What is the use of 22% bovine albumin in the test procedure?

Bovine Albumin is primarily used to enhance the reactivity of blood group antibodies, either in direct agglutination tests or indirect antiglobulin test.

What is 22% bovine albumin?

Bovine albumin 22% contains bovine serum albumin as its reactive component. Bovine albumin 22% is used in blood group serology as an intensification and suspension medium. The reagent is suitable for antibody titration.

What is bovine serum albumin solution?

Bovine serum albumin (also known as BSA or “Fraction V”) is a serum albumin protein isolated from cows. In molecular biology, BSA is used to stabilize some restriction enzymes during digestion of DNA and to prevent adhesion of the enzyme to reaction tubes, pipet tips, and other vessels.

What is bovine serum albumin used for?

Bovine Serum Albumin (BSA) is used in a variety of laboratory applications including its function as a protein concentration standard, its function as a cell nutrient and its ability to stabilize enzymes during restriction digest.

Is Bovine Serum Albumin infectious?

Precautions: Although the bovine serum has been tested for infectious diseases and found negative, the reagent cannot be assumed to be free from infectious agents. However, should be handled cautiously as potentially infectious. Protective clothing should be worn when handling the reagent, such as disposable gloves.

Where is albumin made in the body?

Synthesis of albumin takes place in the liver, after which it is excreted into the bloodstream. Albumin can be found in the bloodstream, interstitial space, as well as other fluids. When found in other fluids in large concentrations, such as in ascites or urine, it is often an indication of underlying pathology.

What is bovine serum albumin made of?

Bovine serum albumin (BSA) BSA is described as a globular non-glycoprotein with a molecular weight close to 66 430. It is made of 583 amino acid residues and has 17 cystine residues (8 disulphides bridges and 1 free thiol group) (Carter and Ho 1994, Hirayama et al. 1990).

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