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AlbumiNZ™ Bovine Serum Albumin (BSA), MP Biomedicals

Supplier: E. Becker & Co. GmbH
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0219989610 0219989625 0219989680 0219989690 0219989691 0219989650
IC219989610EA 87.24 USD InStock
IC219989610 IC219989625 IC219989680 IC219989690 IC219989691 10273-262
AlbumiNZ™ Bovine Serum Albumin (BSA), MP Biomedicals
Proteins and Peptides
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.

  • Stem Cell Grade
  • Presentation: Off-white to Light Yellowish to Brown Powder
  • Isoelectric point (pl): Endogenous material- 4.7, 4.9; Fatty acid depleted- 5.3(In Water at 25 °C)
  • Moisture: ≥5%

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.

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.

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 readily soluble in water and can only be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of albumin is very good (especially if the solutions are stored aliquoted and frozen). Albumin is readily coagulated by heat. When heated to 50 °C or above, albumin quite rapidly forms hydrophobic aggregates which do not revert to monomers upon cooling. Dissolves completely in 20 min at 20-25 °C (20%).


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