An Overview of Enzymatic Reagents for the Removal of Affinity Tags
By D. Waugh. 2011
340 citations recorded by the source corpus.
Although they are often exploited to facilitate the expression and purification of recombinant proteins, every affinity tag, whether large or small, has the potential to interfere with the structure and function of its fusion partner. For this reason, reliable methods for removing affinity tags are needed. Only enzymes have the requisite specificity to be generally useful reagents for this purpose. In this review, the advantages and disadvantages of some commonly used endo- and exoproteases are discussed in light of the latest information.
Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging
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Citations in the corpus
- Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial libraries (2013, background): “Additionally, proteases find numerous applications as reagents in biotechnology, ranging from analytical to preparative biochemistry (6, 10, 11).”
- Recombinant protein expression in Escherichia coli: advances and challenges (2014, background): “Choosing among the different proteases is based on specificity, cost, number of amino acids left in the protein after cleavage and ease of removal after digestion (Waugh, 2011).”