Part:BBa_K4161500:Design

20ipaD for S. cereviae Expression

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]

Design Notes

The sequence was originally retrieved as the amino acid sequence. Because different organisms prefer different codons, codon optimization was done to ease the expression in S. cerevisiae when converting aa sequence into DNA sequence.

Source

Michael L. Barta, Jonathan P. Shearer, Olivia Arizmendi, Jacqueline M. Tremblay, Nurjahan Mehzabeen, Qi Zheng, Kevin P. Battaile, Scott Lovell, Saul Tzipori, William D. Picking, Charles B. Shoemaker, Wendy L. Picking. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. Journal of Biological Chemistry, 292(40): 16677-16687.

References

Michael L. Barta, Jonathan P. Shearer, Olivia Arizmendi, Jacqueline M. Tremblay, Nurjahan Mehzabeen, Qi Zheng, Kevin P. Battaile, Scott Lovell, Saul Tzipori, William D. Picking, Charles B. Shoemaker, Wendy L. Picking. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. Journal of Biological Chemistry, 292(40): 16677-16687.