Coomassie Blue History
The first time Coomassie blue
was used for the visualization of proteins was in 1964. They were separated by electrophoresis, and the cellulose acetate sheet was transferred to a solution of the Coomassie dye. Two years later the same was done with proteins separated in a polyacrylamide gel. However, the Coomassie dye stained both the gel and the proteins, so the gel had to be destained afterwards by electrophoresis. Later, the destaining of the gel has been also done by using acetic acid.
Subsequently, it was found that the staining of the gel can be avoided by using a colloid form of the Coomassie dye in a trichloroacetic acid solution. This way, no destaining of the gel was necessary anymore. Nowadays the typical combination of reagents used is the colloid of the G-form of the Coomassie Blue Stain, phosphoric acid, ethanol and ammonium sulfate. Alternatively, methanol and aluminium sulfate can be used.
Coomassie blue is used in the Bradford assay to estimate the quantity of protein in a solution. Upon binding to the protein, the Coomassie dye turns blue, and the optical absorbance of the solution is measured at 595 nm. This binding also results in the charge of the complex becoming overall negative, which enables separation by polyacrylamide gel electrophoresis. In this electrophoresis, the mobility of protein complexes depends on both the molecular weight and the amount of bound Coomassie dye.
Our specially designed product Coomassie Instant Blue
is a Coomassie Stain that contains no methanol, which makes the possibility of proteins to be dyed
in just a few minutes without doing anything other.
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