Part:BBa_K4421010
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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