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basic_parts.html
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<h2 align="center">BASIC PARTS</h2>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Bacterial Chitinase Combo 1 ( BBa_K3979004)</b></p>
<p class="pl-20 pr-20" >This is a recombinant chitinase gene designed using the catalytic domain(CD) of ChiB from <i>Pseudoalteromonas sp.</i> DL-6 and the chitin-binding domain (CBD) of ChiB from <i>Serratia marcescens</i>. CD-CBD forms the basic chitinase gene framework. The protein sequence is codon-optimized for E.coli expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
</p>
<div class="image-block, text-center">
<img src="assets/img/parts/bc1_map.png" alt="sample image" class="img-fluid">
</div>
<br><br>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Bacterial Chitinase Combo 2 (BBa_K3979003)
</b></p>
<p class="pl-20 pr-20" >This is a recombinant chitinase gene designed using the catalytic domain(CD) of chitinase from <i>Amycolatopsis orientalis</i> and the chitin-binding domain (CBD) of ChiB from <i>Serratia marcescens</i>. CD-CBD forms the basic chitinase gene framework. The protein sequence is codon-optimized for <i>E.coli</i> expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
</p>
<div class="image-block, text-center">
<img src="assets/img/parts/bc2_map.png" alt="sample image" class="img-fluid">
</div>
<br><br>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Plant Chitinase Combo 1 (BBa_K3979007)
</b></p>
<p class="pl-20 pr-20" >This is a recombinant chitinase gene designed using the catalytic domain (CD) of <i>Triticum aestivum</i> cultivar Sumai 3 and the chitin-binding domain (CBD) of <i>Hordeum vulgare</i> cultivar NK1558. The sequences of both barley and wheat chitinases are joined using common (GGGS)<sub>3</sub> linkers. Barley CBD is added to the C-terminal of the combination. The protein sequence is codon-optimized for <i>E.coli</i> expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
</p>
<div class="image-block, text-center">
<img src="assets/img/parts/pc1_map.png" alt="sample image" class="img-fluid">
</div>
<br><br>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Plant Chitinase Combo 2 (BBa_K3979008)
</b></p>
<p class="pl-20 pr-20" >This is a recombinant chitinase gene designed using the catalytic domain (CD) of <i>Triticum aestivum</i> cultivar Sumai 3 and the chitin-binding domain (CBD) of <i>Hordeum vulgare</i> cultivar NK1558. The chimeric chitinase consists of a wheat catalytic domain flanked by two barley chitin-binding domains. The protein sequence is codon-optimized for E.coli expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
</p>
<div class="image-block, text-center">
<img src="assets/img/parts/pc2_map.png" alt="sample image" class="img-fluid">
</div>
<br><br>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Chitinase B from <i>Serratia marcescens</i> QMB1466 (BBa_K3979009)
</b></p>
<p class="pl-20 pr-20" >Chitinase B from <i>Serratia marcescens</i> QMB1466 is a hydrolyzing enzyme that can hydrolyze insoluble chitin to its oligo and monomeric components: N-Acetylglucosamine. The molecular size and weight of the protein are 55.46438 kDa and 1524 base pairs. The protein sequence is codon-optimized for <i>E.coli</i> expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
</p>
<div class="image-block, text-center">
<img src="assets/img/parts/sr_map.png" alt="sample image" class="img-fluid">
</div>
<br><br>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Chitinase A from <i>Amycolatopsis orientalis</i> (BBa_K3979010)
</b></p>
<p class="pl-20 pr-20" >Chitinase A (ChiA) from <i>Amycolatopsis orientalis</i> strain B-37 is a hydrolyzing enzyme that can hydrolyze insoluble chitin to its oligo and monomeric components: N-Acetylglucosamine. The molecular size and weight of the protein are 33.13 kDa and 975 base pairs. The protein sequence is codon-optimized for <i>E.coli</i> expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
</p>
<div class="image-block, text-center">
<img src="assets/img/parts/st_map.png" alt="sample image" class="img-fluid">
</div>
<br><br>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Chitinase II precursor from <i>Triticum aestivum</i> (BBa_K3979005)
</b></p>
<p class="pl-20 pr-20" >Chitinase II precursor derived from <i>Triticum aestivum</i> cultivar Sumai 3 is a hydrolyzing enzyme that can hydrolyze insoluble chitin to its oligo and monomeric components: N-Acetylglucosamine. The molecular size and weight of the protein are 24.73 kDa and 719 base pairs. The protein sequence is codon-optimized for <i>E.coli</i> expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
</p>
<div class="image-block, text-center">
<img src="assets/img/parts/wht_map.png" alt="sample image" class="img-fluid">
</div>
<br>
<br>
<p class="pl-20 pr-20" align="center" style="font-size:25px"><b>Endochitinase 1 from <i>Hordeum vulgare</i> (BBa_K379006)
</b></p>
<p class="pl-20 pr-20" >Endochitinase 1 derived from <i>Hordeum vulgare</i> cultivar NK1558 is a hydrolyzing enzyme that can hydrolyze insoluble chitin to its oligo and monomeric components: N-Acetylglucosamine. The molecular size and weight of the protein are 33.40 kDa and 981 base pairs. The protein sequence is codon-optimized for E.coli expression. BamHI and HindIII sites were added at the 5’ and 3’ end of the gene, respectively.
<div class="image-block, text-center">
<img src="assets/img/parts/br_map.png" alt="sample image" class="img-fluid">
</div>
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<!--<p class="text-center">The sequences that we created are codon-optimized in order to clone and express them in <i>E. coli</i>.</p>-->
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