Difference between revisions of "Team:Stanford-Brown/Parts"

(Undo revision 403111 by Daniel.kunin (talk))
 
(3 intermediate revisions by the same user not shown)
Line 65: Line 65:
 
       <div class="col-sm-6">
 
       <div class="col-sm-6">
 
         <a href="http://parts.igem.org/Part:BBa_K1692004" class="btn" id="be1" target="_blank">
 
         <a href="http://parts.igem.org/Part:BBa_K1692004" class="btn" id="be1" target="_blank">
           <img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="30"><h4> Biobrick: BBa_K1692004</h4>
+
           <h4> Biobrick: BBa_K1692004</h4><img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="35">
 
           <p><b>Codon-optimized PAL with T7 promoter and FLAG tag</b> Phenylalanine ammonia lyase (PAL) catalyzes the conversion of L-phenylalanine to trans-cinnamic acid. Our PAL construct is codon-optimized for expression in E. coli. The original sequence is derived from Anabaena variabilis. We chose the A. variabilis variant of PAL because the literature has characterized it as functioning well, in contrast to University of British Columbia’s 2013 PAL biobrick part (BBa_K1129003) from Streptomyces maritimus, which has much lower activity.  Our construct includes the PAL coding sequence, a T7 inducible promoter, a ribosome binding site, and a FLAG-tag peptide sequence for easy and efficient protein purification. We have sequenced our construct and verified that all these components are indeed present.
 
           <p><b>Codon-optimized PAL with T7 promoter and FLAG tag</b> Phenylalanine ammonia lyase (PAL) catalyzes the conversion of L-phenylalanine to trans-cinnamic acid. Our PAL construct is codon-optimized for expression in E. coli. The original sequence is derived from Anabaena variabilis. We chose the A. variabilis variant of PAL because the literature has characterized it as functioning well, in contrast to University of British Columbia’s 2013 PAL biobrick part (BBa_K1129003) from Streptomyces maritimus, which has much lower activity.  Our construct includes the PAL coding sequence, a T7 inducible promoter, a ribosome binding site, and a FLAG-tag peptide sequence for easy and efficient protein purification. We have sequenced our construct and verified that all these components are indeed present.
 
</p>
 
</p>
Line 90: Line 90:
 
<div class="col-sm-6">
 
<div class="col-sm-6">
 
         <a href="http://parts.igem.org/Part:BBa_K1692007" class="btn" id="be1" target="_blank">
 
         <a href="http://parts.igem.org/Part:BBa_K1692007" class="btn" id="be1" target="_blank">
           <img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="30"><h4> Biobrick: BBa_K1692007</h4>
+
           <h4> Biobrick: BBa_K1692007</h4><img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="35">
 
           <p><b>UbiX with T7 promoter and FLAG tag</b> UbiX is a flavin prenyltransferase that normally plays a role in ubiquinone biosynthesis in E. coli. UbiX transfers a prenyl group from dimethylallyl monophosphate (DMAP) to flavin mononucleotide (FMN), thereby creating a cofactor that happens to be essential to the functionality of FDC. Our genetic construct includes the UbiX coding sequence, a T7 inducible promoter, a ribosome binding site, and a FLAG-tag peptide sequence for easy and efficient protein purification. We have sequenced our construct and verified that all these components are indeed present.</p>
 
           <p><b>UbiX with T7 promoter and FLAG tag</b> UbiX is a flavin prenyltransferase that normally plays a role in ubiquinone biosynthesis in E. coli. UbiX transfers a prenyl group from dimethylallyl monophosphate (DMAP) to flavin mononucleotide (FMN), thereby creating a cofactor that happens to be essential to the functionality of FDC. Our genetic construct includes the UbiX coding sequence, a T7 inducible promoter, a ribosome binding site, and a FLAG-tag peptide sequence for easy and efficient protein purification. We have sequenced our construct and verified that all these components are indeed present.</p>
 
         </a>
 
         </a>
Line 97: Line 97:
 
