Zusammenfassung
Fluorescent probes for the detection of protein phosphorylation on SDS-PAGE are presented. The probes were
designed using a dinuclear metal-chelate phosphate recognition unit and an environmentally sensitive fluorophore.
The specificity of the probes is determined by their binding site selectivity toward phosphate ions and the emission
response induced by the change in the electrostatic ...
Zusammenfassung
Fluorescent probes for the detection of protein phosphorylation on SDS-PAGE are presented. The probes were
designed using a dinuclear metal-chelate phosphate recognition unit and an environmentally sensitive fluorophore.
The specificity of the probes is determined by their binding site selectivity toward phosphate ions and the emission
response induced by the change in the electrostatic environment of the fluorophore upon binding to a phosphorylated
amino acid residue. The staining is fully reversible due to the noncovalent binding of the probe. Gel bands with
less than 100 ng of phosphorylated R-casein are detectable with the new probes on a normal UV-table without
specialized equipment like a laser-based gel scanner or a cooled camera detector
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