Difference between revisions of "Part:BBa K2719002:Design"
Line 2: | Line 2: | ||
__NOTOC__ | __NOTOC__ | ||
<partinfo>BBa_K2719002 short</partinfo> | <partinfo>BBa_K2719002 short</partinfo> | ||
+ | <p>The fusion of this protein is important for give tenascin a higher level of stability, improve its solubility (thus favoring its presence on the aqueous phase) and simplify the purification of this part, because GST could be useful for a affinity purification. The sequence of GST and Tenascin 5 domain V was optimized for expression on <i>E.coli</i> BL21 (DE3) and were fused without polylinker. (Figure 1)<p> | ||
+ | "https://static.igem.org/mediawiki/2018/1/10/T--TecCEM--TCD5%2BGST3DStructure.png" | ||
+ | <p><i>Figure 3.</i> Tenascin V- GST fusion protein 3D structure, modeled with Swiss-Model</p> | ||
<partinfo>BBa_K2719002 SequenceAndFeatures</partinfo> | <partinfo>BBa_K2719002 SequenceAndFeatures</partinfo> |
Revision as of 11:07, 17 October 2018
GST+Tenascin Domain V
The fusion of this protein is important for give tenascin a higher level of stability, improve its solubility (thus favoring its presence on the aqueous phase) and simplify the purification of this part, because GST could be useful for a affinity purification. The sequence of GST and Tenascin 5 domain V was optimized for expression on E.coli BL21 (DE3) and were fused without polylinker. (Figure 1)<p> "" <p>Figure 3. Tenascin V- GST fusion protein 3D structure, modeled with Swiss-Model
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 346
Design Notes
Optimized for E.coli BL21.
Source
Synthetically designed