Bovine Serum Albumin

Bovine serum albumin (BSA) is made up of 583 amino acids, with no carbohydrates. It is a water-soluble protein with a molecular weight of 66.4kDa. Six α-helices form three homologous domains of BSA. Depending on pH, it undergoes reversible conformational isomerization. The native structure of BSA becomes reactive and flexible on heating. BSA acts as a model protein in various studies, such as immunodiagnostic procedures, cell culture media and clinical chemistry. It is also relevant in foods containing bovine milk or meat.
Appl- Bovine serum albumin has been used as a supplement of phosphate buffered saline (PBS) to store brain tissue sections. It has also been used as a blocking agent for cells for immunofluorescence analysis.

Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.

Serum albumin may be referred to as Fraction V. This naming convention is taken from the original Cohn method of fractionating serum proteins using cold ethanol precipitation. Serum albumin was found in the fifth ethanol fraction using Cohn′s method. Since then, the term "Fraction V" has been used by some to describe serum albumin regardless of the method of preparation. Others have used this term to describe serum albumin purified by ethanol fractionation methods that have been highly modified since the original Cohn method was described. Sigma-Aldrich manufactures and distributes serum albumins purified from a variety of primary methods including the true Cohn fractionation method, modified ethanol fractionation methods, heat shock and chromatography. Additional purification steps may include crystallization or charcoal filtration.