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mNeonGreen is derived from the lancelet Branchiostoma lanceolatum multimeric yellow fluorescence protein. Hence, mNeonGreen is evolutionarily distant from jellyfish-derived fluorescent proteins. At sequence level, mNeonGreen shares just 20-25% sequence identity with common GFP derivatives. Due to the low sequence similarity to mNeonGreen, it is expected that in general affinity tools for GFP variants, i.e. antibodies, should not bind to mNeonGreen and vice versa. mNeonGreen consists of 237 amino acids, which translates into 26.6 kDa molecular weight. This size, but not sequence, is very similar to EGFP that comprises 239 amino acids and is 26.9 kDa. Furthermore, mNeonGreen has an excitation maximum at 506 nm and an emission maximum at 517 nm (Shaner et al., 2013). mNeonGreen is compatible with most GFP filter sets. Apparently, it is 3 times brighter than GFP when using GFP filters; optimization of filters may increase its brightness further. In addition, mNeonGreen seems to be more stable and less sensitive to laser induced bleaching than EGFP. Therefore, mNeonGreen is particular suitable for confocal and super resolution microscopy, especially when fusion proteins are investigated, which are expressed at low levels.
150 µL
250 µL
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