Difference between revisions of "Part:BBa K3739017"
| Line 3: | Line 3: | ||
<partinfo>BBa_K3739017 short</partinfo> | <partinfo>BBa_K3739017 short</partinfo> | ||
| − | LMT is a signal peptide from the lytic murein transglycosylase of ''V.natriegen'' and PPO, a tyrosinase able to oxidize polyphenol, is to weaken the | + | LMT is a signal peptide from the lytic murein transglycosylase of ''V.natriegen'' and PPO, a tyrosinase able to oxidize polyphenol, is to weaken the Mfp glue.his-tag is used to be detected by anti-his antibody and purify the his-linking fusion. |
| Line 9: | Line 9: | ||
LMT is a signal peptide from the lytic murein transglycosylase of ''V.natriegen''. | LMT is a signal peptide from the lytic murein transglycosylase of ''V.natriegen''. | ||
PPO, a tyrosinase able to oxidize polyphenol, is to weaken the mussel foot protein glue. | PPO, a tyrosinase able to oxidize polyphenol, is to weaken the mussel foot protein glue. | ||
| − | his-tag is used to be detected by anti-his antibody and purify the his-linking fusion | + | his-tag is used to be detected by anti-his antibody and purify the his-linking fusion. |
Revision as of 17:22, 20 October 2021
LMT-PPO-his
LMT is a signal peptide from the lytic murein transglycosylase of V.natriegen and PPO, a tyrosinase able to oxidize polyphenol, is to weaken the Mfp glue.his-tag is used to be detected by anti-his antibody and purify the his-linking fusion.
Biology
LMT is a signal peptide from the lytic murein transglycosylase of V.natriegen. PPO, a tyrosinase able to oxidize polyphenol, is to weaken the mussel foot protein glue. his-tag is used to be detected by anti-his antibody and purify the his-linking fusion.
Usage
By codon optimization, the sequence suitable for expression in Vibrio Natriegens was constructed. Adding T7-RBS and terminator,construct new composite part BBa_K3739110.We transformed the constructed plasmid into Vibrio Natriegens to verify its successful heterologous expression.
Reference
1. Holten-Andersen, N.; Waite, J. H., Mussel-designed protective coatings for compliant substrates. J Dent Res 2008, 87 (8), 701-9.
2. Kim, E.; Dai, B.; Qiao, J. B.; Li, W.; Fortner, J. D.; Zhang, F., Microbially Synthesized Repeats of Mussel Foot Protein Display Enhanced Underwater Adhesion. ACS Appl Mater Interfaces 2018, 10 (49), 43003-43012.
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]