Difference between revisions of "Part:BBa K3187023"

 
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<partinfo>BBa_K3187023 short</partinfo>
 
<partinfo>BBa_K3187023 short</partinfo>
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<html>
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                <h3>Profile</h3>
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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>Tobacco Etch Virus (TEV) Protease Cleavage Site</td>
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                </tr>
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                <tr>
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                <td><b>Base pairs</b></td>
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                <td>21</td>
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                </tr>
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                <tr>
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                <td><b>Molecular weight</b></td>
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                <td>871 Da</td>
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                </tr>
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                <tr>
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                <td><b>Origin</b></td>
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                <td>Tabacco Etch Virus (TEV) </td>
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                </tr>
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                <tr>
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                <td><b>Properties</b></td>
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                <td> recognition site for the TEV protease</td>
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                </tr>
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                </table>
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                <h3> Usage and Biology</h3>
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                <p>
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The TEV potease cleavage site is the recognition sequence for a highly specific protease originated from the tabacco etch virus (TEV). The TEV protease recognizes the amino acid sequence Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) and cleaves between Gln and (Gly/Ser)
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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-1">[2]
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                            </a>
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                    </sup>
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. We are using this recognition site to cut our protein in front of its polyG tag so it has a C-terminal polyG tag that can be used in a Sortase A reaction
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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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<sup id="cite_ref-4" class="reference">
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                            <a href="#cite_note-4">[4]
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                            </a>
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                    </sup>
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<sup id="cite_ref-5" class="reference">
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                            <a href="#cite_note-5">[5]
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                            </a>
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                    </sup>
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.
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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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                            J C Carrington and W G Dougherty, A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing. Proc Natl Acad Sci U S A. 1988 May; 85(10): 3391–3395.
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                            <a rel="nofollow" class="external autonumber" href="https://dx.doi.org/10.1073%2Fpnas.85.10.3391">[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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                              Product description TEV Protease, New England Biolabs
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                            <a rel="nofollow" class="external autonumber" href="https://international.neb.com/products/p8112-tev-protease#Product Information">[2] </a>
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                            </span>
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                        </li>
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                        <li id="cite_note-3">
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-3">↑</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">[3] </a>
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                            </span>
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                        </li>
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                        <li id="cite_note-4">
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                            <span class="mw-cite-backlink">
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                                <a href="#cite_ref-4">↑</a>
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                            </span>
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                            <span class="reference-text">
 +
                              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">[4] </a>
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                            </span>
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                        </li>
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                        <li id="cite_note-5">
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                            <span class="mw-cite-backlink">
 +
                                <a href="#cite_ref-5">↑</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">[5] </a>
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                            </span>
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                        </li>
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                    </ol>
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Revision as of 13:08, 16 October 2019


Tobacco Etch Virus (TEV) Protease Cleavage Site

Profile

Name Tobacco Etch Virus (TEV) Protease Cleavage Site
Base pairs 21
Molecular weight 871 Da
Origin Tabacco Etch Virus (TEV)
Properties recognition site for the TEV protease

Usage and Biology

The TEV potease cleavage site is the recognition sequence for a highly specific protease originated from the tabacco etch virus (TEV). The TEV protease recognizes the amino acid sequence Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) and cleaves between Gln and (Gly/Ser) [1] [2] . We are using this recognition site to cut our protein in front of its polyG tag so it has a C-terminal polyG tag that can be used in a Sortase A reaction [3] [4] [5] .

References

  1. ↑ J C Carrington and W G Dougherty, A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing. Proc Natl Acad Sci U S A. 1988 May; 85(10): 3391–3395. [1]
  2. ↑ Product description TEV Protease, New England Biolabs [2]
  3. ↑ Tsukiji, S. and Nagamune, T. (2009) Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering [3]
  4. ↑ Proft, T. (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation [4]
  5. ↑ Mao, H., Hart, S. A., Schink, A., and Pollok, B. A. (2004) Sortase-mediated protein ligation: a new method for protein engineering [5]


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]