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<li> | <li> | ||
<a href="http://parts.igem.org/Part:BBa_K1613005">BBa_K1613005</a><span>J23119+B0030+CYP1A2+B0015</span> | <a href="http://parts.igem.org/Part:BBa_K1613005">BBa_K1613005</a><span>J23119+B0030+CYP1A2+B0015</span> | ||
| − | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/ | + | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/3/37/HSNU-TAIPEI-BBa_K1613003%2B05.jpg" width="40%"></div> |
| − | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613005</strong></p> | + | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613003+BBa_K1613005</strong></p> |
</li> | </li> | ||
<li><a href="http://parts.igem.org/Part:BBa_K1613006">BBa_K1613006</a><span>J23119+B0032+CYP1A2+B0015</span></li> | <li><a href="http://parts.igem.org/Part:BBa_K1613006">BBa_K1613006</a><span>J23119+B0032+CYP1A2+B0015</span></li> | ||
| Line 129: | Line 129: | ||
<h3 class="article-title">Benzo[a]pyrene</h3> | <h3 class="article-title">Benzo[a]pyrene</h3> | ||
<ul class="article-ul"> | <ul class="article-ul"> | ||
| − | <li><a href="http://parts.igem.org/Part:BBa_K1613012">BBa_K1613012</a><span>J23113+B0034+K1092104+B0034+K1092000+B0015</span></li> | + | <li><a href="http://parts.igem.org/Part:BBa_K1613012">BBa_K1613012</a><span>J23113+B0034+K1092104+B0034+K1092000+B0015</span> |
| + | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/e/e6/HSNU-TAIPEI-BBa_K1613012.png" width="40%"></div> | ||
| + | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613012</strong></p> | ||
| + | </li> | ||
<li> | <li> | ||
<a href="http://parts.igem.org/Part:BBa_K1613013">BBa_K1613013</a><span>J23113+B0034+E1010+B0015</span> | <a href="http://parts.igem.org/Part:BBa_K1613013">BBa_K1613013</a><span>J23113+B0034+E1010+B0015</span> | ||
| − | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/ | + | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/f/f3/HSNU-TAIPEI-BBa_K1613013.jpg" width="40%"></div> |
| − | <p class="article-p"><strong>▲gel electrophoresis | + | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613013</strong></p> |
</li> | </li> | ||
<li><a href="http://parts.igem.org/Part:BBa_K1613020">BBa_K1613020</a><span>QsrR Binding Site</span><span><mark>(<a href="https://2015.igem.org/Team:HSNU-TAIPEI/Basic_Part" style="color:#000000">Basic Part</a>)</mark></span></li> | <li><a href="http://parts.igem.org/Part:BBa_K1613020">BBa_K1613020</a><span>QsrR Binding Site</span><span><mark>(<a href="https://2015.igem.org/Team:HSNU-TAIPEI/Basic_Part" style="color:#000000">Basic Part</a>)</mark></span></li> | ||
| Line 152: | Line 155: | ||
<li> | <li> | ||
<a href="http://parts.igem.org/Part:BBa_K1613023">BBa_K1613023</a><span>B0015+I721001</span> | <a href="http://parts.igem.org/Part:BBa_K1613023">BBa_K1613023</a><span>B0015+I721001</span> | ||
| − | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/ | + | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/8/86/HSNU-TAIPEI-BBa_K1613023.png" width="40%"></div> |
| − | + | ||
<p class="article-p"><strong>▲gel electrophoresis BBa_K1613023</strong></p> | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613023</strong></p> | ||
</li> | </li> | ||
<li> | <li> | ||
<a href="http://parts.igem.org/Part:BBa_K1613024">BBa_K1613024</a><span>B0032+I721002</span> | <a href="http://parts.igem.org/Part:BBa_K1613024">BBa_K1613024</a><span>B0032+I721002</span> | ||
| − | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/ | + | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/c/c9/HSNU-TAIPEI-BBa_K1613024.jpg" width="40%"></div> |
<p class="article-p"><strong>▲gel electrophoresis BBa_K1613024</strong></p> | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613024</strong></p> | ||
</li> | </li> | ||
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<h4 class="article-h4"> ✔ QsrR Binding Site inhibits the transcription and translation of Red Fluorescent Protein.</h4> | <h4 class="article-h4"> ✔ QsrR Binding Site inhibits the transcription and translation of Red Fluorescent Protein.</h4> | ||
<p class="article-p">There is a QsrR Binding Site between promoter and RBS. Which can combine with Quinone-sensing and response Repressor(QsrR). And inhibit the transcription. While QsrR combines with BaP-1,6-Quinone, the QsrR will be activated and depart the Binding Site. That makes the transcription of downstream.</p> | <p class="article-p">There is a QsrR Binding Site between promoter and RBS. Which can combine with Quinone-sensing and response Repressor(QsrR). And inhibit the transcription. While QsrR combines with BaP-1,6-Quinone, the QsrR will be activated and depart the Binding Site. That makes the transcription of downstream.</p> | ||
| − | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/ | + | <div class="dut"><img src="https://static.igem.org/mediawiki/2015/e/e6/HSNU-TAIPEI-BBa_K1613012.png" width="40%"></div> |
| − | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613012 | + | <p class="article-p"><strong>▲gel electrophoresis BBa_K1613012</strong></p> |
</ul> | </ul> | ||
</article> | </article> | ||
▲gel electrophoresis BBa_K1613003+BBa_K1613005
▲gel electrophoresis BBa_K1613012
▲gel electrophoresis BBa_K1613013
▲gel electrophoresis BBa_K1613023
▲gel electrophoresis BBa_K1613024
cyp1a2 can oxidize the substances that it can metabolism. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP1A2 is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include aflatoxin B1, and acetaminophen.
cyp1a2 can oxidize the substances that it can metabolism. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP1A2 is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include aflatoxin B1, and acetaminophen.
There is a QsrR Binding Site between promoter and RBS. Which can combine with Quinone-sensing and response Repressor(QsrR). And inhibit the transcription. While QsrR combines with BaP-1,6-Quinone, the QsrR will be activated and depart the Binding Site. That makes the transcription of downstream.
▲gel electrophoresis BBa_K1613012
This part is designed to proceed cadmium detection in e.coli.Zintp K896008 is a promoter which is designed by NYMU in 2013.It is a part highly specific to the cadmium.The promoter can trigger the RFP. We combine these part to detect cadmium.
This part is desinged to proceed lead detection in e.coli. When lead ions (Pb2+) enter the e.coli, they will combine with the protein PbrR and then form a dimer. The lead promoter can be controlled by the dimer to further trigger the RFP. The idea of this design came from Brown 2007 igem team, also working on lead detection. We combined I721001 and I721002 from their teams with a constitutive promoter J23102 and RFP to make them function.
This is a device to detect copper. We use the CopA Promoter to detect (Promoter from BBa_K1555000) because it’s more specific and sensitive than MarO, CueO. We linked it with RBS, RFP, and Terminator.
MerB can turn Methyl mercury into Hg2+.MerR can combine with Hg2+ and change the structure of DNA. And DNA can be trancripted easier. PmerT is controlled by MerR. PmerT cannot be transcripted because MerR changes the shape of PmerT. In short, the whole reaction will continue if MerR combines with Hg2+.
PmerT is controlled by MerR. PmerT cannot be transcripted because MerR changes the shape of PmerT. In short, the whole reaction will continue if MerR combines with Hg2+.