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Mouse serum albumin (MSA) is the most abundant protein in mouse plasma, synthesized by hepatocytes and secreted into the bloodstream [1, 11]. Its primary physiological role is the maintenance of colloid osmotic pressure, which is essential for regulating fluid distribution between the intravascular and extravascular compartments [3, 15]. Additionally, MSA functions as a major transport protein, binding and carrying a diverse array of ligands including long-chain fatty acids, bile salts, bilirubin, steroid hormones, and various therapeutic drugs [1, 14]. In drug development, MSA is a critical factor in determining the pharmacokinetic profile of compounds, as its high binding capacity and long half-life—maintained by the neonatal Fc receptor (FcRn) recycling pathway—are often leveraged to improve the delivery and stability of biopharmaceuticals [10, 16]. Pathologically, decreased levels of MSA are indicative of liver dysfunction, nephrotic syndrome, or chronic inflammation, making it a standard biomarker in preclinical and clinical assessments [11, 18].
Reversible binding to specific subdomains (Sudlow sites I and II) and recycling via the neonatal Fc receptor (FcRn) to extend plasma half-life.
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