Search results
Protein Extraction & Protein estimation by Bradford method. Theory/Principle: The Bradford dye assay is based on the equilibrium between three forms of Coomassie Blue G dye. Under strongly acid conditions, the dye is most stable as a doubly-protonated red form.
The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. It is a quick and accurate 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.
Bradford assays are dye-binding assays for fast and simple protein quantification. The assay is performed at room temperature and no special equipment is required.
An assay originally described by Bradford (1) has become the preferred method for quantifying protein in many laboratories. This technique is simpler, faster, and more sensitive than the Lowry method.
The Bradford assay is very fast and uses about the same amount of protein as the Lowry assay. It is fairly accurate and samples that are out of range can be retested within minutes. The Bradford is recommended for general use, especially for determining protein content of cell fractions and assesing protein concentrations for gel electrophoresis.
The Bradford method is a quantitative protein assay method, based on the binding of a dye, Coomassie Brilliant Blue, to a protein sample, and comparing this binding to a standard curve generated by the reaction of known amounts of a standard protein, usually BSA.
The Bradford protein assay is a dye-binding assay based on the differential color change of a dye in response to various concentrations of protein. The dye reagents are commonly purchased from Bio-Rad (Richmond, CA).
