Latest revision as of 02:47, 19 September 2015

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"All in all it's just another brick in the wall" - Pink Floyd

Submitted Parts

Below are our submitted parts. If you want to dig deeper and explore sequencing, characterization etc. click the links and you will be directed to the parts registry page.

Standard Two-hybrid System Devices

BBa_K1638005
Plac-T18: The T18 domain of cyaA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions.

BBa_K1638003
Plac-T25: The T25 domain of cyaA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions.

BBa_K1638032
PcstA-RFP-term-Plac-T18: The T18 domain of cyaA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions. The cAMP-induced promoter PcstA induce transcription of RFP when a protein-protein interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.

BBa_K1638033
PcstA-RFP-term-Plac-T25: The T25 domain of cyaAA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions. The cAMP-induced promoter PcstA induce transcription of RFP when a protein-protein interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.

Control Devices

BBa_K1638011
Plac-T18-Zip: Leucine Zipper fused to the T18 domain of cyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer.

BBa_K1638013
Plac-T25-Zip: Leucine Zipper fused to the T25 domain of cyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer.

BBa_K1638031
PcstA-RFP-term-Plac-T18-Zip: Leucine Zipper fused to the T18 domain of cyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.

BBa_K1638030
PcstA-RFP-term-Plac-T25-Zip: Leucine Zipper fused to the T25 domain of cyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.

Screening Devices

BBa_K1638018
PLlacO-1-T18-linker-hTrx_scaffold-(3xFlag): The human thioredoxin scaffold fused to the T18 domain of cyaA through a flexible linker. The human thioredoxin scaffold is a scaffold used for presentation of peptide aptamers. When a random nucleotide library is inserted into the scaffold, one can use the bacterial two-hybrid system to screen against specific targets. An affinity 3xFlag-tag is fused to the C-terminal for detection purposes. The part is under control of the hybrid PLlacO-1 promoter.

BBa_K1638035
Plac-T18-linker-Intein-hTrx_scaffold-(3xFlag): The human thioredoxin scaffold fused to the T18 domain of cyaA through intein and a flexible linker. The human thioredoxin scaffold is a scaffold used for presentation of peptide aptamers. When a random nucleotide library is inserted into the scaffold, one can use the bacterial two-hybrid system to screen against specific targets. The intein is added for affinity purification purposes. This allows us to only purify the pure hTrx-based peptide aptamer. An affinity 3xFlag-tag is fused to the C-terminal for detection purposes.

BBa_K1638037
PcstA-RFP-term-Plac-T25-linker-CsrA: The carbon storage regulator CsrA fused to the T25 domain of the adenylate cyclase, CyaA. Made for the purpose to be a 'bait' in a peptide-aptamer screening using the hTrx-based peptide aptamer fused to the T18 domain of CyaA. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.

BBa_K1638038
PcstA-RFP-term-Plac-T25-linker-YhbJ: The RNase adapter protein YhbJ fused to the T25 domain of the adenylate cyclase, CyaA. Made for the purpose to be a 'bait' in a peptide-aptamer screening using the hTrx-based peptide aptamer fused to the T18 domain of CyaA. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.

BBa_K1638039
PcstA-RFP-term-Plac-T25-linker-Hfq: The RNA-binding protein Hfq fused to the T25 domain of the adenylate cyclase, CyaA. Made for the purpose to be a 'bait' in a peptide-aptamer screening using the hTrx-based peptide aptamer fused to the T18 domain of CyaA. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.

Reporter Fusions

BBa_K1638009
Plac-T18-linker-GFP: Green Fluorescent Protein (GFP) fused to the T18 domain of the adenylate cyclase CyaA through a flexible linker. This part is used to check gene expression and validate that T18-fusion proteins will fold correctly.

BBa_K1638010
Plac-T25-linker-GFP: Green Fluorescent Protein (GFP) fused to the T25 domain of the adenylate cyclase CyaA through a flexible linker. This part is used to check gene expression and validate that T25-fusion proteins will fold correctly.

BBa_K1638007
linker-GFP: A flexible 10 amino acid linker fused to the N-terminal part of GFP. Intended for use in protein-GFP fusions, where this part can be suffixed to various proteins as a reporter of gene expression.

