Team:Tuebingen/Results/BioBricks

From 2014.igem.org

(Difference between revisions)
 
(9 intermediate revisions not shown)
Line 16: Line 16:
<ul>
<ul>
   <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483000">K1483000</a>: α-N-Acetylgalactosamindase
   <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483000">K1483000</a>: α-N-Acetylgalactosamindase
-
       <p>The α-N-acetylgalactosamindase is an enzyme from <i>Elizabethkingia meningoseptica</i> capable of cleaving off N-acetlygalactosamine from A-group blood antigens.</p></li>
+
       <p>The α-N-acetylgalactosamindase (NAGA) is an enzyme from <i>Elizabethkingia meningoseptica</i> capable of cleaving off N-acetlygalactosamine from A-group blood antigens (Figure 1).</p></li>
-
<img src="https://static.igem.org/mediawiki/2014/5/52/Tue2014_NAGA_Illustration.jpg" style="width: 70%">
+
<img src="https://static.igem.org/mediawiki/2014/5/52/Tue2014_NAGA_Illustration.jpg" style="width: 100%">
 +
<p id="picText">Figure 1: Schematic illustration of NAGA's enzymatic cleavage of A-group blood antigens while erythrocytes pass through a NAGA-coated clumn.</p>
   <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483001">K1483001</a>: Endo-β-Galactosidase
   <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483001">K1483001</a>: Endo-β-Galactosidase
-
       <p>The endo-β-galactosidase - also called EABase - is an enzyme from <i>Clostridium perfringens</i> which can cleave off galactose from the A- and B-group blood antigens which leaves behind a so called Oh antigen.</p></li>
+
       <p>The endo-β-galactosidase - also called EABase - is an enzyme from <i>Clostridium perfringens</i> which can cleave off trisaccharides from the A- and B-group blood antigens which leaves behind a precursor of the H-antigen (Figure 2).</p></li>
 +
 
 +
<img src="https://static.igem.org/mediawiki/2014/d/df/Tue2014_EABase_Illustration.jpg" style="width: 100%">
 +
<p id="picText">Figure 2: Schematic illustration of EABase's enzymatic cleavage of A- and B-group blood antigens while erythrocytes pass through a EABase-coated column. EABase leaves behind Oh antigens.</p>
   <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483002">K1483002</a>: α-Galactosidase
   <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483002">K1483002</a>: α-Galactosidase
-
       <p>This is an enzyme of <i>Bacteroides fragilis</i> which cleaves off B-group blood antigens from erythrocytes thereby creating H-antigens.</p></li>
+
       <p>This <i>Bacteroides fragilis</i> enzyme α-galactosidase (aGAL) cleaves off B-group blood antigens from erythrocytes thereby creating H-antigens (Figure 3).</p></li>
 +
 
 +
<img src="https://static.igem.org/mediawiki/2014/4/4e/Tue2014_aGal_Illustration.jpg" style="width: 100%">
 +
<p id="picText">Figure 3: Schematic illustration of aGAL's enzymatic cleavage of B-group blood antigens while erythrocytes pass through a aGAL-coated column.</p>
 +
 
 +
 
 +
  <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483003">K1483003</a>: <i>Ssp</i> GyrB Split Intein
 +
      <p>This protein naturally occurs in <i>Synechocystis sp.</i> PCC6803. The gyr B split intein is a bacterial intein with a 6 aminoacid long C-intein and a 150 aminoacid long N-intein and can be used e.g. to fuse two proteins (Figure 4).</p></li>
 +
 
 +
<img src="https://static.igem.org/mediawiki/2014/c/c7/Tue2014_Intein.jpg" style="width: 100%">
 +
<p id="picText">Figure 4: Schematic illustration of the interaction of N- and C-intein resulting in a covalent binding between the N- and C-intein-carrying substances (e.g. proteins).
-
  <li><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1483003">K1483003</a>: <a href="http://www.jbc.org/content/284/10/6194.short"><i>Ssp</i> GyrB Split Intein</a>
 
-
      <p>This protein naturally occurs in <i>Synechocystis sp.</i> PCC6803. The gyr B split intein is a bacterial intein with a 6 aminoacid long C-intein and a 150 aminoacid long N-intein and can be used to fuse two proteins.</p></li>
 
</ul>
</ul>

Latest revision as of 03:57, 18 October 2014


Shipped Parts

We are happy to announce that we have successfully created four BioBricks over the course of this summer! Among them is one intein BioBrick, the Ssp GyrB Split Intein which will surely be useful in many future projects.

  • K1483000: α-N-Acetylgalactosamindase

    The α-N-acetylgalactosamindase (NAGA) is an enzyme from Elizabethkingia meningoseptica capable of cleaving off N-acetlygalactosamine from A-group blood antigens (Figure 1).

  • Figure 1: Schematic illustration of NAGA's enzymatic cleavage of A-group blood antigens while erythrocytes pass through a NAGA-coated clumn.

  • K1483001: Endo-β-Galactosidase

    The endo-β-galactosidase - also called EABase - is an enzyme from Clostridium perfringens which can cleave off trisaccharides from the A- and B-group blood antigens which leaves behind a precursor of the H-antigen (Figure 2).

  • Figure 2: Schematic illustration of EABase's enzymatic cleavage of A- and B-group blood antigens while erythrocytes pass through a EABase-coated column. EABase leaves behind Oh antigens.

  • K1483002: α-Galactosidase

    This Bacteroides fragilis enzyme α-galactosidase (aGAL) cleaves off B-group blood antigens from erythrocytes thereby creating H-antigens (Figure 3).

  • Figure 3: Schematic illustration of aGAL's enzymatic cleavage of B-group blood antigens while erythrocytes pass through a aGAL-coated column.

  • K1483003: Ssp GyrB Split Intein

    This protein naturally occurs in Synechocystis sp. PCC6803. The gyr B split intein is a bacterial intein with a 6 aminoacid long C-intein and a 150 aminoacid long N-intein and can be used e.g. to fuse two proteins (Figure 4).

  • Figure 4: Schematic illustration of the interaction of N- and C-intein resulting in a covalent binding between the N- and C-intein-carrying substances (e.g. proteins).