Difference between revisions of "Part:BBa K2719002:Design"
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<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> | ||
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===References=== | ===References=== | ||
+ | Harper S. & Speicher D. (2010). Purification of proteins fused to glutathione S-transferase. Protein Chromatography . Doi: 10.1007/978-1-60761-913-0_14. | ||
+ | Kim S., Thomas H, et. al. (2011). Advances in tenascin-C biology. doi: 10.1007/s00018-011-0783-6 |
Latest revision as of 03:13, 18 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)
""
Figure 3. Tenascin V- GST fusion protein 3D structure, modeled with Swiss-Model
- 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
References
Harper S. & Speicher D. (2010). Purification of proteins fused to glutathione S-transferase. Protein Chromatography . Doi: 10.1007/978-1-60761-913-0_14. Kim S., Thomas H, et. al. (2011). Advances in tenascin-C biology. doi: 10.1007/s00018-011-0783-6