Others

BBa_K1638036
PLlacO-1-Intein: This part consist of an intein from Saccharomyces cerevisiae VMA1 gene including a CBD-tag. This intein is a thiol-induced self-cleavable protein that enables the release of a C-terminal fused protein. The intein is under control of the hybrid PLlacO-1 promoter.

@@ Line 2: / Line 2: @@
 <html>
+<p> <i> "All in all it's just another brick in the wall" - <b>Pink Floyd</b></i></p>
 <h1 align="center" style="opacity: 1;"> Submitted Parts</h1>
-<p> Below mentioned are the submitted parts. To explore sequencing, characterization etc. click the links and you will be directed to the parts registry page. </p>
+<p><b>Below are our submitted parts.</b> If you want to dig deeper and explore sequencing, characterization etc. click the links and you will be directed to the parts registry page.</p>
+<br>
 <div class="accordion"  style="width:100%;">
    <div class="accordionTitel">Standard Two-hybrid System Devices</div>
-   <div class="pane current" style="height:380px;" >
+   <div class="pane current" style="height:360px;" >
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638005" target="_blank">BBa_K1638005</a></span><br>
 <span class="intro">Plac-T18:</span>
-The T18 domain of CyaA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions.
+The T18 domain of <i>cyaA</i> with a <i>lac</i> promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions.
 <br><br>
@@ Line 21: / Line 22: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638003" target="_blank">BBa_K1638003</a></span><br>
 <span class="intro">Plac-T25:</span>
-The T25 domain of CyaA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions.
+The T25 domain of <i>cyaA</i> with a <i>lac</i> promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions.
 <br><br>
@@ Line 27: / Line 28: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638032" target="_blank">BBa_K1638032</a></span><br>
 <span class="intro">PcstA-RFP-term-Plac-T18:</span>
-The T18 domain of CyaA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions. The cAMP-induced promoter PcstA induce transcription of RFP when a protein-protein interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
+The T18 domain of <i>cyaA</i> with a <i>lac</i> promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions. The cAMP-induced promoter PcstA induce transcription of RFP when a protein-protein interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
 <br><br>
@@ Line 33: / Line 34: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638033" target="_blank">BBa_K1638033</a></span><br>
 <span class="intro">PcstA-RFP-term-Plac-T25:</span>
-The T25 domain of CyaA with a lac promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions. The cAMP-induced promoter PcstA induce transcription of RFP when a protein-protein interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
+The T25 domain of <i>cyaA</i>A with a <i>lac</i> promoter. Intented for use in the bacterial two-hybrid system, where a protein of interest can be fused to the C-terminal. The bacterial two-hybrid system allows detection of protein-protein interactions. The cAMP-induced promoter PcstA induce transcription of RFP when a protein-protein interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
    </div>
@@ Line 39: / Line 40: @@
    <div class="accordionTitel">Control Devices</div>
-   <div class="pane" style="height:375px;" >
+   <div class="pane" style="height:355px;" >
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638011" target="_blank">BBa_K1638011</a></span><br>
 <span class="intro">Plac-T18-Zip:</span>
-Leucine Zipper fused to the T18 domain of CyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer.
+Leucine Zipper fused to the T18 domain of <i>cyaA</i>. The expression of the gene is under control of a <i>lac</i> promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer.
 <br><br>
@@ Line 49: / Line 50: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638013" target="_blank">BBa_K1638013</a></span><br>
 <span class="intro">Plac-T25-Zip:</span>
-Leucine Zipper fused to the T25 domain of CyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer.
+Leucine Zipper fused to the T25 domain of <i>cyaA</i>. The expression of the gene is under control of a <i>lac</i> promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer.
 <br><br>
@@ Line 55: / Line 56: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638031" target="_blank">BBa_K1638031</a></span><br>
 <span class="intro">PcstA-RFP-term-Plac-T18-Zip:</span>
