Difference between revisions of "Part:BBa K4421010"
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<partinfo>BBa_K4421010 short</partinfo>
 
<partinfo>BBa_K4421010 short</partinfo>
  
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The 2A peptide sequence self-cleaving sequence， was intercalated between iCASP9 and the GFP tag and it is derived from FMDV (foot-and-mouth disease virus) to allow transcription and expression of one single mRNA molecule.
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The self-cleaving 2A peptide sequence， was intercalated between iCASP9 and the GFP tag and it was derived from FMDV (foot-and-mouth disease virus) to allow transcription and expression of one single mRNA molecule.
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===Usage and Biology===
 
===Usage and Biology===
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The 2A self-cleaving peptide was first identified in 1991 from foot-and-mouth disease virus(Ryan et al., 1991). The 2A peptide, containing the canonical motif DxExNPGP (where “x” is any amino acid which is not conserved), induces the recombinant protein containing 2A peptide to shear itself in the cell, often at the site corresponding to the "-NPG/P-" junction(DOI: 10.5661/bger-26-223).
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The 2A self-cleaving peptide was first identified in 1991 from foot-and-mouth disease virus(Ryan et al., 1991). The 2A peptide, containing the canonical motif DxExNPGP (where “x” is any amino acid which is not conserved), induces the recombinant protein containing 2A peptide to shear itself in the cell, often at the site corresponding to the "-NPG/P-" junction(DOI: 10.5661/bger-26-223).In genetic engineering, 2A peptide can cause an open reading frame (ORF) to translate the peptide chain into several independent peptide chains.
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In some studies, the 2A peptide was used to link icasp9 gene with cytokine and  leucocyte differentiation antigen gene(https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2018664/  https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3236370/),thus 少些质粒。 So we designed it to link icasp9 and GFP,
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===advantages===
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IRES can also translate two peptide chains from an open reading frame,but the peptide chain upstream of IRES is more efficiently expressed than the peptide chain located downstream [10]. In contrast, the peptide chains upstream and downstream of 2A peptide chain exhibit similar amounts in terms of expression efficiency.
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 06:07, 22 June 2022


2A sequence

The self-cleaving 2A peptide sequence， was intercalated between iCASP9 and the GFP tag and it was derived from FMDV (foot-and-mouth disease virus) to allow transcription and expression of one single mRNA molecule.

Usage and Biology

The 2A self-cleaving peptide was first identified in 1991 from foot-and-mouth disease virus(Ryan et al., 1991). The 2A peptide, containing the canonical motif DxExNPGP (where “x” is any amino acid which is not conserved), induces the recombinant protein containing 2A peptide to shear itself in the cell, often at the site corresponding to the "-NPG/P-" junction(DOI: 10.5661/bger-26-223).In genetic engineering, 2A peptide can cause an open reading frame (ORF) to translate the peptide chain into several independent peptide chains.

advantages

IRES can also translate two peptide chains from an open reading frame,but the peptide chain upstream of IRES is more efficiently expressed than the peptide chain located downstream [10]. In contrast, the peptide chains upstream and downstream of 2A peptide chain exhibit similar amounts in terms of expression efficiency. . 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]