http://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&feed=atom&action=historyTeam:Aachen/Project/Gal3 - Revision history2024-03-28T17:58:53ZRevision history for this page on the wikiMediaWiki 1.16.5http://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=397351&oldid=prevNbailly at 03:28, 18 October 20142014-10-18T03:28:26Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Characteristic parts of the '''lipopolysaccharide structure (LPS)''' of ''P. aeruginosa'' can be bound by galectin-3. Specifically, the O polysaccharide (see figure on the left) of the LPS is recognized by galectin-3. Therefore, this specific binding of galectin-3 enables the construction of a fluorescent based detection system. A fusion protein of galectin-3 and a reporter protein, such as a fluorescent protein, can be built and applied in the detection of ''P.&nbsp;aeruginosa''.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Characteristic parts of the '''lipopolysaccharide structure (LPS)''' of ''P.<ins class="diffchange diffchange-inline">&nbsp;</ins>aeruginosa'' can be bound by galectin-3. Specifically, the O polysaccharide (see figure on the left) of the LPS is recognized by galectin-3. Therefore, this specific binding of galectin-3 enables the construction of a fluorescent based detection system. A fusion protein of galectin-3 and a reporter protein, such as a fluorescent protein, can be built and applied in the detection of ''P.&nbsp;aeruginosa''.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In our approach, a '''galectin-3-YFP fusion protein''' is built and expressed in ''E.&nbsp;coli'', including a his-tag and a snap-tag for purification. The fusion protein can then be incorporated into a '''cell-free biosensor system'''. These biosensors have many advantages over systems that use living cells such as an uncomplicated storage. Furthermore, from a [https://2014.igem.org/Team:Aachen/Safety biosafety] and social acceptance point of view, it is advantageous if the sensor system does not contain alive genetically modified organisms.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In our approach, a '''galectin-3-YFP fusion protein''' is built and expressed in ''E.&nbsp;coli'', including a his-tag and a snap-tag for purification. The fusion protein can then be incorporated into a '''cell-free biosensor system'''. These biosensors have many advantages over systems that use living cells such as an uncomplicated storage. Furthermore, from a [https://2014.igem.org/Team:Aachen/Safety biosafety] and social acceptance point of view, it is advantageous if the sensor system does not contain alive genetically modified organisms.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>With the help of David Schönauer and Alan Mertens from the RWTH Aachen Institute of Biotechnolgy we then purified the fusion protein using FPLC.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>With the help of David Schönauer and Alan Mertens from the RWTH Aachen Institute of Biotechnolgy we then purified the fusion protein using FPLC.</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Subsequently, we aimed to test the binding of the Gal-3 fusion protein to the LPS of ''P. aeruginosa'' as shown previously (Kupper, Böcker, Liu et al., 2013). Apparently, because of insufficient sensitivity of the used fluorescence microscope, this could not be confirmed and would require further experiments, idealy using other detection methods.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Subsequently, we aimed to test the binding of the Gal-3 fusion protein to the LPS of ''P.<ins class="diffchange diffchange-inline">&nbsp;</ins>aeruginosa'' as shown previously (Kupper, Böcker, Liu et al., 2013). Apparently, because of insufficient sensitivity of the used fluorescence microscope, this could not be confirmed and would require further experiments, idealy using other detection methods.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>After we received the collection of [https://2014.igem.org/Team:Aachen/Collaborations/Heidelberg pSBX-expression vectors] from Team Heidelberg, we used Gibson assembly to make K1319020 from K1319003 and pSBX1A3, which is the translational unit for an mRFP-Gal3 fusion protein with a C-terminal 6xHis tag:</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>After we received the collection of [https://2014.igem.org/Team:Aachen/Collaborations/Heidelberg pSBX-expression vectors] from Team Heidelberg, we used Gibson assembly to make K1319020 from K1319003 and pSBX1A3, which is the translational unit for an mRFP-Gal3 fusion protein with a C-terminal 6xHis tag:</div></td></tr>
