Difference between revisions of "Part:BBa K3187018"
 
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<partinfo>BBa_K3187018 short</partinfo>
 
<partinfo>BBa_K3187018 short</partinfo>
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<p>
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                <h3>Profile</h3>
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<ul>
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                <table style=“width:80%“>
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                <tr>
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                <td><b>Name</b></td>
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                <td>PolyG-tag</td>
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                </tr>
  
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<li>Name: PolyG tag </li>
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                <tr>
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<li>bp: 12</li>
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                <td><b>Base pairs</b></td>
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<li>Da: 300</li>
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                <td> 12</td>
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<li>Properties: second sequence for Sortase A</li>
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                </tr>
  
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</ul>
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                <tr>
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</p>
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                <td><b>Molecular weight</b></td>
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                <td>300 Da</td>
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                </tr>
  
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<h3>Introduction:</h3>
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                <tr>
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<p>
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                <td><b>Origin</b></td>
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The enzyme Sortase A is able to form a peptide bond between a C-terminal LPXTG motif and a N-terminal poly glycine motif <sup>[1][2][3]</sup>. The DNA sequence below is coding for four glycines that can be used as the second recognition motif in a Sortase reaction.
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                <td> Synthetic </td>
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</p>
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                </tr>
  
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<h4>Sequence:</h4>
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                </table>
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<p>
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                <h3> Usage and Biology</h3>
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GGCggaggcggt
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                <p>
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The enzyme Sortase A is able to form a peptide bond between a C-terminal LPXTG motif <a href="https://parts.igem.org/Part:BBa_K3187019">
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(BBa_K3187019)</a> and a N-terminal poly glycine motif (<a href="https://parts.igem.org/Part:BBa_K3187018"target="_blank">BBa_K3187018</a>)
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<sup id="cite_ref-1” class=”reference">
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                            <a href="#cite_note-1">[1]
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                            </a>
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                    </sup>
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<sup id="cite_ref-2” class=”reference">
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                            <a href="#cite_note-2">[2]
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                            </a>
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                    </sup>
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<sup id="cite_ref-3” class=”reference">
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                            <a href="#cite_note-3">[3]
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                            </a>
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                    </sup>
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. The sequence below is coding for four glycines that can be used as the second recognition motif in a sortase-mediated reaction. For more results visit <a
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                    href="https://parts.igem.org/Part:BBa_K3187028"
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                    target="_blank">BBa_K3187028</a>
 
</p>
 
</p>
  
  
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<h3>References:</h3>
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<p>
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[1] Tsukiji, S. and Nagamune, T. (2009) Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering ChemBioChem
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<br>
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<br>
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[2] Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation
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<br>
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<br>
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[3] Mao, H., Hart, S. A., Schink, A., and Pollok, B. A. (2004) Sortase-mediated protein ligation: a new method for protein engineering
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</p>  
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                    <h2>References</h2>
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                    <ol class="references">
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                        <li id="cite_note-1">
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-1">↑</a>
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                            </span>
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                            <span class="reference-text">
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                            Tsukiji, S. and Nagamune, T. (2009) Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1002/cbic.200800724">[1] </a>
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                            </span>
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                        </li>
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                        <li id="cite_note-2">
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-2">↑</a>
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                            </span>
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                            <span class="reference-text">
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                                Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation
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                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1007/s10529-009-0116-0">[2] </a>
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                            </span>
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                        </li>
  
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Lorem ipsum dolor sit amet, consetetur sadipscing elitr, sed diam nonumy eirmod tempor invidunt ut labore et dolore magna aliquyam erat, sed diam voluptua. At vero eos et accusam et justo duo dolores et ea rebum. Stet clita kasd gubergren, no sea takimata sanctus est Lorem ipsum dolor sit amet. Lorem ipsum dolor sit amet, consetetur sadipscing elitr, sed diam nonumy eirmod tempor invidunt ut labore et dolore magna aliquyam erat, sed diam voluptua. At vero eos et accusam et justo duo dolores et ea rebum. Stet clita kasd gubergren, no sea takimata sanctus est Lorem ipsum dolor sit amet.
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<li id="cite_note-3">
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                            <span class="mw-cite-backlink">
 +
                                <a href="#cite_ref-3">↑</a>
 +
                            </span>
 +
                            <span class="reference-text">
 +
                                Mao, H., Hart, S. A., Schink, A., and Pollok, B. A. (2004) Sortase-mediated protein ligation: a new method for protein engineering
 +
                            <a rel="nofollow" class="external autonumber" href="https://doi.org/10.1021/ja039915e">[3] </a>
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                            </span>
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                        </li>
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                    </ol>
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<!-- Add more about the biology of this part here
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</html>
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===Usage and Biology===
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Latest revision as of 17:51, 21 October 2019


PolyG Tag (GGGG) for Sortase-mediated Ligation

Profile

Name PolyG-tag
Base pairs 12
Molecular weight 300 Da
Origin Synthetic

Usage and Biology

The enzyme Sortase A is able to form a peptide bond between a C-terminal LPXTG motif (BBa_K3187019) and a N-terminal poly glycine motif (BBa_K3187018) [1] [2] [3] . The sequence below is coding for four glycines that can be used as the second recognition motif in a sortase-mediated reaction. For more results visit BBa_K3187028

References

  1. ↑ Tsukiji, S. and Nagamune, T. (2009) Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering [1]
  2. ↑ Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation [2]
  3. ↑ Mao, H., Hart, S. A., Schink, A., and Pollok, B. A. (2004) Sortase-mediated protein ligation: a new method for protein engineering [3]

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]