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Comparison List

EBFP1.2

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

Attributes

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    

Photostability

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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

MVSKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLSHGVQCFARYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYIMADKQKNGIKVNFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDSHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK

Excerpts

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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