Comparison List


EBFP1.2 is a basic (constitutively fluorescent) uv fluorescent protein published in 2007, derived from Aequorea victoria. It has high acid sensitivity.
Oligomerization Organism Molecular Weight Cofactor
Monomer Aequorea victoria 26.9 kDa -

FPbase ID: 514KE


Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
379 446 41,000 0.45 18.45 6.6    


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EBFP1.2 Sequence

EBFP1.2 was derived from EBFP with the following mutations: S30R/Y39N/T65S/S72A/N105T/I171V/N198S/A206V
amino acid numbers relative to avGFP. show relative to EBFP



We had initially presumed that EBFP was close to the maximum achievable fluorescent brightness for its particular chromophore structure. However, the recent report from Waldo and co-workers that introduction of the “superfolder” mutations into BFP improved the fluorescent brightness in bacterial colonies galvanized us to explore whether these mutations could also benefit EBFP. Mutations S30R/Y39N/T65S/S72A/N105T/I171V/N198S/A206V were introduced into EBFP by site-directed mutagenesis to produce EBFP1.2

Ai et al. (2007)

Primary Reference

Additional References

  1. Two-photon absorption properties of fluorescent proteins

    Drobizhev M, Makarov Ns, Tillo Se, Hughes Te, Rebane A

    (2011). Nature Methods, 8(5) , 393-399. doi: 10.1038/nmeth.1596. Article   Pubmed

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