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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

Neuhoff, Volker, Arold, Norbert, Taube, Dieter, Ehrhardt, Wolfgang·1988·ELECTROPHORESIS

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 [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.

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Metadata

Authors
Neuhoff, V., Arold, N., Taube, D., & Ehrhardt, W.
Venue
ELECTROPHORESIS
Publisher
Wiley
Published
1988-01
Volume
9
Issue
6
Pages
255-262
ISSN
  • 0173-0835 (ISSN-L)
  • 1522-2683
OpenAlex
W1964313477
Cited by
2,676
References
0
FWCI
13.52
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: 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. https://app.cochat.ai/papers/10.1002/elps.1150090603
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Neuhoff, V., Arold, N., Taube, D., & Ehrhardt, W. (1988). 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. https://doi.org/10.1002/elps.1150090603

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