Difference between revisions of "Part:BBa K2382004"

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===Usage and Biology===
 
===Usage and Biology===
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This part previously functioned as a DNA recombination and repair protein
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This part previously functioned as a DNA recombination and repair protein in E. coli. <br>
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in E. coli. It is also found that Thioredoxin is capable of increasing the
+
Thioredoxin can facilitate protein folding. And this par has its potential of being used in a fusion protein design.<br>
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solubility of our protein, MSMEG5998. Therefore, we create this part for
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It is also found that Thioredoxin is capable of increasing enzyme activity of our protein, MSMEG5998(BBa_K2382001).
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future igem teams who want to make their protein more soluble when
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We designed a polylinker that has multiple restriction cutting sites at the end of this part for
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facing inclusion bodies in E. coli.
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future iGEM teams who want to make their protein more effective.
  
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===Characterization of the Thioredoxin with polylinker===
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[[File:Csmuxnchu description fig1.png|center|thumb|600px|''<b>BBa_K2382004 showed the gene design of the Thioredoxin fusion system construction.</b> ]]
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==Characterization of the Thioredoxin with polylinker==
  
 
===References===
 
===References===
 
Carsten Berndt, Christopher Horst Lillig, Arne Holmgren, Thioredoxins and glutaredoxins as facilitators of protein folding, In Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Volume 1783, Issue 4, 2008, Pages 641-650, ISSN 0167-4889, https://doi.org/10.1016/j.bbamcr.2008.02.003.
 
Carsten Berndt, Christopher Horst Lillig, Arne Holmgren, Thioredoxins and glutaredoxins as facilitators of protein folding, In Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Volume 1783, Issue 4, 2008, Pages 641-650, ISSN 0167-4889, https://doi.org/10.1016/j.bbamcr.2008.02.003.
 
(http://www.sciencedirect.com/science/article/pii/S0167488908000700)
 
(http://www.sciencedirect.com/science/article/pii/S0167488908000700)
 +
 +
Edward R. LaVallie1, Elizabeth A. DiBlasio1, Sharlotte Kovacic1, Kathleen L. Grant1, Paul F. Schendel1 & John M. McCoy1. A Thioredoxin Gene Fusion Expression System That Circumvents Inclusion Body Formation in the E. coli Cytoplasm. Nature Biotechnology 11, 187 - 193 (1993)
 +
doi:10.1038/nbt0293-187
  
 
Escherichia coli str. K-12 substr. MG1655 https://www.ncbi.nlm.nih.gov/nuccore/NC_000913.3
 
Escherichia coli str. K-12 substr. MG1655 https://www.ncbi.nlm.nih.gov/nuccore/NC_000913.3

Latest revision as of 21:51, 1 November 2017

Thioredoxin with polylinker


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 367
    Illegal XhoI site found at 373
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



Usage and Biology

This part previously functioned as a DNA recombination and repair protein in E. coli.
Thioredoxin can facilitate protein folding. And this par has its potential of being used in a fusion protein design.
It is also found that Thioredoxin is capable of increasing enzyme activity of our protein, MSMEG5998(BBa_K2382001). We designed a polylinker that has multiple restriction cutting sites at the end of this part for future iGEM teams who want to make their protein more effective.

BBa_K2382004 showed the gene design of the Thioredoxin fusion system construction.

Characterization of the Thioredoxin with polylinker

References

Carsten Berndt, Christopher Horst Lillig, Arne Holmgren, Thioredoxins and glutaredoxins as facilitators of protein folding, In Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Volume 1783, Issue 4, 2008, Pages 641-650, ISSN 0167-4889, https://doi.org/10.1016/j.bbamcr.2008.02.003. (http://www.sciencedirect.com/science/article/pii/S0167488908000700)

Edward R. LaVallie1, Elizabeth A. DiBlasio1, Sharlotte Kovacic1, Kathleen L. Grant1, Paul F. Schendel1 & John M. McCoy1. A Thioredoxin Gene Fusion Expression System That Circumvents Inclusion Body Formation in the E. coli Cytoplasm. Nature Biotechnology 11, 187 - 193 (1993) doi:10.1038/nbt0293-187

Escherichia coli str. K-12 substr. MG1655 https://www.ncbi.nlm.nih.gov/nuccore/NC_000913.3