Difference between revisions of "Part:BBa K2926067"

 
 
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<partinfo>BBa_K2926067 short</partinfo>
 
<partinfo>BBa_K2926067 short</partinfo>
  
The extracellular cysteine-rich domain of the membrane protein Opy2 from S. cerevisiae was n-terminally fused to the red fluorescing reporter protein mCherry. Additionally, the M13 bacteriophage major coat protein pVIII was fused to the c-terminus of mCherry. To enable easy protein purification a hexahistidine tag was fused to the c-terminus of the protein.
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The extracellular cysteine-rich domain of the membrane protein Opy2 from <i>S. cerevisiae</i> was n-terminally fused to the red fluorescing reporter protein mCherry. Additionally, the M13 bacteriophage major coat protein pVIII was fused to the C-terminus of mCherry. To enable easy protein purification a hexahistidine tag was fused to the C-terminus of the protein.
  
 
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<span class='h3bb'>Sequence and Features</span>
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<span class='h3bb'><h1>Sequence and Features</h1></span>
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Sequence was validated by Sanger sequencing.
 
<partinfo>BBa_K2926067 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K2926067 SequenceAndFeatures</partinfo>
  

Latest revision as of 22:44, 17 October 2019


Fusion protein of Opy2 (yeast), mCherry and pVIII (bacteriophage M13) with purification tag

The extracellular cysteine-rich domain of the membrane protein Opy2 from S. cerevisiae was n-terminally fused to the red fluorescing reporter protein mCherry. Additionally, the M13 bacteriophage major coat protein pVIII was fused to the C-terminus of mCherry. To enable easy protein purification a hexahistidine tag was fused to the C-terminus of the protein.

Sequence and Features

Sequence was validated by Sanger sequencing.


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
    COMPATIBLE WITH RFC[1000]