Part:BBa_K4422003
T2A Self Cleaving Peptide (Pichia pastoris codon optimized)
When the expression of more than one gene in cells using a single plasmid is required, an efficient strategy is needed. In general, 2A peptides lead to relatively high levels of protein expression compared to other strategies for multigene coexpression, they are viral oligopeptides 18 to 22 amino acids (aa) in length that mediate the "cleavage" of polypeptides during translation in eukaryotic cells, being small in size, they have a lower risk of interfering with the function of co-expressed genes.
Liu, Z., Chen, O., Wall, J., Zheng, M., Zhou, Y., Wang, L., Vaseghi, H. R., Qian, L., & Liu, J. (2017). Systematic comparison of 2A peptides for cloning multi-genes in a polycistronic vector. Scientific reports, 7(1), 2193. https://doi.org/10.1038/s41598-017-02460-2
Kim, J. H., Lee, S. R., Li, L. H., Park, H. J., Park, J. H., Lee, K. Y., Kim, M. K., Shin, B. A., & Choi, S. Y. (2011). High cleavage efficiency of a 2A peptide derived from porcine teschovirus-1 in human cell lines, zebrafish and mice. PloS one, 6(4), e18556. https://doi.org/10.1371/journal.pone.0018556
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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