In the field of life sciences, bovine serum albumin (BSA or "Fraction V") plays a vital role. The protein is derived from bovine serum and was originally isolated based on Edwin Cohen's purification method, which exploited the different solubility properties of plasma proteins. His technique separates the proteins in plasma into several "fractions" by adjusting solvent concentration, pH, salt concentration and temperature, with albumin being the fifth fraction. BSA is not only widely used in research, but also plays a role in medical applications that cannot be underestimated.
Bovine serum albumin can provide cells with essential nutrients, support their growth and division, and is one of the core components of cell culture.
The complete precursor polypeptide of BSA consists of 607 amino acids, but after processing it becomes a mature protein consisting of 583 amino acids. This protein has three homologous but structurally different domains, namely I, II, and III, each of which can be further divided into two subdomains, A and B. The molecular weight of BSA is about 66.5 kDa, and its isoelectric point is 4.7 in water at 25°C. When the pH rises to 5.2-7, the stability of this protein decreases, showing a special property design that makes it different It can work in any environment.
BSA, like other serum albumins, is essential for maintaining the colloid osmotic pressure in capillaries. It is able to transport fatty acids, bilirubin, minerals and hormones, and also has anticoagulant and antioxidant functions. Another feature of BSA is its ability to bind a variety of substances, including antibiotics and certain drugs, which enables it to act as a stabilizer in many biochemical reactions.
BSA's benefits in cell culture include serving as a nutrient source and blocking agent, improving antibody affinity, and enhancing the reproducibility of research results.
BSA is widely used in several biochemical experiments, such as enzyme-linked immunosorbent assay (ELISA), immunoblotting, and immunohistochemistry. Due to its high stability and inertness, BSA is often used as a blocking agent to help improve the specificity of antibodies and antigens and reduce background noise, thereby obtaining a more accurate signal. This, coupled with BSA's continued supply and affordability, makes it an ideal choice for researchers conducting experiments.
In addition to its use in immunoassays, BSA is also used as a nutrient component for cell and microbial culture. It can improve the stability of certain enzymes during DNA digestion, preventing them from sticking to reaction tubes and pipettes, making the experimental process smoother. It is also relatively easy to use BSA to determine the amount of other proteins, and researchers often use the Bradford protein assay for comparative analysis.
BSA is also one of the main components of fetal bovine serum, and the use of fetal bovine serum makes cell culture more common and reliable. With the development of biotechnology, BSA not only serves as a carrier, but also can provide valuable insights in some studies on gene synthesis and the role of metal ions. Its versatility has helped researchers achieve important breakthroughs in multiple biological fields, making it a must-have in many laboratories.
ConclusionThe multiple functions of bovine serum albumin and its importance in biological sciences demonstrate its value and potential. As research continues to deepen, the application scope of BSA will continue to expand, leading the scientific community to explore new possibilities. So, how will future biotechnologies use BSA to further push the boundaries of science?