Difference between revisions of "Part:BBa K2382004"

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

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K2382004 short</partinfo>
-This part previously functioned as a DNA recombination and repair protein
-in E. coli. It is also found that Thioredoxin is capable of increasing the
-solubility of our protein, MSMEG5998. Therefore, we create this part for
-future igem teams who want to make their protein more soluble when
-facing inclusion bodies in E. coli.
-<!-- Add more about the biology of this part here
-===Usage and Biology===
-<!-- -->
+===<span class='h3bb'>Sequence and Features</span>===
-<span class='h3bb'>Sequence and Features</span>
 <partinfo>BBa_K2382004 SequenceAndFeatures</partinfo>
@@ Line 21: / Line 12: @@
 <partinfo>BBa_K2382004 parameters</partinfo>
 <!-- -->
+===Usage and Biology===
+This part previously functioned as a DNA recombination and repair protein in E. coli. <br>
+Thioredoxin can facilitate protein folding. And this par has its potential of being used in a fusion protein design.<br>
+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.
+[[File:Csmuxnchu description fig1.png|center|thumb|600px|''<b>BBa_K2382004 showed the gene design of the Thioredoxin fusion system construction.</b> ]]
+==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