Difference between revisions of "Part:BBa K1159312"
 
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This parts codes for a N-terminal ''Strep''-tag-II flanked by RFC[25] N-part to allow C-terminal fusions. ''Strep''-tag II is originally designed by Prof. Arne Skerra from TU Munich.
 
This parts codes for a N-terminal ''Strep''-tag-II flanked by RFC[25] N-part to allow C-terminal fusions. ''Strep''-tag II is originally designed by Prof. Arne Skerra from TU Munich.
  
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===Usage and Biology===
 
===Usage and Biology===
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The so called N-terminal encoded Strep-Tag-II flanked by RFC[25] N-part consists of the following amino acid sequence: Trp-Ser-His-Pro-Gln-Phe-Glu-Lys. The iGEM Team of TU Munich 2013 used the Streptag to purify several recombinant proteins, which have been expressed in E. coli, by affinity chromatography. An extraordinary benefit of the Strep-tag is its small size and the fact that it is almost inert to biochemical reactions, except its binding affinity to Biotin-labelled beads. Further on Strep-Tag antibodies with enzymatic or reporter genes can be used to target the Strep-Tag. Some applicational examples are Western-Blots, affinity protein purification and several assays.
  
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K1159312 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1159312 SequenceAndFeatures</partinfo>

Latest revision as of 15:08, 23 October 2013

N-terminal Strep-tag-II in RFC[25] N-Part

This parts codes for a N-terminal Strep-tag-II flanked by RFC[25] N-part to allow C-terminal fusions. Strep-tag II is originally designed by Prof. Arne Skerra from TU Munich.


Usage and Biology

The so called N-terminal encoded Strep-Tag-II flanked by RFC[25] N-part consists of the following amino acid sequence: Trp-Ser-His-Pro-Gln-Phe-Glu-Lys. The iGEM Team of TU Munich 2013 used the Streptag to purify several recombinant proteins, which have been expressed in E. coli, by affinity chromatography. An extraordinary benefit of the Strep-tag is its small size and the fact that it is almost inert to biochemical reactions, except its binding affinity to Biotin-labelled beads. Further on Strep-Tag antibodies with enzymatic or reporter genes can be used to target the Strep-Tag. Some applicational examples are Western-Blots, affinity protein purification and several assays.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 4
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]