Albumin, the major protein produced by liver cells, represents more than half of the total protein content of human serum. Many other body fluids also contain albumin. Three major functions for serum albumin have been proposed: maintenance of osmotic pressure, transportation of a variety of substances and an endogenous source of amino acids. The primary sites of albumin degradation are not known, but the protein can be metabolized by almost every organ in the body. Determination of serum albumin levels is a widely used screening test in clinical medicine. A decrease in serum albumin levels may indicate disease states such as malnutrition, cirrhosis, nephrotic syndrome, diabetes, gastrointestinal and hepatic diseases, thermal burns and pulmonary disease.

Rabbit polyclonal anti-Bovine Serum Albumin (BSA)–Agarose reacts with bovine albumin.

Serum albumins are soluble constituents of circulatory system. Bovine serum albumin (BSA) is homologous to human serum albumin (HSA). BSA consists of three homologous domains (I, II, III), that are separated into nine loops by disulfide bonds.

purified BSA from Cohn Fraction V

Heparin-binding Merozoite antigens were detected by heparin-BSA binding assays using rabbit anti-BSAas the primary after plates were incubated with heparin-BSA on merozoite coated plates.

May be used for immunoprecipitation and immunoaffinity purification of Bovine Serum Albumin (BSA) from solutions.

Rabbit Anti-Bovine Albumin (BSA)-Agarose antibody has been used as a negative control in several immunoassays.

Used for immunoprecipitation and immunoaffinity purification of BSA from solutions.
Anti-Bovine Albumin (BSA)-Agarose antibody produced in rabbit has been used in mass spectrometry.

Serum albumin acts as a depot protein.

Suspension in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

Prepared by conjugating the IgG fraction of anti-bovine serum albumin (BSA) to cyanogen bromide-activated agarose.

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