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Human Serum Albumin （HSA） is a multifunctional, non-glycosylated, negatively charged plasma protein synthesized primarily in the liver. It is considered a major acute-phase protein with a negative charge. HSA plays a pivotal role in maintaining colloidal osmotic pressure, which can influence microvascular integrity and various aspects of inflammatory pathways, including neutrophil adhesion and cellular signaling activities. HSA is a single-chain polypeptide consisting of 585 amino acid residues, with a molecular weight of approximately 66 kDa. It contains 17 disulfide bonds, which fold the entire peptide chain into three similar domains, each composed of three similar loops. HSA has one free thiol group and one tryptophan residue. Human Serum Albumin （HSA） is the most abundant protein in human plasma, accounting for about 40% to 60% of the total protein content. It is synthesized exclusively in the liver by hepatocytes and is rapidly secreted into the bloodstream, with very little storage in the liver. HSA represents half of the plasma's total protein content, with concentrations ranging from 3.5 g/dL to 5 g/dL in healthy individuals. The liver produces approximately 10 to 15 grams of albumin per day, which constitutes nearly 10% of all protein synthesis in the liver.