Comparison List


mCherry2 is a basic (constitutively fluorescent) red fluorescent protein published in 2017, derived from Discosoma sp.. It has very low acid sensitivity.
Oligomerization Organism Molecular Weight Cofactor
Monomer Discosoma sp. 26.7 kDa -

FPbase ID: CN92E


Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
589 610 79,400 0.22 17.47 3.3    


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mCherry2 Sequence

mCherry2 was derived from mCherry with the following mutations: K92N/K138C/K139R/S147T/N196D/T202L
amino acid numbers relative to DsRed. show relative to mCherry



This strongly suggests that the fluorescent protein tag caused clustering artifacts (Fig. 2a) and that ClpX and ClpP fluorescent protein fusions cannot be trusted for determining localization of native, untagged proteins. [...] These findings motivated us to evaluate other fluorescent proteins fused to ClpP or ClpX. We found that sfGFP, Venus, mCherry and mCherry2 all caused substantial foci formation, despite being monomers or very weak dimers when expressed alone. mKate2 and TagRFP-T caused intermediate clustering, whereas with mVenus and mYPet most of the fluorescence signal was spatially uniform, although we observed foci in a few cells. mTagBFP and mEos2 fusions resulted in a weak signal with infrequent dim foci. We detected no foci for photoswitchable (PS)-CFP2, reversible switchable (rs)FastLime (data not shown) and a mutant of sfGFP with a charge of −30 (GFP(−30)), but the signals were very dim. Finally, mGFPmut3, Dronpa and Dendra2 displayed an essentially uniform signal. Fluorescent protein fusions to ClpP generally caused more foci formation than fusions to ClpX, in particular for mYPet (Fig. 2d).

Landgraf et al. (2012)

mFruit variant mCherry2 is a further engineered variant of mCherry that retains similar excitation and emission maxima (λex = 589 nm and λem = 610 nm) but has slightly higher brightness. This variant was generated some years ago by several rounds of directed evolution of an mCherry-ferritin fusion, as was originally described for Superfolder GFP (Waldo et al, 1999), but was not characterized in detail until the current work

Shen et al. (2017)

The increased in vitro brightness of mCherry2 does not translate into substantially improved brightness in either bacteria or mammalian cells. However, we noticed that E. coli colonies expressing mCherry2 have a larger size than the ones expressing mCherry, at similar colony densities on LB agar plates. This observation suggested that mCherry2 might have decreased cytotoxicity in E. coli.

Shen et al. (2017)

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