Difference between revisions of "Part:BBa K3593003"

 
 
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Traditional aptamer of thrombin, which is well studied and proved to be binding efficiently. The binding ability is confirmed by our competitive assay of thrombin and electrophoresis afterwards. It is used to characterize our hardware and beneficial for our model construction of competitive assay
 
Traditional aptamer of thrombin, which is well studied and proved to be binding efficiently. The binding ability is confirmed by our competitive assay of thrombin and electrophoresis afterwards. It is used to characterize our hardware and beneficial for our model construction of competitive assay
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=Background=
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Aptamers of thrombin have  been used for anti-coagulation treatments in medicine, but we choose them only because of their high affinity as an aptamer. The aptamer we choose, BBa_K3593003, comes from one previous article[1], whose performance is tested through nitrocellulose filter binding. We elongate it for about some forty base pairs so that it can be amplified via PCR, in which the method of elongation comes from a previous literature[2]. Through experiments on it, we learn more amazing properties about aptamers. It will also be used in the demonstration of our hardware.
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=Sequence and features=
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<partinfo>BBa_K3593003 SequenceAndFeatures</partinfo>
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=Characterisation of this part=
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=References=
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1. D.M. Tasset, M.F. Kubik, W. Steiner, Oligonucleotide Inhibitors of Human Thrombin that Bind Distinct Epitopes ,Journal of Molecular Biology, 272 (1997) 688-698.  <br>
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2. Simon Fredriksson, Mats Gullberg, Jonas Jarvius, Charlotta Olsson,Kristian Pietras, Sigrún Margrét Gústafsdóttir, Arne Östman, and Ulf Landegren. Protein detection using proximity-dependent DNA ligation assays. June 2002·Nature Biotechnology 20(5):473-7 DOI: 10.1038/nbt0502-473 <br>
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===Usage and Biology===
 
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<span class='h3bb'>Sequence and Features</span>
 
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<partinfo>BBa_K3593003 SequenceAndFeatures</partinfo>
 
  
  

Latest revision as of 04:23, 27 October 2020


ssDNA, aptamer for thrombin(Apt29 El)

Traditional aptamer of thrombin, which is well studied and proved to be binding efficiently. The binding ability is confirmed by our competitive assay of thrombin and electrophoresis afterwards. It is used to characterize our hardware and beneficial for our model construction of competitive assay

Background

Aptamers of thrombin have been used for anti-coagulation treatments in medicine, but we choose them only because of their high affinity as an aptamer. The aptamer we choose, BBa_K3593003, comes from one previous article[1], whose performance is tested through nitrocellulose filter binding. We elongate it for about some forty base pairs so that it can be amplified via PCR, in which the method of elongation comes from a previous literature[2]. Through experiments on it, we learn more amazing properties about aptamers. It will also be used in the demonstration of our hardware.

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]

Characterisation of this part

References

1. D.M. Tasset, M.F. Kubik, W. Steiner, Oligonucleotide Inhibitors of Human Thrombin that Bind Distinct Epitopes ,Journal of Molecular Biology, 272 (1997) 688-698.
2. Simon Fredriksson, Mats Gullberg, Jonas Jarvius, Charlotta Olsson,Kristian Pietras, Sigrún Margrét Gústafsdóttir, Arne Östman, and Ulf Landegren. Protein detection using proximity-dependent DNA ligation assays. June 2002·Nature Biotechnology 20(5):473-7 DOI: 10.1038/nbt0502-473