The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
An overview of enzymatic reagents for the removal of affinity tags
Open accessAbstract
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.
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The P1′ specificity of tobacco etch virus protease
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Recombinant protein expression in Escherichia coli: advances and challenges
Rosano, G. L., & Ceccarelli, E. A. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00172 · Cited by 2,556
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Research Applications of Proteolytic Enzymes in Molecular Biology
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Davidi, D., Noor, E., Liebermeister, W., Bar-Even, A., Flamholz, A., Tummler, K., Barenholz, U., Goldenfeld, M., Shlomi, T., & Milo, R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514240113 · Cited by 266
Metadata
- Authors
- Waugh, D. S.
- Venue
- Protein Expression and Purification
- Publisher
- Elsevier BV
- Published
- 2011-12
- Volume
- 80
- Issue
- 2
- Pages
- 283-293
- ISSN
- 1046-5928 (ISSN-L)
- OpenAlex
- W2164623788
- Cited by
- 346
- References
- 73
- FWCI
- 5.88
- Type
- journal article
- Language
- en
- Open access
- green
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