Difference between revisions of "Part:BBa K4759018"
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| − | Recombinant protein expression plays an important role in promoting the development of modern biological technology. By using the host to achieve exogenous protein expression, it provides a powerful tool for studying the structure and function of some important proteins, especially the human source proteins. In order to enable subsequent structure-function studies, the obtained recombinant proteins must be soluble, stable, properly folded as well as biologically active. However, in practical studies, these often become obstacles to obtaining an ideal recombinant protein. The solubility of the recombinant protein expression became the primary addressed problem. | + | Recombinant protein expression plays an important role in promoting the development of modern biological technology. By using the host to achieve exogenous protein expression, it provides a powerful tool for studying the structure and function of some important proteins, especially the human source proteins. In order to enable subsequent structure-function studies, the obtained recombinant proteins must be soluble, stable, properly folded as well as biologically active. However, in practical studies, these often become obstacles to obtaining an ideal recombinant protein. The solubility of the recombinant protein expression became the primary addressed problem.The most prominent advantage of GST is its ability to generate affinity with fixed glutathione, elute under non-denaturing conditions of 10 mmol/L reduced glutathione, finally achieving the purpose of affinity purification. GST has another beneficial effect on recombinant proteins, which is to reduce degradation from inside the host and increase protein stability. However, some reports show that the soluble effect of GST is not very obvious. |
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Latest revision as of 14:42, 2 October 2023
GST
Recombinant protein expression plays an important role in promoting the development of modern biological technology. By using the host to achieve exogenous protein expression, it provides a powerful tool for studying the structure and function of some important proteins, especially the human source proteins. In order to enable subsequent structure-function studies, the obtained recombinant proteins must be soluble, stable, properly folded as well as biologically active. However, in practical studies, these often become obstacles to obtaining an ideal recombinant protein. The solubility of the recombinant protein expression became the primary addressed problem.The most prominent advantage of GST is its ability to generate affinity with fixed glutathione, elute under non-denaturing conditions of 10 mmol/L reduced glutathione, finally achieving the purpose of affinity purification. GST has another beneficial effect on recombinant proteins, which is to reduce degradation from inside the host and increase protein stability. However, some reports show that the soluble effect of GST is not very obvious.
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