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Commit 3202dfd0 authored by Ranjit Patro's avatar Ranjit Patro :slight_smile:
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Update public/contribution

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......@@ -221,16 +221,16 @@
parts
have been added to the Registry of Standard biological parts:
<ul>
<li>pET28b FimH1F: <a href="http://parts.igem.org/Part:BBa_K4449003">BBa_K4449003</a>
<li>pET28b FimH1 F: <a href="http://parts.igem.org/Part:BBa_K4449003">BBa_K4449003</a>
</li>
<li>pET28b FimH1R: <a href="http://parts.igem.org/Part:BBa_K4449004">BBa_K4449004</a>
<li>pET28b FimH1 R: <a href="http://parts.igem.org/Part:BBa_K4449004">BBa_K4449004</a>
</li>
<li>pET15b FimH2F: <a href="http://parts.igem.org/Part:BBa_K4449005">BBa_K4449005</a>
<li>pET15b FimH2 F: <a href="http://parts.igem.org/Part:BBa_K4449005">BBa_K4449005</a>
</li>
<li>pET15b FimH2F: <a href="http://parts.igem.org/Part:BBa_K4449006">BBa_K4449006</a>
<li>pET15b FimH2 F: <a href="http://parts.igem.org/Part:BBa_K4449006">BBa_K4449006</a>
</li>
<li>pET28b BhpF: <a href="http://parts.igem.org/Part:BBa_K4449007">BBa_K4449007</a></li>
<li>pET28b BhpR: <a href="http://parts.igem.org/Part:BBa_K4449008">BBa_K4449008</a></li>
<li>pET28b Bhp F: <a href="http://parts.igem.org/Part:BBa_K4449007">BBa_K4449007</a></li>
<li>pET28b Bhp R: <a href="http://parts.igem.org/Part:BBa_K4449008">BBa_K4449008</a></li>
</ul>
</p>
......@@ -284,9 +284,9 @@
<p class="text-black-50" align="justify" style="margin-top: 1rem;">The following composite parts
have been added to the Registry of Standard biological parts:
<ul>
<li>Apt4UTI C1: <a href="http://parts.igem.org/Part:BBa_K4449009">BBa_K40009</a></li>
<li>Apt4UTI C2: <a href="http://parts.igem.org/Part:BBa_K4449010">BBa_K40010</a></li>
<li>Apt4UTI C3: <a href="http://parts.igem.org/Part:BBa_K4449011">BBa_K40011</a></li>
<li>Apt4UTI C1: <a href="http://parts.igem.org/Part:BBa_K4449009">BBa_K4449009</a></li>
<li>Apt4UTI C2: <a href="http://parts.igem.org/Part:BBa_K4449010">BBa_K4449010</a></li>
<li>Apt4UTI C3: <a href="http://parts.igem.org/Part:BBa_K4449011">BBa_K4449011</a></li>
</ul>
</p>
</ol>
......@@ -375,8 +375,8 @@
<p class="text-black-50" align="justify" style="margin-top: 1rem; margin-bottom: 1rem;">
<ol>
<li><b>SDS PAGE:</b>After purification of the 6X -His tagged protein, we will perform an SDS
PAGE where we will run the molecular mass markers ( lane 1),Coomassie blue stained
cytoplasmic soluble fraction preparation( lane 2), the purified FimH1-6X His protein ( lane
PAGE where we will run the molecular mass markers - 98, 64, 50, 36, 30, 16, 6, kDa (lane 1),Coomassie blue stained
cytoplasmic soluble fraction preparation (lane 2), the purified FimH1-6X His protein ( lane
3) and the purified Staphylococcal Bap like Bhp protein-6X His (lane5 – negative
control))<sup>1</sup>. This will help us to validate our isolation and purification steps.
</li>
......@@ -472,7 +472,7 @@
<p class="text-black-50" align="justify" style="margin-top: 1rem; margin-bottom: 1rem;">
<ol>
<li><b>SDS PAGE:</b>After purificationof the 6X -His tagged protein, we will perform an SDS
PAGE where we will run the molecular mass markers (lane 1),Coomassie blue stained
PAGE where we will run the molecular mass markers - 98, 64, 50, 36, 30, 16, 6, kDa (lane 1),Coomassie blue stained
cytoplasmic soluble preparation(lane 2), the purified FimH2-6X His protein (lane 3) and the
purified Staphylococcal Bap like Bhp protein-6X His (lane5 – negative control).<sup>1</sup>.
This will help us to validate our isolation and purification steps.</li>
......@@ -534,7 +534,7 @@
<div class="img-property-slide">
<img src="https://static.igem.wiki/teams/4449/wiki/project/image5.png"
alt="Image" class="img-fluid">
<p align="justify">Figure -. Schematic illustration of ELISA-based
<p align="justify">Figure: Schematic illustration of ELISA-based
binding assay. His-tagged protein is incubated with biotin-labeled
anti-His antibody, which is immobilized to streptavidin coated
wells. After incubation of FITC labeled aptamers with protein coated
......@@ -574,7 +574,7 @@
a suitable methodology to test the functionality of our purified 6X His tagged Fim H.</p>
<p>We found that Team iGEM13_NYMU-Taipei devised a fluorescence based methodology to test the
functionality of the plac+RFP-FimH protein by expressing it as a fusion protein of RFP-FimH and
functionality of the pLac+RFP-FimH protein by expressing it as a fusion protein of RFP-FimH and
then checking the FimH binding to mannose. Later From our literature surveys
related to the testing of FimH protein, we have found another in vitro methodology that can
serve as a functionality check of purified FimH binding to mannose which used alpha-D
......
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