Range: Table - link nm
||Shaner NC, Steinbach PA, Tsien RY. A guide to choosing fluorescent proteins. Nat Methods. 2005 Dec2(12):905-9. Article - link p.907 table 1 PubMed ID16299475
||Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, Tsien RY. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol. 2004 Dec22(12):1567-72.PubMed ID15558047
||This is the major excitation peak of RFP mCherry. Fluorescent proteins are genetically encoded, easily imaged reporters crucial in biology and biotechnology. Although in many cases, a trial-and-error approach may still be necessary in determining the answers to questions: Which FPs are best for general use? Which are the brightest? What additional factors determine which are best for a given experiment?, a unified characterization of the best available FPs provides a useful guide in narrowing down the options. P.907 left column top paragraph: "Bleaching experiments were performed in parallel for several (but not all) of the FPs [fluorescent proteins] listed in Table 1 expressed in live cells and gave time courses closely matching those of purified proteins in microdroplets. Based on [investigators’] photobleaching assay results, it is clear that photostability can be highly variable between different FPs, even those of the same spectral class. Taking into account brightness and folding efficiencies at 37 °C, the best proteins for long-term imaging are the monomers mCherry and mKO. The red tandem dimer tdTomato is also highly photostable and may be used when the size of the fusion tag is not of great concern. The relative photostability of proteins in each spectral class is indicated in Table 1." P.908 left column top paragraph: "Thus, any of the recommended proteins in Table 1 should be capable of performing well in any application requiring a monomeric fusion tag."