Difference between revisions of "Part:BBa K4165070"
| (3 intermediate revisions by one other user not shown) | |||
| Line 4: | Line 4: | ||
This Part encodes the GST tag which serve as an enhancing tag and also serves in purification of expressed proteins in bacterial expression system. | 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=== | ===Usage and Biology=== | ||
| Line 9: | Line 10: | ||
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. | 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. | ||
| + | |||
<!-- --> | <!-- --> | ||
| − | <span class='h3bb'>Sequence and Features</span> | + | ===<span class='h3bb'>Sequence and Features</span>=== |
<partinfo>BBa_K4165070 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4165070 SequenceAndFeatures</partinfo> | ||
| + | |||
===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. | ||
Latest revision as of 13:38, 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
- 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 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.