Difference between revisions of "Part:BBa K936020"
Ckdeniston (Talk | contribs) |
|||
| Line 3: | Line 3: | ||
Full Cutinase Construct on psB1A3 backbone. <br> | Full Cutinase Construct on psB1A3 backbone. <br> | ||
| + | |||
| + | Through p-nitrophenyl butyrate (pNPB) assays, the UC Davis team gathered enough data to determine that the LC-Cutinase part (BBa_K936000) incorporated in this part most likely exhibits its intended function as an esterase. A detailed description of these assays can be found on the Module Engineering Project page: http://2012.igem.org/Team:UC_Davis/Project/Catalyst. | ||
| + | <br>Additionally, the following data is further described on the UC Davis Cutinase Activity data page: http://2012.igem.org/Team:UC_Davis/Data/Cutinase_Activity | ||
| + | |||
https://static.igem.org/mediawiki/2012/a/aa/UC_Davis_First_pNPB_Run.png <br>(Above Graph) Results of pNPB assay detailing the constitutive construct as having the highest esterase activity.https://static.igem.org/mediawiki/2012/6/62/UC_Davis_Third_pNPB_Run.png<br>(Above Graphs) The graphs above detail higher activity among the constitutive construct and some mutant variants in esterase activity compared to the control and wild type per unit cell. <br>https://static.igem.org/mediawiki/2012/5/59/UC_Davis_Last_pNPB_Run.png<br> (Above graph) This graph represents a possible production of cutinase by the cells upon entering stationary phase.<br><br> | https://static.igem.org/mediawiki/2012/a/aa/UC_Davis_First_pNPB_Run.png <br>(Above Graph) Results of pNPB assay detailing the constitutive construct as having the highest esterase activity.https://static.igem.org/mediawiki/2012/6/62/UC_Davis_Third_pNPB_Run.png<br>(Above Graphs) The graphs above detail higher activity among the constitutive construct and some mutant variants in esterase activity compared to the control and wild type per unit cell. <br>https://static.igem.org/mediawiki/2012/5/59/UC_Davis_Last_pNPB_Run.png<br> (Above graph) This graph represents a possible production of cutinase by the cells upon entering stationary phase.<br><br> | ||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
Revision as of 03:37, 4 October 2012
K206000+B0034+pelB+Cutinase+Polyhistidine Tag
Full Cutinase Construct on psB1A3 backbone.
Through p-nitrophenyl butyrate (pNPB) assays, the UC Davis team gathered enough data to determine that the LC-Cutinase part (BBa_K936000) incorporated in this part most likely exhibits its intended function as an esterase. A detailed description of these assays can be found on the Module Engineering Project page: http://2012.igem.org/Team:UC_Davis/Project/Catalyst.
Additionally, the following data is further described on the UC Davis Cutinase Activity data page: http://2012.igem.org/Team:UC_Davis/Data/Cutinase_Activity
(Above Graph) Results of pNPB assay detailing the constitutive construct as having the highest esterase activity.
(Above Graphs) The graphs above detail higher activity among the constitutive construct and some mutant variants in esterase activity compared to the control and wild type per unit cell. 
(Above graph) This graph represents a possible production of cutinase by the cells upon entering stationary phase.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 125
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 65
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 210
Illegal AgeI site found at 822 - 1000COMPATIBLE WITH RFC[1000]