Description_x000D_ General description_x000D_ Bovine serum albumin is a protein which has a key role in regulating blood colloidal osmotic pressure. A water-soluble protein composed of 583 amino acids, BSA has a calculated molecular weight of 66,430 Daltons. Six α-helices form three homologous domains of BSA. Depending on pH, BSA undergoes reversible conformational isomerization. The native structure of the protein becomes reactive and flexible on heating._x000D_ This BSA product is specifically evaluated and tested for the following properties:_x000D_ • Very low protease content / protease-free_x000D_ • Very low fatty acid content / fatty acid-free_x000D_ Protease-free BSA is especially useful for applications like:_x000D_ • Enzyme assays_x000D_ • Protein-based assays_x000D_ • Protease-sensitive techniques that include:_x000D_ a. Enzyme immunoassay (EIA)_x000D_ b. Nucleic acid hybridization_x000D_ c. Radioimmunoassay (RIA)_x000D_ Application_x000D_ Bovine Serum Albumin has been used:_x000D_ • as a constituent of medium used for the differentiation of human pluripotent stem cells_x000D_ • in enzyme-linked immunosorbent assay (ELISA) and sandwich ELISA_x000D_ • to permeabilize fetal cortical cells_x000D_ This A7030 BSA has specifically been used as a component of blocking buffer in a peptide-based ELISA assay for analysis of COVID-19 / SARS-CoV-2 samples (Poh, C.K. et al., Nat. Commun., 11(1), 2806 (2020))._x000D_ Packaging_x000D_ 1 kg in poly bottle_x000D_ 10, 50, 100, 500 g in poly bottle_x000D_ 5 kg in poly drum_x000D_ Biochem/physiol Actions_x000D_ Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies._x000D_ Features and Benefits_x000D_ • Heat shock fractionated_x000D_ • Protease-free_x000D_ • Fatty acid-free_x000D_ • Essentially globulin-free_x000D_ Preparation Note_x000D_ Prepared using heat shock fractionation_x000D_ 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.