FY2016-2017
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