Bovine serum albumin has been used to quantify proteins in raw enzyme extracts. It has also been used as a blocking agent for mitochondrial imaging.
Albumin from bovine serum can be used for Electron and Immunoelectron microscopy. It can also be used for isolating and culturing neonatal rat cardiac ventricular myocytes.
Bovine serum albumin also refers as BSA or Fraction V is a protein isolated from cows. BSA can block vacant binding sites in enzyme-linked immunosorbent assay (ELISA) in both poly-l-lysine (PLL)-treated and non-treated microwells. It can also trigger insulin dependent diabetes mellitus.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
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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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