       <div class="col-sm-6">
 
       <div class="col-sm-6">
 
         <a href="http://parts.igem.org/Part:BBa_K1692008" class="btn" id="be1" target="_blank">
 
         <a href="http://parts.igem.org/Part:BBa_K1692008" class="btn" id="be1" target="_blank">
           <img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="30"><h4> Biobrick: BBa_K1692008</h4>
+
           <h4> Biobrick: BBa_K1692008</h4><img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="35">
 
           <p><b>Styrene Synthesis Operon</b> This operon is a composite of three enzymes in the following order: FDC, UbiX, and PAL.  PAL converts phenylalanine to cinnamic acid.  FDC converts cinnamic acid to styrene.  UbiX modifies flavin mononucleotide to produce a cofactor that is required for FDC activity. The entire operon is controlled via an inducible T7 promoter. Each protein-coding sequence is preceded by a ribosome binding site and followed by a FLAG-tag peptide, enabling easy and efficient extraction.
 
           <p><b>Styrene Synthesis Operon</b> This operon is a composite of three enzymes in the following order: FDC, UbiX, and PAL.  PAL converts phenylalanine to cinnamic acid.  FDC converts cinnamic acid to styrene.  UbiX modifies flavin mononucleotide to produce a cofactor that is required for FDC activity. The entire operon is controlled via an inducible T7 promoter. Each protein-coding sequence is preceded by a ribosome binding site and followed by a FLAG-tag peptide, enabling easy and efficient extraction.
 
</p>
 
</p>
Line 119: Line 119:
 
       <div class="col-sm-6">
 
       <div class="col-sm-6">
 
         <a href="http://parts.igem.org/Part:BBa_K1692034" class="btn" id="be1" target="_blank">
 
         <a href="http://parts.igem.org/Part:BBa_K1692034" class="btn" id="be1" target="_blank">
           <h4>Biobrick: BBa_K1692034</h4>
+
           <h4>Biobrick: BBa_K1692034</h4><img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="35">
 
           <p><b>Pank + hybrid phaCAB + lysis</b> Construct that was cloned to have P(3HB) producing <i>E. coli</i> cells lyse when induced with Arabinose. This would greatly facilitate P(3HB) extraction. We are currently still testing and characterizing this part.  </p>
 
           <p><b>Pank + hybrid phaCAB + lysis</b> Construct that was cloned to have P(3HB) producing <i>E. coli</i> cells lyse when induced with Arabinose. This would greatly facilitate P(3HB) extraction. We are currently still testing and characterizing this part.  </p>
 
         </a>
 
         </a>
Line 176: Line 176:
 
       <div class="col-sm-6">
 
       <div class="col-sm-6">
 
         <a href="http://parts.igem.org/Part:BBa_K1692033" class="btn" id="be1" target="_blank">
 
         <a href="http://parts.igem.org/Part:BBa_K1692033" class="btn" id="be1" target="_blank">
           <h4>Biobrick : BBa_K1692033</h4>
+
           <h4>Biobrick : BBa_K1692033</h4><img src="https://static.igem.org/mediawiki/2015/6/6a/SB2015_CraneLogoBlue.png" class="pull-left img-rounded img-responsive" width="35">
 
           <p><b>RFP gDNA</b> This gene provides the intermediate for synthesizing gRNA targeting RFP (BBa_J04450). When used in conjuction with the CRISPR/Cas system, this gRNA will bind to and digest the RFP plasmid. </p>
 
           <p><b>RFP gDNA</b> This gene provides the intermediate for synthesizing gRNA targeting RFP (BBa_J04450). When used in conjuction with the CRISPR/Cas system, this gRNA will bind to and digest the RFP plasmid. </p>
 
         </a>
 
         </a>

Latest revision as of 03:19, 19 September 2015

Biobricks

Our Biobricks

Polystyrene Synthesis BioBricks

P(3HB) Synthesis BioBricks

BioHYDRA BioBricks

Cellulose Sheets BioBricks

CRATER Briobricks


Copyright © 2015 Stanford-Brown iGEM Team