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We constructed three composite parts and all of their function have been validated:<a href="https://2017.igem.org/Team:NTHU_Taiwan/Results">Results</a></td> | We constructed three composite parts and all of their function have been validated:<a href="https://2017.igem.org/Team:NTHU_Taiwan/Results">Results</a></td> |
Revision as of 12:47, 31 October 2017
Composite Parts
We constructed three composite parts and all of their function have been validated:Results
biobrick | type | name | description | designer | length |
K2354010 | composite | monobody-GBP HS | Bind to ER alpha when ER alpha is bind with EDCs and it can bind on the gold surface. | Chan, Wei-Jen | 850 |
K2354011 | composite | INP-ER-alpha HS | Expression of ER-alpha on the membrane of E. coli and ER-alpha can bind to EDCs | Chan, Wei-Jen | 2284 |
K2354012 | composite | HRP-his tag | Degrade Estrogen Disrupt Chemicals | Chan, Wei-Jen | 1325 |
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.
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.
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.