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The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [2] spectroscopic analytical procedure used to measure the concentration of protein in a solution. The reaction is dependent on the amino acid composition of the measured proteins.
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.
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.
BCA protein assay in a 96 well plate. The bicinchoninic acid assay (BCA assay), also known as the Smith assay, after its inventor, Paul K. Smith at the Pierce Chemical Company, [1] now part of Thermo Fisher Scientific, is a biochemical assay for determining the total concentration of protein in a solution (0.5 μg/mL to 1.5 mg/mL), similar to Lowry protein assay, Bradford protein assay or ...
Coffee beans are hitting record high prices not seen in nearly 50 years after difficult growing seasons among some of the world's top producing regions. Earlier this week, the Wall Street Journal ...
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