Difference between revisions of "Part:BBa K3934016"
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− | [1] L. Huang, H. Ruan, W. Gu, Z. Xu, P. Cen, and L. Fan, ‘Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli’, Prep. Biochem. Biotechnol., vol. 37, no. 3, pp. 205–217, 2007, doi: 10.1080/10826060701386695. | + | <br>[1] L. Huang, H. Ruan, W. Gu, Z. Xu, P. Cen, and L. Fan, ‘Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli’, Prep. Biochem. Biotechnol., vol. 37, no. 3, pp. 205–217, 2007, doi: 10.1080/10826060701386695. |
Latest revision as of 13:16, 10 October 2021
Enterokinase cleavage site used to cleave off fusion protein
Entereokinase is a protease which cleaves DNA after the specific sequence Asp-Asp-Asp-Asp-Lys [1]. The sequence can be used in protein expression to cleave off tags or fusion proteins after purification.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
[1] L. Huang, H. Ruan, W. Gu, Z. Xu, P. Cen, and L. Fan, ‘Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli’, Prep. Biochem. Biotechnol., vol. 37, no. 3, pp. 205–217, 2007, doi: 10.1080/10826060701386695.