-Leucine Zipper fused to the T18 domain of CyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
+Leucine Zipper fused to the T18 domain of <i>cyaA</i>. The expression of the gene is under control of a <i>lac</i> promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
 <br><br>
@@ Line 61: / Line 62: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638030" target="_blank">BBa_K1638030</a></span><br>
 <span class="intro">PcstA-RFP-term-Plac-T25-Zip:</span>
-Leucine Zipper fused to the T25 domain of CyaA. The expression of the gene is under control of a lac promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
+Leucine Zipper fused to the T25 domain of <i>cyaA</i>. The expression of the gene is under control of a <i>lac</i> promoter. This part can be used to validate the bacterial two-hybrid system as leucine zippers is known to form a homodimer. The cAMP-induced promoter PcstA induce transcription of RFP when a positive interaction occurs and the T18 and T25 domains associate and catalyse the formation of cAMP.
    </div>
@@ Line 70: / Line 71: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638018" target="_blank">BBa_K1638018</a></span><br>
-<span class="intro">PLlac-T18-linker-hTrx_scaffold-(3xFlag):</span>
+<span class="intro">PLlacO-1-T18-linker-hTrx_scaffold-(3xFlag):</span>
-The human thioredoxin scaffold fused to the T18 domain of CyaA through a flexible linker. The human thioredoxin scaffold is a scaffold used for presentation of peptide aptamers. When a random nucleotide library is inserted into the scaffold, one can use the bacterial two-hybrid system to screen against specific targets. An affinity 3xFlag-tag is fused to the C-terminal for detection purposes.
+The human thioredoxin scaffold fused to the T18 domain of <i>cyaA</i> through a flexible linker. The human thioredoxin scaffold is a scaffold used for presentation of peptide aptamers. When a random nucleotide library is inserted into the scaffold, one can use the bacterial two-hybrid system to screen against specific targets. An affinity 3xFlag-tag is fused to the C-terminal for detection purposes. The part is under control of the hybrid PLlacO-1 promoter.
 <br><br>
@@ Line 77: / Line 78: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638035" target="_blank">BBa_K1638035</a></span><br>
 <span class="intro">Plac-T18-linker-Intein-hTrx_scaffold-(3xFlag):</span>
-The human thioredoxin scaffold fused to the T18 domain of CyaA through intein and a flexible linker. The human thioredoxin scaffold is a scaffold used for presentation of peptide aptamers. When a random nucleotide library is inserted into the scaffold, one can use the bacterial two-hybrid system to screen against specific targets. The intein is added for affinity purification purposes. This allows us to only purify the pure hTrx-based peptide aptamer. An affinity 3xFlag-tag is fused to the C-terminal for detection purposes.
+The human thioredoxin scaffold fused to the T18 domain of <i>cyaA</i> through intein and a flexible linker. The human thioredoxin scaffold is a scaffold used for presentation of peptide aptamers. When a random nucleotide library is inserted into the scaffold, one can use the bacterial two-hybrid system to screen against specific targets. The intein is added for affinity purification purposes. This allows us to only purify the pure hTrx-based peptide aptamer. An affinity 3xFlag-tag is fused to the C-terminal for detection purposes.
 <br><br>
@@ Line 101: / Line 102: @@
    <div class="accordionTitel">Reporter Fusions</div>
-   <div class="pane" style="height:225px;" >
+   <div class="pane" style="height:205px;" >
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638009" target="_blank">BBa_K1638009</a></span><br>
 <span class="intro">Plac-T18-linker-GFP:</span>
-The T18 domain of CyaA to be used in the bacterial two-hybrid system. The expression of the gene is under control of a lac promoter. The bacterial two-hybrid system allows detection of protein-protein interactions
+Green Fluorescent Protein (GFP) fused to the T18 domain of the adenylate cyclase CyaA through a flexible linker. This part is used to check gene expression and validate that T18-fusion proteins will fold correctly.
 <br><br>
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638010" target="_blank">BBa_K1638010</a></span><br>
 <span class="intro">Plac-T25-linker-GFP:</span>
-The T25 domain of CyaA to be used in the bacterial two-hybrid system. The expression of the gene is under control of a lac promoter. The bacterial two-hybrid system allows detection of protein-protein interactions
