Protein_Domain

Part:BBa_K4439004

Designed by: Pauline Verchinine   Group: iGEM22_EPFL   (2022-09-29)

mSA

Monomer Streptavidin

Abstract

mSA, or monomeric streptavidin, is an engineered streptavidin/rhizavidin hybrid that binds to biotin with high affinity as a monomer, it was constructed and characterized by Lim et al. in 2013 (see References). It can be fused as a genetic tag to heterologous proteins to enable biotin binding. The biotin affinity of mSA is the highest among nontetrameric streptavidin, the monomer also has significantly higher stability and solubility than all other previously engineered monomers to ensure the folding and functionality of the molecule during its application. It is therefore a useful tool for biotechnology applications making use of the streptavidin-biotin interaction.

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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 85
    Illegal AgeI site found at 145
  • 1000
    COMPATIBLE WITH RFC[1000]

References

  • Lim, K. H., Huang, H., Pralle, A. & Park, S. (2012, august 8). Stable, high-affinity streptavidin monomer for protein labeling and monovalent biotin detection. Biotechnology and Bioengineering, 110(1), 57‑67. https://doi.org/10.1002/bit.24605
[edit]
Categories
Parameters
None