Team:Tuebingen/Results/BioBricks
From 2014.igem.org
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<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 | + | <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%"> | <img src="https://static.igem.org/mediawiki/2014/d/df/Tue2014_EABase_Illustration.jpg" style="width: 100%"> | ||
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<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 <i>Bacteroides fragilis</i> enzyme α-galactosidase (aGAL) 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%"> | <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 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>: | + | <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 to fuse two proteins.</p></li> | + | <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). | ||
+ | |||
</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).
- 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).
- K1483002: α-Galactosidase
This Bacteroides fragilis enzyme α-galactosidase (aGAL) cleaves off B-group blood antigens from erythrocytes thereby creating H-antigens (Figure 3).
- 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 1: Schematic illustration of NAGA's enzymatic cleavage of A-group blood antigens while erythrocytes pass through a NAGA-coated clumn.
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.
Figure 3: Schematic illustration of aGAL's enzymatic cleavage of B-group blood antigens while erythrocytes pass through a aGAL-coated column.
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).