Difference between revisions of "Part:BBa K339000:Design"
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===Design Notes=== | ===Design Notes=== | ||
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===Source=== | ===Source=== | ||
− | + | Plasmid DNA was obtained from Jean-Betton labs in France (Betton et al., 2002). | |
===References=== | ===References=== | ||
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+ | Betton, J., Phichith, D. and Hunke, S. (2002). Folding and aggregation of export-defective mutants of the maltose-binding protein. ''Research in Microbiology''. (153): 399-404. | ||
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+ | Kapust, R. and Waugh, D. (1999). ''Escherichia coli'' maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. ''Protein Science''. 8(8):1688-1674. | ||
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+ | ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201, USA. |
Latest revision as of 23:31, 30 October 2010
Maltose Binding Protein (malE)
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 435
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 133
Design Notes
Source
Plasmid DNA was obtained from Jean-Betton labs in France (Betton et al., 2002).
References
Betton, J., Phichith, D. and Hunke, S. (2002). Folding and aggregation of export-defective mutants of the maltose-binding protein. Research in Microbiology. (153): 399-404.
Kapust, R. and Waugh, D. (1999). Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Science. 8(8):1688-1674.
ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201, USA.