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

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<h2> Part Collection</h2>
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<title>Team:HUST-China:Results</title>
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<h4>Note</h4>
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<p>In order to be considered for the <a href="https://2015.igem.org/Judging/Awards#SpecialPrizes">Best Part Collection award</a>, you must fill out this page.</p>
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<p>Did your team make a lot of great parts? Is there a theme that ties all your parts together? Do you have more than 10 parts in this collection? Did you make a CRISPR collection, a MoClo collection, or a collection of awesome pigment parts? Describe your parts collection on this page, so the judges can evaluate you for the Best Part Collection award.</p>
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<h4 align="center" style="color:white"><b>click it~</b></h4>
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  <h3 style="color:black" align="center"><b>Bestآ Partآ Collection:
 +
</b></h3>
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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>
 +
<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>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>
 +
<p>Here is the collection list (click Part Number to see more details)
 +
</p>
 +
<table border="part collection">
 +
            <tr>
 +
<th>Part Number</th>
 +
<th>Description</th>
 +
<th>Abbreviation</th>
 +
</tr>
 +
<tr>
 +
<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>Si-tag1-his</td>
 +
</tr>
 +
<tr>
 +
<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>Si-tag2-his</td>
 +
</tr>
 +
<tr>
 +
<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>Si-tag3-his</td>
 +
</tr>
 +
<tr>
 +
<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>ST12</td>
 +
</tr>
 +
<tr>
 +
<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>ST23</td>
 +
</tr>
 +
<tr>
 +
<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>ST13</td>
 +
</tr>
 +
<tr>
 +
<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>ST1L3-his</td>
 +
</tr>
 +
<tr>
 +
<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>ST123</td>
 +
</tr>
 +
</table>
 +
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Revision as of 23:33, 17 September 2015

Team:HUST-China:Results


click it~

Bestآ Partآ Collection:

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.

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.

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.

Here is the collection list (click Part Number to see more details)

Part Number Description Abbreviation
BBa_K1592007 LIP prepro + E. coli ribosomal protein L2 (1-60) + YLcwp3 Fusion Si-tag1-his
BBa_K1592008 LIP prepro + E. coli ribosomal protein L2 (61-202) + YLcwp3 Fusion Si-tag2-his
BBa_K1592009 LIP prepro + E. coli ribosomal protein L2 (203-273) + YLcwp3 Fusion Si-tag3-his
BBa_K1592010 LIP2 prepro + E. coli ribosomal protein L2 (1-202)+ YLcwp3 Fusion ST12
BBa_K1592011 LIP prepro + E. coli ribosomal protein L2 (61-273) + YLcwp3 Fusion ST23
BBa_K1592012 LIP prepro + E. coli ribosomal protein L2 (1-60,203-273) + YLcwp3 Fusion ST13
BBa_K1592013 LIP prepro + E. coli ribosomal protein L2 (1-60,GS linker,202-273) + YLcwp3 ST1L3-his
BBa_K1592014 LIP prepro + E. coli ribosomal protein L2 (1-273) + YLcwp3 ST123