</table>Nbaillyhttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=397145&oldid=prevNbailly: /* Achievements */2014-10-18T03:27:10Z<p><span class="autocomment">Achievements</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>With the help of David Schönauer and Alan Mertens from the RWTH Aachen Institute of Biotechnolgy we then purified the fusion protein using FPLC.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>With the help of David Schönauer and Alan Mertens from the RWTH Aachen Institute of Biotechnolgy we then purified the fusion protein using FPLC.</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Subsequently, we aimed to test the binding of the Gal-3 fusion protein to the LPS of ''P. aeruginosa'' as shown previously <del class="diffchange diffchange-inline">[1]</del>. Apparently, because of insufficient sensitivity of the used fluorescence microscope, this could not be confirmed and would require further experiments, idealy using other detection methods.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Subsequently, we aimed to test the binding of the Gal-3 fusion protein to the LPS of ''P. aeruginosa'' as shown previously <ins class="diffchange diffchange-inline">(Kupper, Böcker, Liu et al., 2013)</ins>. Apparently, because of insufficient sensitivity of the used fluorescence microscope, this could not be confirmed and would require further experiments, idealy using other detection methods.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>After we received the collection of [https://2014.igem.org/Team:Aachen/Collaborations/Heidelberg pSBX-expression vectors] from Team Heidelberg, we used Gibson assembly to make K1319020 from K1319003 and pSBX1A3, which is the translational unit for an mRFP-Gal3 fusion protein with a C-terminal 6xHis tag:</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>After we received the collection of [https://2014.igem.org/Team:Aachen/Collaborations/Heidelberg pSBX-expression vectors] from Team Heidelberg, we used Gibson assembly to make K1319020 from K1319003 and pSBX1A3, which is the translational unit for an mRFP-Gal3 fusion protein with a C-terminal 6xHis tag:</div></td></tr>
</table>Nbaillyhttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=397004&oldid=prevNbailly at 03:26, 18 October 20142014-10-18T03:26:22Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>|Aachen_14-10-04_Expression_Pellets_iMO.png|Aachen_Gal3_Expression.png|title1=Pellets of different fusion protein expressions|title2=SDS-PAGE of K1319020 expression|subtitle1=Expression in the pET17 vector was much more leaky than the expression in the pSBX vectors.|subtitle2=The fusion protein was fully translated to the correct molecular mass of 74&nbsp;kDa.|width=425px}} </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>|Aachen_14-10-04_Expression_Pellets_iMO.png|Aachen_Gal3_Expression.png|title1=Pellets of different fusion protein expressions|title2=SDS-PAGE of K1319020 expression|subtitle1=Expression in the pET17 vector was much more leaky than the expression in the pSBX vectors.|subtitle2=The fusion protein was fully translated to the correct molecular mass of 74&nbsp;kDa.|width=425px}} </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== References ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== References ==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del class="diffchange diffchange-inline">[1] </del>Kupper <del class="diffchange diffchange-inline">CE</del>, Böcker S, <del class="diffchange diffchange-inline">Liu </del>H, et al. Fluorescent SNAP-tag galectin fusion proteins as novel tools in glycobiology. <del class="diffchange diffchange-inline">Curr Pharm Des. 2013;</del>19(30)<del class="diffchange diffchange-inline">:</del>5457-67. Available at: http://www.ncbi.nlm.nih.gov/pubmed/23431989. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Kupper<ins class="diffchange diffchange-inline">, C. E.</ins>, Böcker<ins class="diffchange diffchange-inline">, </ins>S<ins class="diffchange diffchange-inline">., Elling, L., Lui</ins>, H<ins class="diffchange diffchange-inline">., Adamzyk, C., de Kamp, J. v.</ins>, et al<ins class="diffchange diffchange-inline">. (2013)</ins>. Fluorescent SNAP-tag galectin fusion proteins as novel tools in glycobiology. <ins class="diffchange diffchange-inline">Current Pharmaceutical Design, </ins>19(30)<ins class="diffchange diffchange-inline">, </ins>5457-67. Available at: http://www.ncbi.nlm.nih.gov/pubmed/23431989. </div></td></tr>
