Difference between revisions of "Part:BBa K2692000:Design"

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===References===
 
===References===
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[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
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[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

Revision as of 03:17, 11 October 2018


CutA metal binding protein from E.coli


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE 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. The coding sequence is codon optimized for efficient expression in E.coli .

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