+Green Fluorescent Protein (GFP) fused to the T25 domain of the adenylate cyclase CyaA through a flexible linker. This part is used to check gene expression and validate that T25-fusion proteins will fold correctly.
 <br><br>
@@ Line 117: / Line 117: @@
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638007" target="_blank">BBa_K1638007</a></span><br>
 <span class="intro">linker-GFP:</span>
-The T25 domain of CyaA to be used in the bacterial two-hybrid system. The expression of the gene is under control of a lac promoter. The bacterial two-hybrid system allows detection of protein-protein interactions
+A flexible 10 amino acid linker fused to the N-terminal part of GFP. Intended for use in protein-GFP fusions, where this part can be suffixed to various proteins as a reporter of gene expression.
    </div>
@@ Line 123: / Line 123: @@
    <div class="accordionTitel">Others</div>
-   <div class="pane" style="height:50px;" >
+   <div class="pane" style="height:70px;" >
 <span class="intro"><a class="dialogLink" href="http://parts.igem.org/Part:BBa_K1638036" target="_blank">BBa_K1638036</a></span><br>
-<span class="intro">PLlac-Intein:</span>
+<span class="intro">PLlacO-1-Intein:</span>
-The T18 domain of CyaA to be used in the bacterial two-hybrid system. The expression of the gene is under control of a lac promoter. The bacterial two-hybrid system allows detection of protein-protein interactions
+This part consist of an intein from <i>Saccharomyces cerevisiae</i> <i>VMA1</i> gene including a CBD-tag. This intein is a thiol-induced self-cleavable protein that enables the release of a C-terminal fused protein. The intein is under control of the hybrid PLlacO-1 promoter.
    </div>
@@ Line 133: / Line 133: @@
 </div>
-<p>Each team will make new parts during iGEM and will submit them to the Registry of Standard Biological Parts. The iGEM software provides an easy way to present the parts your team has created. The <code>&lt;groupparts&gt;</code> tag (see below) will generate a table with all of the parts that your team adds to your team sandbox.</p>
-<p>Remember that the goal of proper part documentation is to describe and define a part, so that it can be used without needing to refer to the primary literature. Registry users in future years should be able to read your documentation and be able to use the part successfully. Also, you should provide proper references to acknowledge previous authors and to provide for users who wish to know more.</p>
-<div class="highlightBox">
-<h4>Note</h4>
-<p>Note that parts must be documented on the <a href="http://parts.igem.org/Main_Page"> Registry</a>. This page serves to <i>showcase</i> the parts you have made. Future teams and other users and are much more likely to find parts by looking in the Registry than by looking at your team wiki.</p>
-</div>
-<h4>Adding parts to the registry</h4>
-<p>You can add parts to the Registry at our <a href="http://parts.igem.org/Add_a_Part_to_the_Registry">Add a Part to the Registry</a> link.</p>
-<p>We encourage teams to start completing documentation for their parts on the Registry as soon as you have it available. The sooner you put up your parts, the better you will remember all the details about your parts. Remember, you don't need to send us the DNA sample before you create an entry for a part on the Registry. (However, you <b>do</b> need to send us the DNA sample before the Jamboree. If you don't send us a DNA sample of a part, that part will not be eligible for awards and medal criteria.)</p>
-<h4>What information do I need to start putting my parts on the Registry?</h4>
-<p>The information needed to initially create a part on the Registry is:</p>
-<ul>
-<li>Part Name</li>
-<li>Part type</li>
-<li>Creator</li>
-<li>Sequence</li>
-<li>Short Description (60 characters on what the DNA does)</li>
-<li>Long Description (Longer description of what the DNA does)</li>
-<li>Design considerations</li>
-</ul>
-<p>
-We encourage you to put up <em>much more</em> information as you gather it over the summer. If you have images, plots, characterization data and other information, please also put it up on the part page. </p>
-<h4>Inspiration</h4>
-<p>We have a created  a <a href="http://parts.igem.org/Well_Documented_Parts">collection of well documented parts</a> that can help you get started.</p>
 </html>
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Difference between revisions of "Team:SDU-Denmark/Tour53"

Latest revision as of 02:47, 19 September 2015

Submitted Parts