Difference between revisions of "Team:HUST-China/Part Collection"

 
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   <h3 style="color:black" align="center"><b>Best Part Collection:
 
   <h3 style="color:black" align="center"><b>Best Part Collection:
 
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         <p>This year we had 26 parts documented and already sent them to the registry of Standard Biological Parts. Particularly,we did well in the standardization of E.coli 50S ribosomal protein (Si-tag) with the different combination of its domains:1,2,3,1+2,1+3,2+3,1+2+3,1L3. </p>
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<p>The protein has been found from several bacterial strains and proved to have a silica-binding property. To make it a more thouroghly functional part,we added a signal peptide LIP2 prepro and cell wall protein of Yarrowia.Lipolytica YLcwp3 respectively at the N end and C end of the Si-tags. </p>
+
<p>This year, we submitted 26 new parts in total, including basic parts and composite parts. All the parts we used in our Euk.cement project were completely submitted and shipped. Particularly, we did well in the standardization of E.coli 50S ribosomal protein (Si-tag) with the different combination of domains: 1, 2, 3, 1+2,1+3,2+3,1+2+3,1L3.   </p>
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<p>The surface display strategy expressed in eukaryotic cells can immobilize the silica affinitive protein on the surface of the cell wall. We achived a considerable characterazation results with fluorescence immunoassay to test the surface display system and glass binding test to verify the proteins’s affinity to silica solid. The former one showed that we succeeded in displaying the silica-tag onto cell surface and the latter proved  each protein domain had different binding ability. So we can choose different combinations of Si-tag domains to satisfy different requirement of binding intensity thus making a more flexible application.
+
<p>We added a signal peptide and cell wall protein respectively at N-erminal and C-terminal of the Si-tags which can immobilize the working protein onto cell wall to promote the protein’s function. </p>
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</p>
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<p>The results of immunofluorescence assay showed that we succeeded in displaying the silica-tag onto the cell surface. Silica surface binding test shows each protein domain had different binding ability, so that we can choose different combinations of Si-tag domains to satisfy different requirement of binding intensity in further real utilization. </p>
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<p>Here is the collection list (click Part Number to see more details)
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<table border="part collection">
 
<table border="part collection">
 
             <tr>
 
             <tr>
 
<th>Part Number</th>
 
<th>Part Number</th>
 
<th>Description</th>
 
<th>Description</th>
−
<th>Abbreviation</th>
+
<th>Nick Name</th>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592007">BBa_K1592007</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592007">BBa_K1592007</a></td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-60) + YLcwp3 Fusion</td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-60) + YLcwp3 Fusion</td>
−
<td>Si-tag1-his</td>
+
<td>Si-tag1</td>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592008">BBa_K1592008</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592008">BBa_K1592008</a></td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (61-202) + YLcwp3 Fusion</td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (61-202) + YLcwp3 Fusion</td>
−
<td>Si-tag2-his</td>
+
<td>Si-tag2</td>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592009">BBa_K1592009</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592009">BBa_K1592009</a></td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (203-273) + YLcwp3 Fusion</td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (203-273) + YLcwp3 Fusion</td>
−
<td>Si-tag3-his</td>
+
<td>Si-tag3</td>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592010">BBa_K1592010</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592010">BBa_K1592010</a></td>
 
<td>LIP2 prepro + E. coli ribosomal protein L2 (1-202)+ YLcwp3 Fusion</td>
 
<td>LIP2 prepro + E. coli ribosomal protein L2 (1-202)+ YLcwp3 Fusion</td>
−
<td>ST12</td>
+
<td>Si-tag12</td>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592011">BBa_K1592011</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592011">BBa_K1592011</a></td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (61-273) + YLcwp3 Fusion</td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (61-273) + YLcwp3 Fusion</td>
−
<td>ST23</td>
+
<td>Si-tag23</td>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592012">BBa_K1592012</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592012">BBa_K1592012</a></td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-60,203-273) + YLcwp3 Fusion</td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-60,203-273) + YLcwp3 Fusion</td>
−
<td>ST13</td>
+
<td>Si-tag13</td>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592013">BBa_K1592013</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592013">BBa_K1592013</a></td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-60,GS linker,202-273) + YLcwp3</td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-60,GS linker,202-273) + YLcwp3</td>
−
<td>ST1L3-his</td>
+
<td>Si-tag1L3</td>
 
</tr>
 
</tr>
 
<tr>
 
<tr>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592014">BBa_K1592014</a></td>
 
<td><a href="http://parts.igem.org/Part:BBa_K1592014">BBa_K1592014</a></td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-273) + YLcwp3</td>
 
<td>LIP prepro + E. coli ribosomal protein L2 (1-273) + YLcwp3</td>
−
<td>ST123</td>
+
<td>Si-tag123</td>
 
</tr>
 
</tr>
 
</table>
 
</table>

Latest revision as of 15:41, 18 September 2015

Team:HUST-China:Results


click it~

Best Part Collection:

This year, we submitted 26 new parts in total, including basic parts and composite parts. All the parts we used in our Euk.cement project were completely submitted and shipped. Particularly, we did well in the standardization of E.coli 50S ribosomal protein (Si-tag) with the different combination of domains: 1, 2, 3, 1+2,1+3,2+3,1+2+3,1L3.

We added a signal peptide and cell wall protein respectively at N-erminal and C-terminal of the Si-tags which can immobilize the working protein onto cell wall to promote the protein’s function.

The results of immunofluorescence assay showed that we succeeded in displaying the silica-tag onto the cell surface. Silica surface binding test shows each protein domain had different binding ability, so that we can choose different combinations of Si-tag domains to satisfy different requirement of binding intensity in further real utilization.

 
Part Number Description Nick Name
BBa_K1592007 LIP prepro + E. coli ribosomal protein L2 (1-60) + YLcwp3 Fusion Si-tag1
BBa_K1592008 LIP prepro + E. coli ribosomal protein L2 (61-202) + YLcwp3 Fusion Si-tag2
BBa_K1592009 LIP prepro + E. coli ribosomal protein L2 (203-273) + YLcwp3 Fusion Si-tag3
BBa_K1592010 LIP2 prepro + E. coli ribosomal protein L2 (1-202)+ YLcwp3 Fusion Si-tag12
BBa_K1592011 LIP prepro + E. coli ribosomal protein L2 (61-273) + YLcwp3 Fusion Si-tag23
BBa_K1592012 LIP prepro + E. coli ribosomal protein L2 (1-60,203-273) + YLcwp3 Fusion Si-tag13
BBa_K1592013 LIP prepro + E. coli ribosomal protein L2 (1-60,GS linker,202-273) + YLcwp3 Si-tag1L3
BBa_K1592014 LIP prepro + E. coli ribosomal protein L2 (1-273) + YLcwp3 Si-tag123