Difference between revisions of "Template:Team:TU Eindhoven/Future HTML"
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<h1>Future prospects</h1><br /><br /> | <h1>Future prospects</h1><br /><br /> | ||
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If the system is proven to be stable, a TEV-protease can be used to release transcription factors in the presence of specific protein. TEV-proteases cleave a specific amino acid sequence, which we use to connect a transcription factor to a second OmpX . When the transcription factor is cleaved, it can start a signaling cascade. The advantage of TEV-protease is that one has a wide range of uses, since it can activate genes. This adaptability, however, comes at a cost; the process reacts a bit slower than the split luciferase approach. | If the system is proven to be stable, a TEV-protease can be used to release transcription factors in the presence of specific protein. TEV-proteases cleave a specific amino acid sequence, which we use to connect a transcription factor to a second OmpX . When the transcription factor is cleaved, it can start a signaling cascade. The advantage of TEV-protease is that one has a wide range of uses, since it can activate genes. This adaptability, however, comes at a cost; the process reacts a bit slower than the split luciferase approach. | ||
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Latest revision as of 14:04, 22 July 2015
Future prospects
If the system is proven to be stable, a TEV-protease can be used to release transcription factors in the presence of specific protein. TEV-proteases cleave a specific amino acid sequence, which we use to connect a transcription factor to a second OmpX . When the transcription factor is cleaved, it can start a signaling cascade. The advantage of TEV-protease is that one has a wide range of uses, since it can activate genes. This adaptability, however, comes at a cost; the process reacts a bit slower than the split luciferase approach.