Difference between revisions of "Part:BBa K1182425:Design"
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===Design Notes=== | ===Design Notes=== | ||
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| + | This is an alpha fragment of beta galactosidase split enzyme. The enzyme beta galactosidase is expressed separately into two fragment, the alpha and omega fragment. When the alpha and omega fragment meets they will exhibit an enzymatic activity similar to the full length expressed beta galactosidase enzyme. | ||
| + | This split reporter can be used as biosensor using ternary complexation mediated protein complementation principle where the interaction of two proteins (in this case the alpha and omega fragment) is mediated by another protein. | ||
===Source=== | ===Source=== | ||
| − | + | The part is fragment of E.coli LacZ gene, acquired by PCR. | |
===References=== | ===References=== | ||
Latest revision as of 19:38, 30 September 2013
Split β-galactosidase - α fragment
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
This is an alpha fragment of beta galactosidase split enzyme. The enzyme beta galactosidase is expressed separately into two fragment, the alpha and omega fragment. When the alpha and omega fragment meets they will exhibit an enzymatic activity similar to the full length expressed beta galactosidase enzyme.
This split reporter can be used as biosensor using ternary complexation mediated protein complementation principle where the interaction of two proteins (in this case the alpha and omega fragment) is mediated by another protein.
Source
The part is fragment of E.coli LacZ gene, acquired by PCR.
References
Stains, C.I., et al. (2010). A General Approach for Receptor and Antibody-Targeted Detection of Native Proteins utilizing Split-Luciferase Reassembly. ACS Chem Biol. 5(10): 943–952. doi:10.1021/cb100143m.
Broome, A.M., et al. (2010). Expanding the utility of Beta-galactosidase complementation: pieceby piece. Mol Pharm. 7(1): 60–74. doi:10.1021/mp900188e.