Difference between revisions of "Team:NTHU Formosa/Parts"

 
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     <h2 class="w3-wide">Parts&Component</h2>
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    <br>
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     <p class="w3-justify"><a id="myLink"><u>TEV protease</u></a>
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    <br>
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    <br>
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     <h2 class="w3-wide" style="font-size:60px;font-family:Quicksand;">Parts & Component</h2>
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     <br>
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    <br>
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    <br>
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    <br>
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      <table>
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        <tr>
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          <th><font face="Quicksand">Name</font></th>
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          <th><font face="Quicksand">Type</font></th>
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          <th><font face="Quicksand">Description</font></th>
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        </tr>
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        <tr>
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          <td><a
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href="http://parts.igem.org/Part:BBa_K2635000">
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          <font face="Quicksand">BBa_K2635000</font>
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            </a></td>
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          <td><font face="Quicksand">basic</font></td>
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          <td><font face="Quicksand">pTRE3G-mCherry</font></td>
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        </tr> 
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        <tr>
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          <td><a
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href="http://parts.igem.org/Part:BBa_K2635001">
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          <font face="Quicksand">BBa_K2635001</font>
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            </a></td>
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          <td><font face="Quicksand">composite</font></td>
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          <td><font face="Quicksand">pCAG-GBP</font></td>
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        </tr> 
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        <tr>
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          <td><a  
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href="http://parts.igem.org/Part:BBa_K2635002">
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          <font face="Quicksand">BBa_K2635002</font>
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            </a></td>
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          <td><font face="Quicksand">basic</font></td>
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          <td><font face="Quicksand">GBP N-terminal</font></td>
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        </tr>
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 +
        <tr>
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          <td><a
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href="http://parts.igem.org/Part:BBa_K2635003">
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          <font face="Quicksand">BBa_K2635003</font>
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            </a></td>
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          <td><font face="Quicksand">basic</font></td>
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          <td><font face="Quicksand">GBP C-terminal</font></td>
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        </tr>
  
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</p>
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        <tr>
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<p class="w3-justify">1.What is bioluminescence?
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          <td><a
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Bioluminescence is found in living organism. It’s light produced by chemical reaction in which luciferase catalyzed substrates and result in the emission of light.
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href="http://parts.igem.org/Part:BBa_K2635004">
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</p>
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          <font face="Quicksand">BBa_K2635004</font>
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<p class="w3-justify">2.Bioluminescence vs. Fluorescence
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            </a></td>
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Bioluminescence results from chemical reaction which convert chemical energy to light energy. About 20% of the converted energy is released in the form of heat.
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          <td><font face="Quicksand">basic</font></td>
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Fluorescence is radiation emission, usually visible light. It occurs when the excited orbital electrons fall back to ground state and release the energy as light and heat.
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          <td><font face="Quicksand">TEV N-terminal</font></td>
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</p>
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        </tr>
  
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        <tr>
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          <td><a
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href="http://parts.igem.org/Part:BBa_K2635005">
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          <font face="Quicksand">BBa_K2635005</font>
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            </a></td>
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          <td><font face="Quicksand">basic</font></td>
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          <td><font face="Quicksand">TEV C-terminal</font></td>
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        </tr>
  
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<p class="w3-justify">3.About luciferase:
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Since 1986, the discoveries of bioluminescence, the firefly luciferase, Renilla luciferase and NanoLuc luciferase, are nonstop. The firefly Luciferase has been widely used as sensor target after successfully cloned. Alternate bioluminescent reporter systems like these are the most common bioluminescence assays, which induce bioluminescence by substrates. The bioluminescence we use in our project is the codon-optimized self-directed bacterial luciferase gene cassette (lux). Lux is very unique among the present bioluminescence systems due to its ability to retrieves intercellular components to synthesize all substrates needed for its production of light.
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          <td><a
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href="http://parts.igem.org/Part:BBa_K2635006">
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          <font face="Quicksand">BBa_K2635006</font>
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            </a></td>
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          <td><font face="Quicksand">basic</font></td>
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          <td><font face="Quicksand">tTA</font></td>
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        </tr>
  
