Difference between revisions of "Part:BBa K2692000:Design"
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===Design Notes=== | ===Design Notes=== | ||
− | The hexahistidine tag has the ability to also bind to metals (this is why is is able to bind to a nickle column). To gain accurate results, the his tag would have to be removed to ensure that the cutA protein is binding the copper. | + | The hexahistidine tag has the ability to also bind to metals (this is why is is able to bind to a nickle column). To gain accurate results, the his tag would have to be removed to ensure that the cutA protein is binding the copper and not the tag itself. |
===Source=== | ===Source=== | ||
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===References=== | ===References=== | ||
+ | [1] Zhao, Y., Wang, Y., Hu, J., Zhang, X., and Zhang, Y. (2012) CutA divalent cation tolerance homolog (Escherichia coli) (CUTA) regulates beta-cleavage of beta-amyloid precursor protein (APP) through interacting with beta-site APP cleaving protein 1 (BACE1). Journal of Biological Chemistry 287, 11141-11150 |
Latest revision as of 03:21, 11 October 2018
CutA metal binding protein from E.coli
Assembly Compatibility:
- 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
The hexahistidine tag has the ability to also bind to metals (this is why is is able to bind to a nickle column). To gain accurate results, the his tag would have to be removed to ensure that the cutA protein is binding the copper and not the tag itself.
Source
The part (in plasmid) was a gift from the Weiden lab at the University of Lethbridge and is originally a plasmid from the ASKA database.
References
[1] Zhao, Y., Wang, Y., Hu, J., Zhang, X., and Zhang, Y. (2012) CutA divalent cation tolerance homolog (Escherichia coli) (CUTA) regulates beta-cleavage of beta-amyloid precursor protein (APP) through interacting with beta-site APP cleaving protein 1 (BACE1). Journal of Biological Chemistry 287, 11141-11150