follow. It is done in one step where the Bradford reagent is added to a test tube along with the sample. After mixing well, the mixture almost immediately changes to a blue color. When the dye binds to the proteins through a process that takes about 2 minutes, a change in the absorption maximum of the dye from 465 nm to 595 nm in acidic solutions occurs. This dye creates strong noncovalent bonds with the proteins, via electrostatic interactions with the amino and carboxyl groups, as well as Van Der Waals interactions. Only the molecules that bind to the proteins in solution exhibit this change in absorption, which eliminates the concern that unbound molecules of the dye might contribute to the experimentally obtained absorption reading. This process is more beneficial since it is less pricey than other methods, easy to use, and has high sensitivity of the dye for protein. After 5 minutes of incubation, the absorbance can be read at 595 nm using a spectrophotometer or a mobile smartphone camera (RGBradford method). This assay is one of the fastest assays performed on proteins. The total time it takes to set up and complete the assay is under 30 minutes. The entire experiment is done at room temperature. The Bradford protein assay can measure protein quantities as little as 1 to 20 μg. 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. Protein samples usually contain salts, solvents, buffers, preservatives, reducing agents and metal chelating agents. These molecules are frequently used for solubilizing and stabilizing proteins. Other protein assay like BCA and Lowry are ineffective because molecules like reducing agents interfere with the assay. Using Bradford can be advantageous against these molecules because they are compatible to each other and will not interfere. The linear graph acquired from the assay (absorbance versus protein concentration in μg/mL) can be easily extrapolated to determine the concentration of proteins by using the slope of the line. It is a sensitive technique. It is also very simple: measuring the OD at 595 nm after 5 minutes of incubation. This method can also make use of a Vis spectrophotometer or a mobile smartphone camera (RGBradford method). Disadvantages The Bradford assay is linear over a short range, typically from