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</table>Nbaillyhttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=396294&oldid=prevNbailly: /* Natural Functions of Galectin-3 */2014-10-18T03:22:26Z<p><span class="autocomment">Natural Functions of Galectin-3</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Human galectin-3 is a protein of the lectin-family that was shown to bind the LPS of multiple human pathogens. Some of them, including ''P.&nbsp;aeruginosa'' protect themselves against the human immune system by mimicking the lipopolysaccharides (LPS) present on human erythrocytes.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Human galectin-3 is a protein of the lectin-family that was shown to bind the LPS of multiple human pathogens. Some of them, including ''P.&nbsp;aeruginosa'' protect themselves against the human immune system by mimicking the lipopolysaccharides (LPS) present on human erythrocytes.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>By making fusion proteins of galectin-3 with fluorescent reporter proteins, pathogens can be labelled and '''made visible by fluorescence-microscopy'''.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>By making fusion proteins of galectin-3 with fluorescent reporter proteins, pathogens can be labelled and '''made visible by fluorescence-microscopy'''.</div></td></tr>
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</table>Nbaillyhttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=389122&oldid=prevPdemling: /* Galectin-3 */2014-10-18T02:29:37Z<p><span class="autocomment">Galectin-3</span></p>
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</table>Pdemlinghttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=386975&oldid=prevR.hanke: /* An Alternative Sensing Molecule */2014-10-18T02:10:46Z<p><span class="autocomment">An Alternative Sensing Molecule</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>{{Team:Aachen/FigureFloat|Aachen_14-10-09_Pseudomonas_LPS_iNB.png|title=Cell wall composition of ''P. aeruginosa''|subtitle=Gram-negative bacteria have two cell membranes. The LPS are embedded in the outer membrane and are composed of a lipid and an O polysaccharide.|width=420px}}</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>{{Team:Aachen/FigureFloat|Aachen_14-10-09_Pseudomonas_LPS_iNB.png|title=Cell wall composition of ''P. aeruginosa''|subtitle=Gram-negative bacteria have two cell membranes. The LPS are embedded in the outer membrane and are composed of a lipid and an O polysaccharide.|width=420px}}</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del class="diffchange diffchange-inline">The specific binding of galectin-3 enables the construction of a fluorescent based detection system when fusing to a fluorescent protein. Parts </del>of the '''lipopolysaccharide structure (LPS)''' of ''P. aeruginosa'' can be bound by galectin-3. Specifically, the O polysaccharide (see figure on the left) of the LPS is recognized by galectin-3. A fusion protein of galectin-3 and a reporter protein, such as a fluorescent protein, can be built and applied in the detection of ''P.&nbsp;aeruginosa''.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins class="diffchange diffchange-inline">Characteristic parts </ins>of the '''lipopolysaccharide structure (LPS)''' of ''P. aeruginosa'' can be bound by galectin-3. Specifically, the O polysaccharide (see figure on the left) of the LPS is recognized by galectin-3. <ins class="diffchange diffchange-inline">Therefore, this specific binding of galectin-3 enables the construction of a fluorescent based detection system. </ins>A fusion protein of galectin-3 and a reporter protein, such as a fluorescent protein, can be built and applied in the detection of ''P.&nbsp;aeruginosa''.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>In our approach, a '''galectin-3-YFP fusion protein''' is built and expressed in ''E.&nbsp;coli''<del class="diffchange diffchange-inline">. A </del>his-tag and a snap-tag for purification <del class="diffchange diffchange-inline">are included</del>. The fusion protein can then be incorporated into a '''cell-free biosensor system'''. <del class="diffchange diffchange-inline">Such </del>biosensors have many advantages over systems that use living cells<del class="diffchange diffchange-inline">; </del>storage, <del class="diffchange diffchange-inline">for example, is much easier. From </del>a [https://2014.igem.org/Team:Aachen/Safety biosafety] and social acceptance <del class="diffchange diffchange-inline">perspective</del>, it is <del class="diffchange diffchange-inline">also </del>advantageous if the sensor system does not contain <del class="diffchange diffchange-inline">live </del>genetically modified organisms.