Bovine serum albumin (BSA or "Fifth Fraction") is a serum albumin derived from cattle that is valued for its widespread use in biochemical research. As the standard protein concentration in the laboratory, BSA provides a convenient research basis for countless scientists.
BSA's name "Fraction V" comes from the purification method developed by Edwin Cohn, a technique that exploits the soluble properties of plasma proteins to obtain different fractions.
The first commercialization of this purification method originated from the medical production of human albumin, and subsequently this technology was also introduced into the production of BSA. The development of this technology not only improves medical capabilities, but also provides the basis for various experiments in the research community.
The full-length precursor polypeptide of BSA consists of 607 amino acids. After preliminary trimming, the mature BSA protein has 583 amino acids. This gives BSA unique structural properties and the ability to remain stable in a variety of environments.
BSA's physical properties include: molecular weight 66.5 kDa, isoelectric point 4.7, pH 5.2-7 at 25°C, etc.
These properties make BSA indispensable in experiments, and many scientific studies rely on the stability and diverse functions of this protein.
BSA has many important functions in the body. It provides expansion pressure for capillaries and is responsible for transporting fatty acids, bilirubin, minerals and hormones. BSA also has anticoagulant and antioxidant functions.
BSA has different binding sites for long-chain fatty acids in its structure, and can be combined with a variety of substances such as hydrochloric acid, sulfa drugs, etc. to expand its application scope.
In addition, the coexistence of its binding sites with other biomolecules shows the complexity of its role in organisms, providing researchers with more potential research directions.
BSA has a wide range of applications in biochemical experiments, including enzyme-linked immunosorbent assay (ELISA), immunoblotting, immunohistochemistry, etc. Because it does not react significantly, BSA is often used as a blocking agent in immunohistochemistry to reduce non-specific binding.
During the immunohistochemistry process, the specificity of the antibody for the target antigen can be improved through pretreatment with BSA blocking agent.
The use of BSA in these experiments helps to improve signal sensitivity, reduce background noise to a minimum, and provide clearer data for research.
In addition to its applications in standardization and stability, BSA is also used as a nutrient for cell and microbial cultures and to stabilize the activity of some enzymes in restriction enzyme digestion reactions. It is also used to determine the content of other proteins. Due to its lack of impact on the device and its economic efficiency, BSA has almost become a "standard product" in life science laboratories.
BSA is not limited to academia, its applications are still expanding, from the synthesis of nanostructures to the study of the impact of metal ions, BSA is becoming an important cornerstone of biochemical research.
Will one day BSA play a more important role in our lives and become a key ingredient in a wider range of applications?
Facing future research prospects, whether it is the application of new technologies or the deepening of the understanding of BSA, scientists are still exploring its endless potential. If BSA can unlock more mysteries in the biomedical field, what kind of scientific revolution will we face?