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 gold binding protein, and monobody can bind to ER-alpha/EDCs complex.
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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.
 
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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.
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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.
 
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Revision as of 12:51, 31 October 2017

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JUDGING FORM

Composite Parts

We constructed three composite parts and all of their function have been validated:Results

　 　 　 　 　 　 　 　 　 　 　 　 　 　 　
biobricktype name description designer length
K2354010composite 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
K2354011composite 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
K2354012composite HRP-his tag Degrade Estrogen Disrupt Chemicals Chan, Wei-Jen 1325

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 the gold-binding protein, and monobody can bind to ER-alpha/EDCs complex.

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.

K2354012

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.