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The entire experiment is done at room temperature. The Bradford protein assay can measure protein quantities as little as 1 to 20 μg. [14] It is an extremely sensitive technique. The dye reagent is a stable ready to use product prepared in phosphoric acid. It can remain at room temperature for up to 2 weeks before it starts to degrade.
The Bradford assay uses the spectral properties of Coomassie brilliant blue G-250 to estimate the amount of protein in a solution. [19] A protein sample is added to a solution of the dye in phosphoric acid and ethanol. Under the acid conditions the dye is normally a brownish colour but on binding to the protein the blue form of the dye is produced.
Marion Mckinley Bradford (October 28, 1946 - May 3, 2021) was an American scientist [1] who developed and patented the Bradford protein assay, [2] a method to quickly quantify the amount of protein in a sample. [3] [4] His paper describing the method is among the most cited scholarly articles of all time. [5] [6] [7]
Bradford assay method uses a dye to bind to protein. Most commonly, Coomassie brilliant blue G-250 dye is used. When free of protein, the dye is red but once bound to protein it turns blue. [11] The dye-protein complex absorbs light maximally at the wavelength 595 nanometers and is sensitive for samples containing anywhere from 1 ug to 60 ug.
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Protein detection evaluates the concentration and amount of different proteins in a particular specimen. [2] There are different methods and techniques to detect protein in different organisms. Protein detection has demonstrated important implications for clinical diagnosis, treatment and biological research. [3]