Beta mercaptoethanol (BME) is a small, thiol-containing reducing agent that is commonly used in biochemistry and molecular biology. It is particularly important in protein studies due to its ability to break disulfide bonds within proteins, which helps to denature them and ensure they are in their extended form.
In the context of SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) assays, beta mercaptoethanol plays a crucial role. SDS-PAGE is used to separate proteins based on their molecular weight, but this process requires the proteins to be fully denatured. The presence of disulfide bonds can prevent proteins from unfolding properly, which might lead to inaccurate results in terms of size and separation.
By including beta mercaptoethanol in the sample buffer, researchers can effectively reduce these bonds, allowing the proteins to denature completely. This ensures that the SDS can bind uniformly to the protein, imparting a negative charge proportional to the protein’s mass. Therefore, including beta mercaptoethanol is essential for achieving accurate and reproducible results in SDS-PAGE assays.