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Serum Albumin

Serum albumin plays a crucial role in maintaining blood oncotic pressure and transporting various compounds throughout the body, including lipids, bile pigments, hormones, and metal ions. Mammalian albumins have many applications in research and diagnostics and human serum albumin (HSA) is produced in large quantities for treating conditions such as hypovolemic shock and hypoalbuminemia.

While HSA is traditionally produced from pooled human plasma using cold ethanol precipitation (the Cohn Process), chromatographic methods are increasingly being adopted either as an alternative or in addition to the Cohn Process to enhance purities and recoveries. Astrea Bioseparations supplies high-performance chromatography resins that are optimized for the capture and purification of serum albumin from various sources.

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    Capture and purification of serum albumin using Mimetic Blue® SA resins

    Mimetic Blue® SA resins, developed through extensive collaboration with albumin producers, feature the specially optimized Mimetic Blue® SA ligand. This ligand binds selectively to human serum albumin (HSA) and other mammalian serum albumins from plasma and albumin-containing plasma fractions, ensuring high recoveries of purified albumin. The resins are exceptionally durable, exhibit minimal ligand leakage, and support high flow rates, low back pressures, and long operational lifetimes. They can be cleaned and sanitized using 0.5 or 1.0M NaOH. HSA is bound at neutral to slightly acidic pH levels and eluted at mildly alkaline pH in the presence of salt (NaCl) and/or sodium caprylate. Manufactured in large batch sizes, Mimetic Blue® SA resins are non-toxic affinity resins with a proven track record in the production of therapeutic serum albumins.

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    Purification of serum albumins using PuraBead® IEX

    Both anion and cation exchange chromatography are commonly used for serum albumin purification. Anion exchange chromatography targets proteins with isoelectric points lower than that of albumin, while cation-exchange chromatography is used to remove proteins with isoelectric points higher than albumin. Additionally, anion exchange chromatography utilizing DEAE PuraBead® P6HF can be applied in a flow-through mode following capture with Mimetic Blue® SA resin to eliminate residual plasma proteins and other impurities, thereby producing high-purity human serum albumin. All PuraBead® ion exchange resins are designed for ease of cleaning, fully alkali-stable, and composed of near-monodisperse chromatographic materials that ensure high binding capacities, rapid flow rates, low back pressures, and extended operational lifetimes. 

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