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>In our approach, a '''galectin-3-YFP fusion protein''' is built and expressed in ''E.&nbsp;coli''<ins class="diffchange diffchange-inline">, including a </ins>his-tag and a snap-tag for purification. The fusion protein can then be incorporated into a '''cell-free biosensor system'''. <ins class="diffchange diffchange-inline">These </ins>biosensors have many advantages over systems that use living cells <ins class="diffchange diffchange-inline">such as an uncomplicated </ins>storage<ins class="diffchange diffchange-inline">. Furthermore</ins>, <ins class="diffchange diffchange-inline">from </ins>a [https://2014.igem.org/Team:Aachen/Safety biosafety] and social acceptance <ins class="diffchange diffchange-inline">point of view</ins>, it is advantageous if the sensor system does not contain <ins class="diffchange diffchange-inline">alive </ins>genetically modified organisms.</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>To detect ''P.&nbsp;aeruginosa'' cells, an agar chip could be used to sample a solid surface. However, other materials but agar can be considered to collect <del class="diffchange diffchange-inline">the </del>pathogens. The <del class="diffchange diffchange-inline">cell </del>stick to the sampling chip which is then immersed in a detection buffer containing the galectin-3-YFP fusion protein. Excess protein is removed during washing in a suitable buffer. The galectin-3 remains bound to the pathogen and '''illumination with 514&nbsp;nm''', the excitation <del class="diffchange diffchange-inline">frequency </del>of YFP, in a modified version of our measurement device reveals the location of the cells. The picture taken by the measurement device can then be analyzed by our software ''Measurarty''.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>To detect ''P.&nbsp;aeruginosa'' cells, an agar chip could be used to sample a solid surface. However, other materials but agar can be considered to collect pathogens. The <ins class="diffchange diffchange-inline">cells </ins>stick to the sampling chip which is then immersed in a detection buffer containing the galectin-3-YFP fusion protein. Excess protein is removed during washing in a suitable buffer. The galectin-3 remains bound to the pathogen and '''illumination with 514&nbsp;nm''', the excitation <ins class="diffchange diffchange-inline">wavelength </ins>of YFP, in a modified version of our measurement device reveals the location of the cells. The picture taken by the measurement device can then be analyzed by our software ''Measurarty''.</div></td></tr>
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</table>R.hankehttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=386039&oldid=prevR.hanke: /* An Alternative Sensing Molecule */2014-10-18T02:01:58Z<p><span class="autocomment">An Alternative Sensing Molecule</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>{{Team:Aachen/FigureFloat|Aachen_14-10-09_Pseudomonas_LPS_iNB.png|title=Cell wall composition of ''P. aeruginosa''|subtitle=Gram-negative bacteria have two cell membranes. The LPS are embedded in the outer membrane and are composed of a lipid and an O polysaccharide.|width=420px}}</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>{{Team:Aachen/FigureFloat|Aachen_14-10-09_Pseudomonas_LPS_iNB.png|title=Cell wall composition of ''P. aeruginosa''|subtitle=Gram-negative bacteria have two cell membranes. The LPS are embedded in the outer membrane and are composed of a lipid and an O polysaccharide.|width=420px}}</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>The specific binding of galectin-3 enables the construction of <del class="diffchange diffchange-inline">such </del>a detection system. Parts of the '''lipopolysaccharide structure (LPS)''' of ''P. aeruginosa'' can be bound by galectin-3. Specifically, the O polysaccharide (see figure on the left) of the LPS is recognized by galectin-3. A fusion protein of galectin-3 and a reporter protein, such as a fluorescent protein, can be built and applied in the detection of ''P.&nbsp;aeruginosa''.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>The specific binding of galectin-3 enables the construction of a <ins class="diffchange diffchange-inline">fluorescent based </ins>detection system <ins class="diffchange diffchange-inline">when fusing to a fluorescent protein</ins>. Parts of the '''lipopolysaccharide structure (LPS)''' of ''P. aeruginosa'' can be bound by galectin-3. Specifically, the O polysaccharide (see figure on the left) of the LPS is recognized by galectin-3. A fusion protein of galectin-3 and a reporter protein, such as a fluorescent protein, can be built and applied in the detection of ''P.