compare

Comparison List

Comparing:

mCherry, mRuby3, mScarlet

You can share this comparison at: www.fpbase.org/compare/mcherry,mruby3,mscarlet

Attribute Comparison

Name λex λem StokesλΔ EC QY Brightness pKa Aggregation Maturation Lifetimeτ kDa
mCherry 587 610 23 72,000 0.22 15.84 4.5 m 15.0 1.4 26.72
mRuby3 558 592 34 128,000 0.45 57.6 4.8 m 136.5 26.56
mScarlet 569 594 25 100,000 0.7 70.0 5.3 m 174.0 3.9 26.35

Sequence Comparison

mRuby3          MVSKGEE----LIKEnMRmKVvMEGSVNGHqFkctGEGEGRPYEGvQTmriKVieGGPLP
mCherry         MVSKGEEdnmaIIKEfMRFKVHMEGSVNGHEFEIEGEGEGRPYEGTQTAKLKVTKGGPLP
mScarlet        MVSKGEa----VIKEfMRFKVHMEGSmNGHEFEIEGEGEGRPYEGTQTAKLKVTKGGPLP

mRuby3          FAfDILatsFMYGSRtFIKyPADIPDfFKQSFPEGFtWERVtryEDGGVVTVTQDTSLED
mCherry         FAWDILSPQFMYGSkAyVKHPADIPDYlKlSFPEGFKWERVMNFEDGGVVTVTQDsSLqD
mScarlet        FsWDILSPQFMYGSRAFtKHPADIPDYYKQSFPEGFKWERVMNFEDGGaVTVTQDTSLED

mRuby3          GELvYnVKvRGvNFPSnGPVMQKKTkGWEpnTEmMYPaDGgLrGytdiALKvdgGGHlhc
mCherry         GEfIYKVKLRGTNFPSDGPVMQKKTMGWEASsERMYPEDGaLKGeIKqrLKLKDGGHYdA
mScarlet        GtLIYKVKLRGTNFPpDGPVMQKKTMGWEASTERlYPEDGvLKGdIKmALrLKDGGrYlA

mRuby3          NFvTTYrsKKtVgnikMPGvhaVDhrLerieesdneTyVvQrEvAvakySnlgGGMDELY
mCherry         EvKTTYKAKKPV---QlPGAYNVniKLDiTSHNEDYTIVEQYErAEGRHST--GGMDELY
mScarlet        DFKTTYKAKKPV---QMPGAYNVDrKLDiTSHNEDYTVVEQYErsEGRHST--GGMDELY

mRuby3          K
mCherry         K
mScarlet        K

References

  1. Shaner et al. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nature Biotechnology.Journal   Pubmed

  2. Shu et al. (2006) Novel Chromophores and Buried Charges Control Color in mFruits†,‡. Biochemistry.Journal   Pubmed

  3. Merzlyak et al. (2007) Bright monomeric red fluorescent protein with an extended fluorescence lifetime. Nature Methods.Journal   Pubmed

  4. Drobizhev et al. (2011) Two-photon absorption properties of fluorescent proteins. Nature Methods.Journal   Pubmed

  5. Landgraf et al. (2012) Segregation of molecules at cell division reveals native protein localization. Nature Methods.Journal   Pubmed

  6. Bindels et al. (2016) mScarlet: a bright monomeric red fluorescent protein for cellular imaging. Nature Methods.Journal   Pubmed

  7. Bajar et al. (2016) Improving brightness and photostability of green and red fluorescent proteins for live cell imaging and FRET reporting. Scientific Reports.Journal   Pubmed

  8. Heppert et al. (2016) Comparative assessment of fluorescent proteins for in vivo imaging in an animal model system. Molecular Biology of the Cell.Journal   Pubmed

  9. Mastop et al. (2017) Characterization of a spectrally diverse set of fluorescent proteins as FRET acceptors for mTurquoise2. Scientific Reports.Journal   Pubmed

  10. Balleza et al. (2017) Systematic characterization of maturation time of fluorescent proteins in living cells. Nature Methods.Journal   Pubmed

  11. Dunsing et al. (2018) Optimal fluorescent protein tags for quantifying protein oligomerization in living cells. Scientific Reports.Journal   Pubmed

  12. Stoddard & Rolland (2019) I see the light! Fluorescent proteins suitable for cell wall/apoplast targeting in Nicotiana benthamiana leaves. Plant Direct.Journal   Pubmed

  13. McCullock et al. (2020) Comparing the performance of mScarlet-I, mRuby3, and mCherry as FRET acceptors for mNeonGreen. PLOS ONE.Journal   Pubmed

  14. Myšková et al. (2020) Directionality of light absorption and emission in representative fluorescent proteins. Proceedings of the National Academy of Sciences.Journal   Pubmed

  15. Drobizhev et al. (2021) Local Electric Field Controls Fluorescence Quantum Yield of Red and Far-Red Fluorescent Proteins. Frontiers in Molecular Biosciences.Journal   Pubmed

  16. Joron et al. (2023) Fluorescent protein lifetimes report densities and phases of nuclear condensates during embryonic stem-cell differentiation. Nature Communications.Journal   Pubmed