Difference between revisions of "Part:BBa K3815015"
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− | + | This is an engineered derivative of wildtype ssrA tag from Escherichia coli, acquired by mutagenizing the WT tag with mixed primers. Compared to the WT, three C-terminal amino acids LAA are replaced to LGA. To quantify its efficiency of protein degradation, ... of E.coli overnight culture bearing a plasmid expressing GFP-ssrA tag fusion protein was measured by Qubit, and then compared to the WT and other mutants. | |
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Revision as of 14:07, 20 October 2021
AANDENYALGA. mutant SsrA degradation tag
This is an engineered derivative of wildtype ssrA tag from Escherichia coli, acquired by mutagenizing the WT tag with mixed primers. Compared to the WT, three C-terminal amino acids LAA are replaced to LGA. To quantify its efficiency of protein degradation, ... of E.coli overnight culture bearing a plasmid expressing GFP-ssrA tag fusion protein was measured by Qubit, and then compared to the WT and other mutants.
Usage and Biology
This is an engineered derivative of wildtype ssrA tag from Escherichia coli, acquired by mutagenizing the WT tag with mixed primers. Compared to the WT, three C-terminal amino acids LAA are replaced to LGA. To quantify its efficiency of protein degradation, ... of E.coli overnight culture bearing a plasmid expressing GFP-ssrA tag fusion protein was measured by Qubit, and then compared to the WT and other mutants.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Result
Improvement from existing parts
This is a part improved from BBa_K1051206. In this part, three C-terminal amino acids LAA were replaced with LGA, resulting in a reduced protein degradation efficiency.