Description
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The kit is designed for protein quantification in biological samples.
Background: The Bradford assay is based on the direct binding of Coomassie brilliant blue G-250 dye to proteins at arginine, tryptophan, tyrosine, histidine, and phenylalanine residues. Anionic dye binds to these residues producing an absorbance maximum at 595 nm. The dye interacts with the protein via van der Waals forces between the hydrophobic regions of the protein and the nonpolar region of the dye, and the electrostatic interaction between the negatively charged dye and positively charged amino groups of protein. The formation of the dye-protein complex takes about two minutes and remains stable for an hour, so the procedure is very fast and the time for trial is not limiting. The dye-protein complex has a high extinction coefficient, which makes the highly sensitive assay. Highly alkaline buffers present interference but it can be countered running appropriate targets. Reagents as magnesium chloride, potassium, sodium, ammonium sulfate and ethanol has no effect on the assay. Other reagents such as Tris, acetic acid, 2-mercaptoethanol, sucrose, glycerol, EDTA and traces of detergents Triton® X-100, sodium dodecyl sulphate (SDS) and Hemosol has light effects that can be easily removed. The presence of large amounts of detergents has a high interferenc. Nevertheless, many chemical reagents do not directly affect the development of dye color when used the standard protocol.
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