Difference between revisions of "Part:BBa K2382004"

(References)
(Usage and Biology)
Line 18: Line 18:
 
found that Thioredoxin is capable of increasing enzyme activity of our protein, MSMEG5998.
 
found that Thioredoxin is capable of increasing enzyme activity of our protein, MSMEG5998.
 
We designed a polylinker that has multiple restriction cutting sites at the end of this part for
 
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
+
future iGEM teams who want to make their protein more effective.
  
 
==Characterization of the Thioredoxin with polylinker==
 
==Characterization of the Thioredoxin with polylinker==

Revision as of 21:27, 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. It is also found that Thioredoxin is capable of increasing enzyme activity of our protein, MSMEG5998. 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.

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