Difference between revisions of "Part:BBa K4165070"
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===References===
 
===References===
 
1- Harper, S., & Speicher, D. W. (2011). Purification of proteins fused to glutathione S-tranferase. Methods in molecular biology (Clifton, N.J.), 681, 259. https://doi.org/10.1007/978-1-60761-913-0_14.
 
1- Harper, S., & Speicher, D. W. (2011). Purification of proteins fused to glutathione S-tranferase. Methods in molecular biology (Clifton, N.J.), 681, 259. https://doi.org/10.1007/978-1-60761-913-0_14.

Revision as of 10:33, 10 October 2022


Glutathione S-Transferase

This Part encodes the GST tag which serve as an enhancing tag and also serves in purification of expressed proteins in bacterial expression system.

Usage and Biology

Glutathione S-transferase (GST), used for affinity purification when fused to a gene of interest [1]. Glutathione-agarose affinity chromatography provides the quick, delicate, non-denaturing, and very selective purification of glutathione-binding sequence-containing proteins, such as Glutathione S-Transferase (GST), glutathione peroxidase, and glyoxalase.

In our case, we also used GST to enhance the stability and expression yield of our protein pair DocS and Coh2, so we fused them once with GST and once with His tag to determine which one will give more yield and stability.

Sequence and Features


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 SapI.rc site found at 85


References

1- Harper, S., & Speicher, D. W. (2011). Purification of proteins fused to glutathione S-tranferase. Methods in molecular biology (Clifton, N.J.), 681, 259. https://doi.org/10.1007/978-1-60761-913-0_14.