Difference between revisions of "Part:BBa K3712022"
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<center><img src="https://2021.igem.org/wiki/images/5/5f/T--HUST2-China--SDS-PAGE_of_Wild-type_TLR2-27ELP%2C_Optimized_TLR2-27_ELP_expression_results.png" style="width:646px;height:544px"></center> | <center><img src="https://2021.igem.org/wiki/images/5/5f/T--HUST2-China--SDS-PAGE_of_Wild-type_TLR2-27ELP%2C_Optimized_TLR2-27_ELP_expression_results.png" style="width:646px;height:544px"></center> | ||
| − | <p><b>Figure 1.</b>SDS-PAGE of Wild-type TLR2-27ELP, Optimized TLR2-27 ELP expression results. Near the 25kDa marker, the binds of Wild-type TLR2- | + | <p><b>Figure 1.</b>SDS-PAGE of Wild-type TLR2-27ELP, Optimized TLR2-27 ELP expression results. Near the 25kDa marker, the binds of Wild-type TLR2-27 ELP and Optimized TLR2-27 ELP after induction are darker than the expression system without induction.</p> |
<h1>Future direction</h1> | <h1>Future direction</h1> | ||
Latest revision as of 19:52, 21 October 2021
Wild-type TLR2 antagonist-27 ELP
USAGE AND BIOLOGY
We connected the TLR2 antagonist to 27ELP in order to verify the ability of the TLR2 antagonist to bind to acylated lipoproteins and the heat-responsive aggregation effect of ELP after TLR2 and ELP were connected.
RESULTS
Figure 1.SDS-PAGE of Wild-type TLR2-27ELP, Optimized TLR2-27 ELP expression results. Near the 25kDa marker, the binds of Wild-type TLR2-27 ELP and Optimized TLR2-27 ELP after induction are darker than the expression system without induction.
Future direction
Unfortunately, due to time issues, we have no way to complete the purification of TLR2 antagonist. In the future, we will try different linkers to connect Wild-type/Optimized TLR2 antagonist and 27 ELP.
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]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 178