Bovine serum albumin (BSA or "Fraction V") is a protein extracted from bovine serum and is widely used in laboratories as a standard for protein concentration. The "Fraction V" in the name actually comes from the fractional purification technique first used by Edwin Cohn in the 1940s, which separates the different solubility characteristics of plasma proteins and adjusts them by varying the solvent concentration. , pH, salt concentration and temperature to obtain the most components. Initially, human albumin was used commercially earlier, but the technology was later introduced to the production of bovine serum albumin.
The precursor polypeptide of BSA consists of 607 amino acids, but during the secretion process, the 18 amino acid signal peptide at the front N-terminus is removed and the mature BSA protein finally contains 583 amino acids.
BSA's physical properties include a high molecular weight of 66,463 Da and an isoelectric point of 4.7 in water at 25 °C.
BSA plays multiple roles in the body, including providing turgor pressure in capillaries and transporting fatty acids, bilirubin, minerals and hormones. In addition, BSA can act as an anticoagulant and antioxidant, which makes it essential in many biochemical experiments.
Specifically, there are about six long-chain fatty acid binding sites on BSA, of which the three strongest ones are scattered in different domains.
BSA plays an important role in many biochemical applications, especially in enzyme-linked immunosorbent assay (ELISA), immunoblot and immunohistochemistry. Since BSA itself is a small, stable, and moderately non-reactive protein, it is often used as a blocking agent in immunohistochemistry. In this process, tissue sections are incubated with BSA blocking agent to cover nonspecific binding sites, thereby improving the antibody's ability to bind to a specific antigen.
BSA is also used as a nutrient for cell and microbial culture and to stabilize some enzymes during restriction enzyme digestion.
During antibody detection, the blocking effect of BSA can not only reduce background noise, but also help improve the sensitivity of detection. By binding BSA to nonspecific binding sites, these interferences are minimized and the best signal-to-noise ratio can be achieved.
In addition, BSA's low cost and easy purification make it an important and economical material in scientific research.
With the continuous advancement of science and technology, the potential of BSA will be further utilized, for example in the synthesis of nanostructures and metal ion toxicity testing. These innovations can provide more solutions and opportunities in future biomedical research.
BSA is not only a research tool, but also quietly influences a wide range of experimental results and scientific progress.
Will BSA's hidden function in science change your perception of other laboratory reagents?