Line 3: | Line 3: | ||
<p> | <p> | ||
− | We constructed three composite parts and all of their function have been validated: | + | We constructed three composite parts and all of their function have been validated: |
+ | <ul> | ||
+ | <li><a href="https://2016.igem.org/Team:INSA-Lyon/Integrated_Practices">2016 INSA Lyon</a></li> | ||
+ | <li><a href="https://2016.igem.org/Team:UofC_Calgary/Integrated_Practices">2016 UofC Calgary</a></li> | ||
+ | <li><a href="https://2015.igem.org/Team:Bielefeld-CeBiTec/Practices">2015 Bielefeld</a></li> | ||
+ | <li><a href="https://2015.igem.org/Team:Edinburgh/Practices">2015 Edinburgh</a></li> | ||
+ | </ul> | ||
</P> | </P> | ||
Revision as of 19:37, 28 October 2017
NTHU_Taiwan
We constructed three composite parts and all of their function have been validated:
BBa_K2354010
Monobody was fused with gold binding protein and linked with 6×his tag. This fused protein can bind to the gold surface by the function of gold binding protein, and monobody can bind to ER-alpha/EDCs complex.
BBa_K2354011
ER-alpha was fused with ice nucleating protein. This fused protein can be anchored on the membrane of E.coli via the function of ice nucleating protein and ER-alpha can bind to EDCs for detection.
BBa_K2354012
Horseradish peroxidase is one kind of peroxidase which has heme as cofactor, and it can degrade EDCs to the less toxic compounds. Moreover, we linked fused protein with 6×his tag for purification.