AlbumiNZ Low Endo BSA, 100g

Bovine albumin is a single polypeptide chain consisting of approximately 583 to 595 amino acid residues and no carbohydrates. At pH 5-7 it contains 17 intrachain disulfide bridges and 1 sulfhydryl group. Albumin binds water, Ca2+, Na+, and K+. Due to a hydrophobic cleft, albumin binds fatty acids, bilirubin, hormones and drugs. The main biological function of albumin is to regulate the colloidal osmotic pressure of blood and, to a lesser degree, to provide cellular nutrition. Human and bovine albumins contain 16% nitrogen and are often used as standards in protein calibration studies . Albumin is used to solubilize lipids, stabilize protein solutions, and is also used as a blocking agent in Western blots or ELISA applications. Globulin free albumins are suitable for use in applications where no other proteins should be present such as electrophoresis. Albumin loses its helical structure rapidly in 2-4 M urea and 4 M guanidinium chloride. The unfolding is reversible, even, to some extent, after concomitant reduction of all disulfide bonds. Reduced albumin can reform into structures capable of binding antibodies and other ligands. Formation of SS bonds is rapid but the return of native structure is slow and some wrong disulfide pairings may persist. After oxidation of the cystine bridges, however, native structure is irreversibly lost. Albumins are a group of acidic proteins which occur in the body fluids and tissues of mammals and in some plant seeds. Serum and plasma albumin is carbohydrate-free and comprises 55-62% of the protein present. However, only about 40% of the total albumin in the body is in the circulating plasma at one time with the remainder being in extracellular spaces with which there is, in general, equilibration about every 24 hours.

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