Human Serum Albumin
Human Serum Albumin - Related Videos
08:26
Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
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2018
The protocols for studying the binding of gold cations (Au(III)) to various conformations of bovine serum albumin (BSA) as well as for characterizing the conformational dependent unique BSA-Au fluorescence are presented.
06:44
Isolation of Small Noncoding RNAs from Human Serum
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Cited by 13 •
2014
This protocol describes a method for extracting small RNAs from human serum. We have used this method to isolate microRNAs from cancer serum for use in DNA arrays and also singleplex quantitative PCR. The protocol utilizes phenol and guanidinium thiocyanate reagents with modifications to yield high quality RNA.
09:23
Using Extraordinary Optical Transmission to Quantify Cardiac Biomarkers in Human Serum
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Cited by 2 •
2017
This work describes a nanoimprinting lithography method to fabricate high-quality sensing arrays that work on the principle of extraordinary optical transmission. The biosensor is low-cost, robust, easy to use, and can detect cardiac troponin I in serum at clinically relevant concentrations (99th percentile cutoff ∼10-400 pg/mL, depending on the assay).
05:33
A Microneutralization Assay to Measure Neutralizing Antibody Titers in Human Serum
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2025
This video demonstrates Microneutralization assays to measure neutralizing antibodies using Madin-Darby Canine Kidney cells overexpressing α2,6-linked sialic acid in human sera. This assay is often used for influenza human...
02:55
Determining the Role of Vitronectin in Bacterial Resistance to Bactericidal Activity of Human Serum
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2025
This video demonstrates the role of vitronectin, a human serum glycoprotein, on bacterial resistance. Antibodies in the serum interact with bacterial surface proteins, activating complement proteins and forming the membrane attack complex, causing bacterial cell lysis. Vitronectin binding on bacterial membrane protein prevents the membrane attack complex formation, resulting in bacterial survival.
FAQs
Human serum albumin contains multiple sites that bind fatty acids, hormones, bilirubin, metal ions, and many drugs reversibly. This arrangement allows these molecules to associate with the protein during circulation and then dissociate, making albumin relevant to studies of protein-ligand interactions. The same binding behavior helps explain its importance in examining how drugs are carried through blood.
Albumin contributes to colloid osmotic pressure, a property that helps maintain fluid distribution within blood plasma. Its abundance makes this function biologically important for plasma homeostasis, the maintenance of stable internal conditions. In biology, examining this role connects protein concentration and plasma behavior with the broader regulation of fluid balance in the circulation.
HSA is synthesized primarily by the liver, linking hepatic protein production to the composition and function of blood plasma. This origin matters when researchers study plasma homeostasis because albumin must be present in circulation to support colloid osmotic pressure and molecular transport. It also provides biological context for investigating how the liver contributes to systemic stability.
Studies of HSA-ligand interactions can reveal how fatty acids, hormones, bilirubin, metal ions, and drugs associate with a major plasma transport protein. Because the interactions are reversible, research can focus on binding behavior rather than permanent attachment. These findings help clarify molecular transport in blood and support analysis of how albumin may influence drug distribution.
Because HSA binds many drugs reversibly, it is relevant to research on drug distribution through the circulation. Investigators can examine how association with albumin relates to the movement of drug molecules in blood. This perspective connects protein-ligand interaction studies with biomedical questions about how drugs are transported after entering the bloodstream.
Human serum albumin supports drug formulation, diagnostics, and engineered delivery systems because its stability and natural transport function are useful biomedical features. These applications draw on the same biological capabilities studied in plasma, while applying them to designed biomedical systems. Thus, HSA links fundamental protein biology with practical research and development.