Difference between revisions of "Part:BBa K2719000"

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<partinfo>BBa_K2719000 short</partinfo>
 
<partinfo>BBa_K2719000 short</partinfo>
  
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Glutathione S-transferase (GST) is a peptide derived from Schistosoma japonicum, in which a target protein may be fused on the N-terminal. This fusion allows the purification of the target protein using glutathione affinity and maximize the presence of the protein in soluble state, rather than on inclusion bodies. In addition, this fusion protein gives stability to the domine of Tenascin V and for this is necessary to use a polyproline linker to maintain the original three dimensional structure of the protein.This tag may be later removed by adding a protease recognition site between GST and the target protein (Harper & Speicher, 2013).
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Glutathione S-transferase (GST) is a peptide derived from <i>Schistosoma japonicum</i>, in which a target protein may be fused on the N-terminal. This fusion allows the purification of the target protein using glutathione affinity and maximize the presence of the protein in soluble state, rather than on inclusion bodies. In addition, this fusion protein gives stability to the domain of Tenascin V and for this is necessary to use a polyproline linker to maintain the original three dimensional structure of the protein. This tag may be later removed by adding a protease recognition site between GST and the target protein (Harper & Speicher, 2013).
  
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===Usage and Biology===
  
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===Usage and Biology===
 
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Tertiary structure of GST
 
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The tertiary structure was modeled using Swiss-Model, the results are shown on <i>figure 1.</i>
 
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"http://2018.igem.org/File:T--TecCEM--TCD53DStructure.png"
 
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[[Image:TCD53DStructure.png|300px]]
 
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<i>Figure 1.</i> GST 3D structure, modelled with Swiss-Model
 
  
  

Latest revision as of 11:05, 17 October 2018


GST

Glutathione S-transferase (GST) is a peptide derived from Schistosoma japonicum, in which a target protein may be fused on the N-terminal. This fusion allows the purification of the target protein using glutathione affinity and maximize the presence of the protein in soluble state, rather than on inclusion bodies. In addition, this fusion protein gives stability to the domain of Tenascin V and for this is necessary to use a polyproline linker to maintain the original three dimensional structure of the protein. This tag may be later removed by adding a protease recognition site between GST and the target protein (Harper & Speicher, 2013).

Usage and Biology

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