Albumin from Human

Albumins are a group of simple proteins found in the body fluids and tissues of animals and in some plant seeds. Unlike globulins, albumins have low molecular weights, are soluble in water, are easily crystallized and contain an excess of acidic amino acids. Serum and plasma albumin is carbohydrate-free and comprises 55-62% of the protein present. Due to its high charge to mass ratio albumin binds water, Ca2+, Na+, K+, fatty acids, bilirubin, hormones and drugs. Structurally it is a single polypeptide chain with one free sulfhydryl group on residue no 34 and 17 intrachain disulfide bonds.

The main biological function of albumin is to regulate the colloidal osmotic pressure of blood. Human and bovine albumins contain 16% nitrogen and are often used as standards in protein calibration studies. Due to their free hydrophobic region fatty acid free albumins are used to solubilize lipids in tissue culture, and are also used as blocking agents in Western blots or ELISA applications. Globulin free albumins are suitable for use in applications where no other proteins should be present (e.g., electrophoresis).

Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones, and is vital in regulating the colloidal osmotic pressures of blood. Albumin is also seen to bind to exogenous substances, particularly drugs (e.g., ibuprofen, warfarin), and strongly influence their pharmacokinetics. Oxidative stress leading to changes in the redox state of albumin has widely varied effects on its physiological function.

Each donor unit used in the manufacture of this product was tested by an FDA approved method for the presence of antibody to HIV 1/2, antibody to HCV, HIV-Ag, as well as for the Hepatitis B Surface Antigen (HBsAg), and found to be negative (not repeatably reactive).