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Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G‐250 and R‐250

Electrophoresis · 1988 · Vol. 9(6) · pp. 255–262
V. NeuhoffNorbert AroldDieter TaubeWolfgang Ehrhardt

Abstract

An improved procedure for staining of proteins following separation in polyacrylamide gels is described which utilizes the colloidal properties of Coomassie Brilliant Blue G-250 and R-250. The new method is based on addition of 20% v/v methanol and higher concentrations of ammonium sulfate to the staining solution previously described. The method combines the advantage of much shorter staining time with high sensitivity, a clear background not requiring destaining, stepwise staining, and stable fixation after staining. The method has been applied to staining of polyacrylamide gels after sodium dodecyl sulfate-electrophoresis and isoelectric focusing in carrier ampholyte-generated pH gradients.

Molecular Biology Techniques and ApplicationsAdvanced Proteomics Techniques and ApplicationsProtein purification and stabilityStainingIsoelectric focusingCoomassie Brilliant BluePolyacrylamideChromatographyChemistryPolyacrylamide gel electrophoresisSilver stainSodium dodecyl sulfateElectrophoresis

MeSH terms

Acrylic ResinsDensitometryElectrophoresis, Polyacrylamide GelGelsIsoelectric FocusingLightProteinsRosaniline DyesScattering, RadiationStaining and Labeling
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