Difference between revisions of "Part:BBa K2719002:Design"

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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.
 
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)

"T--TecCEM--TCD5%2BGST3DStructure.png"

Figure 3. Tenascin V- GST fusion protein 3D structure, modeled with Swiss-Model


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE 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