Human Serum Albumin Conjugated to Agarose Beads, High-Capacity, 5 mL – Catalog #B2025631

Human Serum Albumin Conjugated to Agarose Beads – High-Capacity (Catalog #B2025631) is a premium-grade formulation of HSA immobilized on agarose at elevated density, optimized for applications requiring maximum binding capacity and throughput. Supplied as 5 mL of suspension, this conjugate is designed for large-scale protein purification, pharmaceutical screening, and bioaffinity chromatography where sample volume or antigen concentration demands efficient, high-capacity affinity separation. The globular 66 kDa HSA structure features three major binding domains with numerous pockets for small molecules and proteins.

Scientific Overview

Human Serum Albumin (HSA) is the most abundant protein in blood plasma, comprising approximately 50–60% of total plasma proteins. Its 66 kDa globular structure is composed of three homologous domains (I, II, and III), each containing distinct ligand-binding sites. HSA is an exceptional transporter and binder of hydrophobic molecules, including fatty acids (up to ~10 molecules per HSA), hormones, bilirubin, and pharmaceuticals. These multivalent binding properties make HSA an ideal affinity ligand for chromatographic separations and bioanalytical research.

The high-capacity formulation delivers increased HSA loading density per unit of agarose beads, enabling:

• Enhanced binding capacity for large sample volumes
• Faster binding kinetics due to higher HSA concentration
• Greater efficiency in high-throughput applications
• Improved cost-effectiveness for large-scale processing

Key applications include:

• Large-scale affinity chromatography for HSA-ligand enrichment
• Purification of abundant HSA-binding proteins or antibodies
• High-throughput pharmaceutical screening and drug discovery
• Processing of concentrated samples or crude extracts

Usage & Handling Guidance

Store at 2–8°C. Allow beads to warm to room temperature before use. Mix gently to resuspend beads; vigorous vortexing may cause bead aggregation. Avoid repeated freeze–thaw cycles.

• High-capacity workflows: The elevated HSA density supports larger sample volumes and higher antigen concentrations; pre-titrate to determine the optimal bead-to-sample ratio.
• Binding conditions: Incubate at 4°C for maximum selectivity; room temperature permits faster kinetics. Equilibrate beads thoroughly with binding buffer before each use.
• Elution: Standard protocols use 0.1 M glycine pH 2.5, 3 M NaCl, or pH 8–9 buffers; pH neutralization must follow acidic elution immediately.
• Regeneration: Beads support multiple cycles of regeneration and reuse; capacity and binding kinetics remain stable over 10+ cycles with proper technique.

What You Get

• 5 mL of high-capacity human serum albumin conjugated to agarose beads, supplied as a suspension
• Premium-grade affinity support with enhanced binding density
• Optimized for large-scale and high-throughput applications
• For research use only (RUO)

Why Researchers Choose It

• High HSA density enables efficient separation of abundant HSA-binding targets
• Increased binding capacity reduces beads required per reaction, lowering per-assay costs
• Well-established HSA structure and binding properties enable rational experimental design
• Compatible with standard and automated chromatography systems for high-throughput work

Frequently Asked Questions (FAQ)

• What is the difference between standard and high-capacity HSA agarose beads?
  High-capacity formulations feature elevated HSA loading density, providing greater binding capacity per unit of beads. Use high-capacity for larger sample volumes, higher antigen concentrations, or high-throughput applications.
• How many ligand-binding sites does HSA have?
  HSA contains ~10 high-affinity sites for fatty acids and multiple lower-affinity pockets for diverse small molecules. Capacity also depends on conjugation density and your specific ligand.
• Can these beads handle concentrated protein samples?
  Yes. The high-capacity formulation is designed for concentrated samples. Pre-titrate with your sample to find optimal bead:sample ratio to avoid saturation.
• What is typical binding capacity per mL of beads?
  Capacity varies with HSA loading density and the specific ligand. Request a COA/TDS for lot-specific capacity data.
• Are these beads compatible with automated systems?
  Yes. The suspension format works with standard and many automated liquid handlers. Confirm compatibility with your specific equipment before large-scale implementation.

References

• Park J, Kim MS, Park T, Kim YH, Shin DH. Crystal structure of pharmaceutical-grade human serum albumin. Int J Biol Macromol. 2021;166:221-228.
• Catalano C, Lucier KW, To D, Senko S, Tran NL, Farwell AC, Silva SM, Dip PV, Poweleit N, Scapin G. The CryoEM structure of human serum albumin in complex with ligands. J Struct Biol. 2024;216(3):108105.
• Salehi N, Peng CA. Purification of CD47-streptavidin fusion protein from bacterial lysate using biotin-agarose affinity chromatography. Biotechnol Prog. 2016;32(4):949-58.