Bovine Serum Albumin (BSA) is a globular and α-helical single-chain protein, produced in the liver. This non-glycosylated protein belongs to the serum albumins family. BSA consists of three homologous domains with two sub-domains each.
Bovine Serum Albumin (BSA) has been used:
- as a standard protein in the elution-filter aided proteome preparation (FASP) method and in sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)
- as a component of the molecular weight marker in SDS-PAGE and western blotting
- as a blocking agent in immunofluorescence
Bovine Serum Albumin (BSA) participates in the transport of endogenous and exogenous substances, such as hormones, fatty acids, drugs, and xenobiotics. It is used as a blocking agent in enzyme-linked immunosorbent assay (ELISA). BSA is usually preferred for the preparation of serum-free media. It is used in the pharmaceutical and cosmetic industry.
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.
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