&nbsp;aeruginosa''.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In our approach, a '''galectin-3-YFP fusion protein''' is built and expressed in ''E.&nbsp;coli''. A his-tag and a snap-tag for purification are included. The fusion protein can then be incorporated into a '''cell-free biosensor system'''. Such biosensors have many advantages over systems that use living cells; storage, for example, is much easier. From a [https://2014.igem.org/Team:Aachen/Safety biosafety] and social acceptance perspective, it is also advantageous if the sensor system does not contain live genetically modified organisms.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>In our approach, a '''galectin-3-YFP fusion protein''' is built and expressed in ''E.&nbsp;coli''. A his-tag and a snap-tag for purification are included. The fusion protein can then be incorporated into a '''cell-free biosensor system'''. Such biosensors have many advantages over systems that use living cells; storage, for example, is much easier. From a [https://2014.igem.org/Team:Aachen/Safety biosafety] and social acceptance perspective, it is also advantageous if the sensor system does not contain live genetically modified organisms.</div></td></tr>
</table>R.hankehttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=385834&oldid=prevR.hanke: /* Galectin-3 */2014-10-18T02:00:02Z<p><span class="autocomment">Galectin-3</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <div class="team-item team-info" ></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <div class="team-item team-info" ></div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <div class="menukachel" style="line-height:1.5em;top:<del class="diffchange diffchange-inline">25</del>%;">An Alternative Sensing Molecule</div></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <div class="menukachel" style="line-height:1.5em;top:<ins class="diffchange diffchange-inline">33</ins>%;">An Alternative Sensing Molecule</div></div></td></tr>
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</table>R.hankehttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=385788&oldid=prevR.hanke: /* Galectin-3 */2014-10-18T01:59:40Z<p><span class="autocomment">Galectin-3</span></p>
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</table>R.hankehttp://2014.igem.org/wiki/index.php?title=Team:Aachen/Project/Gal3&diff=385533&oldid=prevR.hanke: /* An Alternative Sensing Molecule */2014-10-18T01:57:20Z<p><span class="autocomment">An Alternative Sensing Molecule</span></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 01:57, 18 October 2014</td>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del style="color: red; font-weight: bold; text-decoration: none;">To detect ''P.&nbsp;aeruginosa'' cells, an agar chip could be used to sample a solid surface. However, other materials but agar can be considered to collect the pathogens. The cell stick to the sampling chip which is then immersed in a detection buffer containing the galectin-3-YFP fusion protein. Excess protein is removed during washing in a suitable buffer. The galectin-3 remains bound to the pathogen and '''illumination with 514&nbsp;nm''', the excitation frequency of YFP, in a modified version of our measurement device reveals the location of the cells. The picture taken by the measurement device can then be analyzed by our software ''Measurarty''.</del></div></td><td colspan="2"> </td></tr>
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<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;">To detect ''P.&nbsp;aeruginosa'' cells, an agar chip could be used to sample a solid surface. However, other materials but agar can be considered to collect the pathogens. The cell stick to the sampling chip which is then immersed in a detection buffer containing the galectin-3-YFP fusion protein. Excess protein is removed during washing in a suitable buffer. The galectin-3 remains bound to the pathogen and '''illumination with 514&nbsp;nm''', the excitation frequency of YFP, in a modified version of our measurement device reveals the location of the cells. The picture taken by the measurement device can then be analyzed by our software ''Measurarty''.</ins></div></td></tr>
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</table>R.hanke