Difference between revisions of "Part:BBa K2926058"
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<partinfo>BBa_K2926058 short</partinfo> | <partinfo>BBa_K2926058 short</partinfo> | ||
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− | To visualize the interactions of the n-terminal lectin binding domain of the S. cerevisiae protein Flo11 we fused the coding sequence | + | To visualize the interactions of the n-terminal lectin binding domain of the <i>S. cerevisiae</i> protein Flo11 we fused the coding sequence N-terminally to the coding sequence of the fluorescence reporter protein mCherry. mCherry was N-terminally fused to the M13 bacteriophage major coat protein pVIII. The whole protein was fused to a C-terminal hexahistidine tag to enable protein purification via metal ions. |
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<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
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− | <span class='h3bb'>Sequence and Features</span> | + | <span class='h3bb'><h1>Sequence and Features</h1></span> |
+ | Sequence was validated by Sanger sequencing. | ||
<partinfo>BBa_K2926058 SequenceAndFeatures</partinfo> | <partinfo>BBa_K2926058 SequenceAndFeatures</partinfo> | ||
Latest revision as of 21:53, 17 October 2019
Fusion protein of Flo11 (yeast), mCherry and pVIII (M13 bacteriophage) with purification tag
To visualize the interactions of the n-terminal lectin binding domain of the S. cerevisiae protein Flo11 we fused the coding sequence N-terminally to the coding sequence of the fluorescence reporter protein mCherry. mCherry was N-terminally fused to the M13 bacteriophage major coat protein pVIII. The whole protein was fused to a C-terminal hexahistidine tag to enable protein purification via metal ions.
Sequence and Features
Sequence was validated by Sanger sequencing.
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]