Bovine Serum Albumin (BSA) is a versatile and widely studied protein derived from bovine blood, with a molecular weight of approximately 66.5 kDa and composed of 583 amino acids. It is characterized by its stability, solubility, and ability to bind a variety of molecules, making it a crucial component in numerous biochemical and molecular biology applications. BSA is used as a standard in protein quantification assays, such as the Bradford and Lowry methods, due to its consistent properties. It also serves as a stabilizing agent in enzyme assays, a blocking agent in immunoassays like ELISA and Western blotting, and a cryoprotectant in cell culture. Additionally, BSA is involved in the transport and metabolism of various ligands, including fatty acids and metal ions, and has antioxidant properties. Its structure, consisting of three globular domains with multiple disulfide bonds, contributes to its stability and functionality. BSA's ability to bind and transport molecules, along with its role in maintaining blood pH and colloid osmotic pressure, highlights its importance in both research and physiological contexts.