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          <td><a
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href="http://parts.igem.org/Part:BBa_K2635007">
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          <font face="Quicksand">BBa_K2635007</font>
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            </a></td>
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          <td><font face="Quicksand">basic</font></td>
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          <td><font face="Quicksand">TEV cleavage site ENLYFQL</font></td>
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        </tr>
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 +
        <tr>
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          <td><a
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href="http://parts.igem.org/Part:BBa_K2635008">
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          <font face="Quicksand">BBa_K2635008</font>
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            </a></td>
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          <td><font face="Quicksand">basic</font></td>
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          <td><font face="Quicksand">TEV cleavage site ENLYFQG</font></td>
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        </tr>       
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      </table>
  
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    <img class="w3-round-large" src="https://static.igem.org/mediawiki/2018/9/94/T--NTHU_Formosa--GBPpart.png" style="margin-left:auto;margin-right:auto;width:60%;" ;>
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    <br>
  
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    <img class="w3-round-large" src="https://static.igem.org/mediawiki/2018/a/a1/T--NTHU_Formosa--10107b.png" style="margin-left:auto;margin-right:auto;width:30%;" ;>
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    <img class="w3-round-large" src="https://static.igem.org/mediawiki/2018/thumb/e/ed/T--NTHU_Formosa--10107c.png/798px-T--NTHU_Formosa--10107c.png" style="margin-left:auto;margin-right:auto;width:60%;" ;>
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    <img class="w3-round-large" src="https://static.igem.org/mediawiki/2018/2/2c/T--NTHU_Formosa--BIOBRICK_03_03.png" style="margin-left:auto;margin-right:auto;width:13%;" ;>
  
 
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     <span class="close">&times;</span>
 
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     <p>TEV proteases are the 27kDa catalytic domains of the NIa (Nuclear Inclusion a) protein encoded by Tobacco Etch Virus (TEV), where TEV proteases cut polyproteins into single proteins during biogenesis. TEV proteases recognize a linear epitope of the general form E-Xaa-Xaa-Y-Xaa-Q-(G/S) and cut the linkage between Q and G/S (Xaa can be freely substituted because variability in these positions was found in the natural cleavage sites of TEV’s polyprotein). Comparison of cleavage efficiency of different substract sequences demonstrated that “ENLYFQS” is the most efficient substrate sequence. The high-specificity of TEV’s cleavage makes it a popular tool for direct expression in living cells and protein purification.</p>
+
     <p>TEV proteases are the 27kDa catalytic domains of the NIa (Nuclear Inclusion a) protein encoded by Tobacco Etch Virus (TEV), where TEV proteases cut polyproteins into single proteins during biogenesis. TEV proteases recognize a linear epitope of the
 +
      general form E-Xaa-Xaa-Y-Xaa-Q-(G/S) and cut the linkage between Q and G/S (Xaa can be freely substituted because variability in these positions was found in the natural cleavage sites of TEV’s polyprotein). Comparison of cleavage efficiency of
 +
      different substract sequences demonstrated that “ENLYFQS” is the most efficient substrate sequence. The high-specificity of TEV’s cleavage makes it a popular tool for direct expression in living cells and protein purification.</p>
 
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Latest revision as of 00:55, 18 October 2018




Parts & Component





Name Type Description
BBa_K2635000 basic pTRE3G-mCherry
BBa_K2635001 composite pCAG-GBP
BBa_K2635002 basic GBP N-terminal
BBa_K2635003 basic GBP C-terminal
BBa_K2635004 basic TEV N-terminal
BBa_K2635005 basic TEV C-terminal
BBa_K2635006 basic tTA
BBa_K2635007 basic TEV cleavage site ENLYFQL
BBa_K2635008 basic TEV cleavage site ENLYFQG