BSA's structure comprises 583 amino acid residues organized into three homologous domains formed by six a-helices, stabilized by 17 intrachain disulfide bridges and a single free sulfhydryl group. This structural stability, combined with its carrier-protein binding capacity, explains its dual role in the lab: as a stabilizer that protects labile enzymes and proteins from degradation in solution, and as a blocking reagent that saturates non-specific binding sites in ELISA, Western blot, and immunohistochemistry protocols. The "Fraction V" designation originates from the classical Cohn cold-ethanol fractionation method, where serum albumin was isolated in the fifth ethanol fraction --- a naming convention still used today regardless of the specific purification method (Cohn fractionation, heat-shock, or chromatographic).
Bovine Serum Albumin (BSA), also known as "Fraction V," is a water-soluble, single-chain globular protein isolated from bovine blood serum. Synthesized in the liver, its primary physiological role is regulating colloidal osmotic pressure in blood, while its hydrophobic binding cleft makes it a versatile carrier for fatty acids, hormones, and drugs --- properties that underlie its extensive use across biochemistry, immunoassays, and cell culture.
| Chemical Name | Bovine Serum Albumin (BSA), Fraction V |
| CAS Number | 9048-46-8 |
| IUPAC Name | Albumin from Bovine Serum (Fraction V) |
| Molecular Formula | N/A |
| Molecular Weight | ~66,430 Da (66.5 kDa) g/mol |
Standard blocking agent in ELISA, Western blot, and immunohistochemistry to prevent non-specific antibody binding.
Used as a carrier protein and antioxidant supplement in serum-free and specialized cell culture formulations.
Reference standard in Bradford, BCA, and other colorimetric protein assay methods.
Applied as a stabilizing excipient for labile enzymes and low-concentration proteins in solution.
Biochem. Biophys. Res. Commun.
J. Immunol. Methods (immunoassay methodology reference)
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