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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
Author(s) -
Neuhoff Volker,
Arold Norbert,
Taube Dieter,
Ehrhardt Wolfgang
Publication year - 1988
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150090603
Subject(s) - staining , isoelectric focusing , coomassie brilliant blue , polyacrylamide , chromatography , chemistry , polyacrylamide gel electrophoresis , silver stain , sodium dodecyl sulfate , electrophoresis , gel electrophoresis , biochemistry , microbiology and biotechnology , biology , genetics , polymer chemistry , enzyme
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 [1]. 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.