(2013). Nature Methods, 10(5) , 407-409. doi: 10.1038/nmeth.2413. Article Pubmed
| Protein (state) | t1/2 (s) | Power | Light | Mode | In Cell | Fusion | ˚C |
|---|---|---|---|---|---|---|---|
| Clover | 50.0 | ||||||
| mNeonGreen | 158.0 | 4.3 mW | Arc-lamp | Widefield | H2B |
| Protein | % Normal Cells | OSER/NE ratio | Cell Type | Temp (˚C) |
|---|---|---|---|---|
| mEGFP | 98.1 ± 1.6 (10000 cells) | - | HeLa | - |
| mTurquoise | 93.8 ± 1.0 (10000 cells) | - | HeLa | - |
| mRuby2 | 87.4 ± 5.8 (10000 cells) | - | HeLa | - |
| Clover | 72.9 ± 5.5 (10000 cells) | - | HeLa | - |
| mNeonGreen | 90.4 ± 2.1 (10000 cells) | - | HeLa | - |
| EGFP | 76.5 ± 6.9 (10000 cells) | - | HeLa | - |
mNeonGreen is the brightest monomeric green or yellow fluorescent protein yet described to our knowledge, performs exceptionally well as a fusion tag for traditional imaging as well as stochastic single-molecule superresolution imaging and is an excellent fluorescence resonance energy transfer (FRET) acceptor for the newest cyan fluorescent proteins.
... as it has so little sequence identity in common with other frequently used fluorescent proteins, mNeonGreen will be an attractive target for antibody development and should be amenable to orthogonal immunoprecipitation experiments along with jellyfish-derived and coral-derived fluorescent proteins.
Most newly cloned green and yellow fluorescent proteins are not subjected to additional engineering simply because of their lack of improved properties relative to existing proteins. Thus, we were intrigued that a yellow fluorescent protein from B. lanceolatum (LanYFP) exhibits an unusually high quantum yield (∼0.95) and extinction coefficient (∼150,000 M−1 cm−1), making it a very attractive candidate for additional development.