Serum albumin is a crucial protein found in human blood plasma. It is the most abundant protein in human blood, constituting about half of the serum protein. Serum albumin is produced in the liver and plays a vital role in maintaining the colloidal osmotic pressure of blood and in the transportation of various substances, including hormones, fatty acids, and drugs .
Human serum albumin (HSA) is a monomeric protein that is soluble in water. It has a molecular mass of approximately 68 kDa and consists of a single polypeptide chain. The protein is known for its ability to bind to a wide range of endogenous and exogenous substances, which makes it an essential carrier protein in the bloodstream .
The primary functions of serum albumin include:
Serum Albumin Human, Sf9, refers to human serum albumin produced using the Sf9 insect cell line. The Sf9 cell line is derived from the fall armyworm (Spodoptera frugiperda) and is commonly used in biotechnology for the production of recombinant proteins. The use of Sf9 cells allows for the production of glycosylated proteins, which can be important for the proper folding and function of certain proteins .
The production of human serum albumin in Sf9 cells involves the use of recombinant DNA technology. The gene encoding human serum albumin is inserted into a baculovirus vector, which is then used to infect the Sf9 cells. The infected cells produce the recombinant human serum albumin, which can then be harvested and purified using various chromatographic techniques .
The recombinant human serum albumin produced in Sf9 cells is a single, glycosylated polypeptide chain consisting of 597 amino acids. It is fused to a 6 amino acid His Tag at the C-terminus, which aids in the purification process. The protein shows multiple bands between 50-70 kDa on SDS-PAGE under reducing conditions .
Human serum albumin produced in Sf9 cells has several applications in research and biotechnology: