Albumin from human serum

Albumin is the most abundant protein in blood plasma, produced in the liver.

Albumin is a known carrier of fatty acids (FA). Thus control over specific FA′s for cell culture is important, as different cell lines can differ in their sensitivity to particular fatty acids. Fatty acid-free human serum albumin (HSA) is therefore useful for cell culture studies where specific fatty acid content must be strictly controlled, so that researchers can use particular fatty acids specific to their cell lines. Fatty acid-free albumin also allows for optimal and maximum binding sites for using specific fatty acids in cell culture. The use of FA-free HSA also addresses concerns about endogenous FA′s potentially in non-FA-free HSA.

Albumin is the most copious plasma protein in humans. Albumin turnover is seen in infants with iron deficiency anemia. Serum albumin is a reliable prognostic indicator in liver disease. Oxidative damage of albumin is associated with advanced liver disease.

Albumin is widely used as a blocking agent in immunoassays and immunodetection procedures, and as a carrier protein for dilution of antibodies. Awareness of potential trace endogenous content of globulins / IgG in human serum albumin (HSA) is therefore important, because such trace globulins / IgG may serve as antigens for secondary antibodies in immunodetection work. This product undergoes testing for low globulin content / status as essentially globulin-free.

Albumin from human serum has been used in the preparation of glycated human serum albumin (gHSA) in a glucose solution. It has also been used in the study to estimate the impact of surface nanotopography and chemical composition on blood compatibility.

Albumin was used to test its effect on the in vitro bactericidal activity of cefditoren against penicillin-resistant Streptococcus pneumonia. It has been clinically used in serious and often life-threatening conditions, such as shock and blood loss due to trauma, burns, and surgery. It was used also to test the effect of non-enzymatic glycation on the unfolding of human serum albumin.

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.

View more information on human serum albumin.