Ruthenium (II) tris (bathophenantroline disulfonate)

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In recent years, 2-D electrophoresis has been widely accepted as a standard procedure to separate complex protein mixtures in proteome studies. Protein visualisation by Ruthenium (II) tris (bathophentroline disulfonate) has become a firmly established and widely used method in proteomic analysis [1,2,3,4,5,6,7,8,9,10,11,12,13,14,15] and a crucial step in protein expression profiling.

For protein detection, it is advantageous to use fluorescent labels containing chromophores which have longer excitation and emission wavelength than the aromatic amino acids. The dyes used for this important step should combine attributes like good signal to background ratio (contrast), broad linear dynamic range, broad application range, photo stability and compatibility to protein identification techniques, e.g. mass spectrometry (MS) or Western blotting.

Originally, the transition metal complex, Ruthenium (II) tris (4,7-diphenyl-1,10-phenantrolin disulfonate) also termed as Ruthenium (II) tris (bathophentroline disulfonate) was synthesized as a precursor for a dye that was used as a non-radioactive label for oligo nucleotides [16]. Later, Rabilloud et al. [17] used RuBPS as a fluorescent label for protein detection in polyacrylamide gels. The fact that RuBPS is not only easy to synthesize but also easy to handle, induced further developments in this field.

Lamanda et al. [18] improved the RuBPS staining protocol by selectively destaining the polyacrylamide matrix while the protein content remained tinctured. This new technique entailed a variety of advantages like strong signals, ameliorated signal to background ratio, better linearity and advanced baseline resolution. More information about Ruthenium (II) tris (bathophenantroline disulfonate) staining can be found on [1]

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