Crystal violet stains proteins in SDS-PAGE gels and zymograms
| Autor: | Robert G.E. Krause, J.P. Dean Goldring |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Biophysics
01 natural sciences Biochemistry Stain 03 medical and health sciences chemistry.chemical_compound Escherichia coli Crystal violet Coloring Agents Molecular Biology Polyacrylamide gel electrophoresis Volume concentration 030304 developmental biology 0303 health sciences Chromatography Staining and Labeling Chemistry Escherichia coli Proteins Coomassie Brilliant Blue 010401 analytical chemistry Cell Biology 0104 chemical sciences Staining Double staining Electrophoresis Polyacrylamide Gel Gentian Violet Nitrocellulose |
| Zdroj: | Analytical Biochemistry. 566:107-115 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/j.ab.2018.11.015 |
| Popis: | Coomassie brilliant blue R250, an anionic dye is the most popular stain to detect proteins resolved in SDS-PAGE gels. Crystal violet, a cationic dye was found to be versatile and stained proteins in SDS-PAGE gels and in zymograms. Stained proteins can be transferred to nitrocellulose and the stained proteins on the western detected with enzyme coupled antibodies. Staining can be reversed. Staining takes 3 h at RT or 30 min at 60 °C. Crystal violet stained some E. coli high and low molecular weight proteins not stained by Coomassie blue R250. Crystal violet stained down to 16 ng of protein, some five-fold lower than Coomassie blue, though the two stains had a similar linear dynamic range. The staining sensitivity could be increased to 2 ng when crystal violet and Coomassie blue were combined in a double staining/counterion dye formulation. The low concentrations of the dye without a destaining step reduces the costs of the technique and results in a more environmentally friendly stain compared to traditional staining methods. |
| Databáze: | OpenAIRE |
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