Difference between revisions of "Part:BBa K3139012"

 
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<partinfo>BBa_K3139012 short</partinfo>
 
<partinfo>BBa_K3139012 short</partinfo>
  
TEV is a member of the Poty viridae family responsible for infections of many different plants species of Solanaceae including N.tabacum ,One of the most important TEV proteases is Nuclear Inclusion protein a(Nla).TEVpS is part of the Nuclear Inclusion a(Nla) enzyme.It is an efficient and specific protease, nowadays TEVpS is a unique endopepidase largely exploited in biotechnology from industrial applications to in vitro and in vivo cellular studies. In our project, we use it to secrete cutting enzyme, which can specifically recognize cleavage site on our designed fusion protein sequence and cut it into several individual anti-plasmodium peptide.
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TEV is a member of the Poty viridae family responsible for infections of many different plants species of Solanaceae including N.tabacum ,One of the most important TEV proteases is Nuclear Inclusion protein a(Nla).TEVpS is part of the Nuclear Inclusion a(Nla) enzyme.It is an efficient and specific protease, able to cleave its substrate ENLYFQS between the Q and S residues, leaving an ENLYFQ-tail on the C-terminus of the protein encoded upstream and a serine residue on the N-terminus of the downstream-encoded protein. Nowadays TEVpS is a unique endopepidase largely exploited in biotechnology from industrial applications to in vitro and in vivo cellular studies. In our project, we use it to secrete cutting enzyme, which can specifically recognize cleavage site on our designed fusion protein sequence and cut it into several individual anti-plasmodium peptide.
  
 
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Revision as of 00:22, 21 October 2019


TEVpS

TEV is a member of the Poty viridae family responsible for infections of many different plants species of Solanaceae including N.tabacum ,One of the most important TEV proteases is Nuclear Inclusion protein a(Nla).TEVpS is part of the Nuclear Inclusion a(Nla) enzyme.It is an efficient and specific protease, able to cleave its substrate ENLYFQS between the Q and S residues, leaving an ENLYFQ-tail on the C-terminus of the protein encoded upstream and a serine residue on the N-terminus of the downstream-encoded protein. Nowadays TEVpS is a unique endopepidase largely exploited in biotechnology from industrial applications to in vitro and in vivo cellular studies. In our project, we use it to secrete cutting enzyme, which can specifically recognize cleavage site on our designed fusion protein sequence and cut it into several individual anti-plasmodium peptide.

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
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI.rc site found at 322
    Illegal SapI.rc site found at 670