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Comparison List

mCherry

mCherry is a basic (constitutively fluorescent) red fluorescent protein published in 2004, derived from Discosoma sp.. It is reported to be a very rapidly-maturing monomer with low acid sensitivity.
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Oligomerization Organism Molecular Weight Cofactor
Monomer Discosoma sp. 26.7 kDa -

FPbase ID: ZERB6

Attributes

Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
587 610 72,000 0.22 15.84 4.5 15.0 1.4

mCherry OSER Measurements

% Normal Cells OSER/NE ratio Cell Type Reference
95.0 ± 0.8 (10000 cells) - HeLa Cranfill et al. (2016)
91.0 (98 cells) - HeLa Costantini et al. (2015)
80.0 (369 cells) 2.0 ± 0.3 (38 cells) U-2 OS Bindels et al. (2016)
69.0 (1130 cells) - U-2 OS Manna et al. (2018)

Photostability

t1/2 (s) Power Light Mode In Cell Fusion ˚C Reference
68.0   Shu et al. (2006)

mCherry Sequence

mCherry was derived from mRFP1.5 with the following mutations: N6D/K194N/T195V/D196N
amino acid numbers relative to DsRed. show relative to mRFP1.5

MVSKGEEDNMAIIKEFMRFKVHMEGSVNGHEFEIEGEGEGRPYEGTQTAKLKVTKGGPLPFAWDILSPQFMYGSKAYVKHPADIPDYLKLSFPEGFKWERVMNFEDGGVVTVTQDSSLQDGEFIYKVKLRGTNFPSDGPVMQKKTMGWEASSERMYPEDGALKGEIKQRLKLKDGGHYDAEVKTTYKAKKPVQLPGAYNVNIKLDITSHNEDYTIVEQYERAEGRHSTGGMDELYK
GenBank: AAV52164
UniProtKB: X5DSL3
IPG: 3838123

Structure

Deposited: ,
Chromophore:

Excerpts

Randomization of position 163 in mRFP1.4 led to the identification of the substitution M163Q, which results in a nearly complete disappearance of the absorbance peak at ∼510 nm, present in all previous mRFP clones.

Shaner et al. (2004)

To test whether the introduction of GFP-type termini into mRFP variants would benefit fusion proteins expressed in mammalian cells, we fused mRFP1 and mCherry to the N terminus of α-tubulin. In most HeLa cells, expression of mRFP1-α-tubulin resulted in diffuse cytoplasmic fluorescence rather than proper incorporation into microtubules. However, mCherry-α-tubulin fusions were successfully incorporated into microtubules in most cells, similar to results seen with GFP-coupled tubulin.

Shaner et al. (2004)

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)

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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