Difference between revisions of "Team:NTHU Taiwan/Composite Part"
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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 the gold-binding protein, and monobody can bind to ER-alpha/EDCs complex. | 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 the gold-binding protein, and monobody can bind to ER-alpha/EDCs complex. | ||
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ER-alpha was fused with ice nucleating protein. This fused protein can be anchored on the membrane of <I>E. coli</I> via the function of ice nucleating protein and ER-alpha can bind to EDCs for detection. | ER-alpha was fused with ice nucleating protein. This fused protein can be anchored on the membrane of <I>E. coli</I> via the function of ice nucleating protein and ER-alpha can bind to EDCs for detection. | ||
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Revision as of 13:45, 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 the 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 a kind of peroxidase which uses heme as it's cofactor, and it can degrade EDCs to less toxic compounds. Moreover, we linked fused protein with 6×his tag for purification.
