Difference between revisions of "Part:BBa K3712011"

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<center><img src="https://2021.igem.org/wiki/images/e/e0/T--HUST2-China--The_elution_peak_height_of_Wild-type_BLP-7-27_ELP_and_Optimized_BLP-7-27_ELP_and_the_running_gel_spectrum_after_purification.png" style="width:793px;height:360px"></center>
 
<center><img src="https://2021.igem.org/wiki/images/e/e0/T--HUST2-China--The_elution_peak_height_of_Wild-type_BLP-7-27_ELP_and_Optimized_BLP-7-27_ELP_and_the_running_gel_spectrum_after_purification.png" style="width:793px;height:360px"></center>
 
<center><b>Figure 2.</b>A) The elution peak height of Wild-type BLP-7-27 ELP is 1.41;  B) The height of the Optimized BLP-7-27 ELP elution peak is 1.26;  C) The gel running map, lane 1/2 is two-tube stream, lane 3 For Wild-type BLP-7-27 ELP, a thicker band appears near the 15kDa marker; lane 4/5/6 is a three-pipe stream that collects Optimized BLP-7-27 ELP, and a thicker band appears near the 15kDa marker.</center>
 
<center><b>Figure 2.</b>A) The elution peak height of Wild-type BLP-7-27 ELP is 1.41;  B) The height of the Optimized BLP-7-27 ELP elution peak is 1.26;  C) The gel running map, lane 1/2 is two-tube stream, lane 3 For Wild-type BLP-7-27 ELP, a thicker band appears near the 15kDa marker; lane 4/5/6 is a three-pipe stream that collects Optimized BLP-7-27 ELP, and a thicker band appears near the 15kDa marker.</center>
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<h2>Future direction:</h2>
 
<h2>Future direction:</h2>
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<center>(1) Unfortunately, due to time issues, we have no way to complete the purification of TLR2 antagonist. In the future, we will try different linkers to connect Wild-type/Optimized TLR2 antagonist and 27ELP.
 
<center>(1) Unfortunately, due to time issues, we have no way to complete the purification of TLR2 antagonist. In the future, we will try different linkers to connect Wild-type/Optimized TLR2 antagonist and 27ELP.
 
(2) Although our purified samples will not affect the subsequent functional verification, it can be seen from SDS-PAGE that even the purified bands will also have miscellaneous bands. Therefore, we want to use molecular sieves and freeze dryers for further purification attempts to obtain purer samples and make our experiment more successful.</center>
 
(2) Although our purified samples will not affect the subsequent functional verification, it can be seen from SDS-PAGE that even the purified bands will also have miscellaneous bands. Therefore, we want to use molecular sieves and freeze dryers for further purification attempts to obtain purer samples and make our experiment more successful.</center>

Revision as of 07:38, 21 October 2021


Flexible peptide

USAGE AND BIOLOGY

We use it when connecting ELP with other proteins, because it helps maintain the conformation of the two proteins

Sequence and Features


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]