Difference between revisions of "Part:BBa K2333435"

Revision as of 20:37, 29 October 2017

pBad mf-Lon

This is an arabinose-inducible mf-Lon construct containing the pBad promoter. William and Mary 2017 has modified the mf-Lon gene via codon-optimization for iGEM use and added a double terminator.

Usage and Biology

This contains mf-Lon under the control of the inducible pBad promoter. The mf-Lon protease specifically targets different protein degradation tags with varying affinities corresponding to varying degradation rates. This arabinose-inducible mf-Lon construct can be used in tandem with aTc-inducible pdt reporter constructs to obtain gene expression speed measurements.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
INCOMPATIBLE WITH RFC[12]
Illegal NheI site found at 1245
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 1184
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 1019
Illegal AgeI site found at 3102
Illegal AgeI site found at 3186
Illegal AgeI site found at 3392
Illegal AgeI site found at 3417
1000
INCOMPATIBLE WITH RFC[1000]
Illegal SapI site found at 1001

@@ Line 7: / Line 7: @@
 ===Usage and Biology===
-This composite part is a combination circuit with the LacI repressor under the constitutive promoter J23105 and mf-Lon under the control of the inducible pBad promoter. The mf-Lon protease specifically targets different protein degradation tags with varying affinities corresponding to varying degradation rates. This arabinose-inducible mf-Lon construct can be used in tandem with aTc-inducible pdt reporter constructs to obtain gene expression speed measurements.
+This contains mf-Lon under the control of the inducible pBad promoter. The mf-Lon protease specifically targets different protein degradation tags with varying affinities corresponding to varying degradation rates. This arabinose-inducible mf-Lon construct can be used in tandem with aTc-inducible pdt reporter constructs to obtain gene expression speed measurements.
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