Difference between revisions of "Part:BBa K1896012"
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<partinfo>BBa_K1896012 short</partinfo> | <partinfo>BBa_K1896012 short</partinfo> | ||
| − | + | This part was designed to express the Streptavidin molecule on the cell surface of ''E. coli''. Protein fusion containing the INP<sub>NC</sub> membrane domain have been described to be directed to the outer cell membrane [1], but it appears that the tetrameric nature of Streptavidin makes the resulting protein toxic to the cell, as no correct colonies could be obtained after multiple attempts. | |
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<partinfo>BBa_K1896012 SequenceAndFeatures</partinfo> | <partinfo>BBa_K1896012 SequenceAndFeatures</partinfo> | ||
| + | ===References=== | ||
| + | <ol> | ||
| + | <li>Wu, P. H., Giridhar, R., & Wu, W. T. (2006). Surface display of transglucosidase on Escherichia coli by using the ice nucleation protein of Xanthomonas campestris and its application in glucosylation of hydroquinone. ''Biotechnology and bioengineering'', 95(6), 1138-1147.</li> | ||
| + | </ol> | ||
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Revision as of 13:18, 19 October 2016
INP_NC-streptavidin generator
This part was designed to express the Streptavidin molecule on the cell surface of E. coli. Protein fusion containing the INPNC membrane domain have been described to be directed to the outer cell membrane [1], but it appears that the tetrameric nature of Streptavidin makes the resulting protein toxic to the cell, as no correct colonies could be obtained after multiple attempts.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 7
Illegal NheI site found at 30 - 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 466
Illegal AgeI site found at 1082
Illegal AgeI site found at 1133 - 1000COMPATIBLE WITH RFC[1000]
References
- Wu, P. H., Giridhar, R., & Wu, W. T. (2006). Surface display of transglucosidase on Escherichia coli by using the ice nucleation protein of Xanthomonas campestris and its application in glucosylation of hydroquinone. Biotechnology and bioengineering, 95(6), 1138-1147.