Human Serum Albumin Conjugated to Agarose Beads, 5 mL – Catalog #B2025623

Human Serum Albumin Conjugated to Agarose Beads (Catalog #B2025623) combines the multifunctional protein-binding properties of human serum albumin (HSA) with the inert, hydrophilic agarose matrix. Supplied as 5 mL of suspension, this conjugate provides a versatile affinity support for protein purification, ligand binding studies, and bioaffinity chromatography. HSA's 66 kDa globular structure contains numerous binding sites for fatty acids, pharmaceuticals, and other small molecules, as well as non-specific protein interactions useful for affinity separation applications.

Scientific Overview

Human Serum Albumin (HSA) is a major blood plasma protein (~66 kDa) produced by the liver. Its structure consists of three homologous domains, each with multiple ligand-binding pockets. HSA serves as a transport protein for fatty acids, hormones, pharmaceuticals, and other hydrophobic molecules in blood, and its multivalent binding properties make it a valuable tool in affinity chromatography and bioanalytical research.

When conjugated to agarose beads, HSA creates a versatile affinity matrix useful for:

• Capturing HSA-binding molecules (fatty acids, drugs, bilirubin)
• Purifying HSA-binding proteins or antibodies
• General protein separation based on affinity interactions
• Studying HSA-ligand interactions and binding kinetics

Key applications include:

• Affinity chromatography for HSA-ligand enrichment
• Purification of HSA-binding proteins or antibodies
• Drug and small-molecule compound screening
• Bioaffinity applications requiring a universal protein carrier

Usage & Handling Guidance

Store at 2–8°C. Allow beads to warm to room temperature before use. Mix gently to resuspend beads; do not vortex. Avoid repeated freeze–thaw cycles.

• Equilibration: Wash beads thoroughly with binding buffer (PBS, TBS, or custom buffer) before each use.
• Binding: Incubate sample with beads at 4°C for enhanced specificity or room temperature for faster kinetics.
• Elution: Use low-pH buffers (0.1 M glycine pH 2.5) or high-salt solutions (3 M NaCl), followed by immediate pH neutralization.
• Regeneration: Beads can be regenerated using standard washing and re-equilibration protocols for multiple reuse cycles.

What You Get

• 5 mL of human serum albumin conjugated to agarose beads, supplied as a suspension
• A versatile affinity support with multiple ligand-binding sites
• Suitable for affinity chromatography and bioaffinity research
• For research use only (RUO)

Why Researchers Choose It

• HSA's multiple binding sites enable diverse separation and purification applications
• Well-characterized structure and binding properties backed by extensive literature
• Compatible with standard chromatography workflows and equipment
• Cost-effective carrier protein for affinity-based research and drug screening

Frequently Asked Questions (FAQ)

• What can I bind to HSA agarose beads?
  HSA binds many small molecules (fatty acids, drugs, hormones), as well as proteins with affinity for albumin. Specificity depends on binding pocket chemistry and buffer conditions.
• How is HSA-agarose different from protein A or protein G?
  HSA is a general carrier protein with broad ligand-binding properties, while protein A and G are highly specific for the Fc region of antibodies. HSA is preferred for non-antibody applications.
• What elution pH and salt are recommended?
  Standard protocols use 0.1 M glycine pH 2.5, 3 M NaCl, or pH 8–9 buffers depending on ligand stability. Optimize for your specific application.
• Can I use these beads for multiple cycles?
  Yes. Regenerate by washing with elution buffer and re-equilibrating with binding buffer. Beads typically support 5–10+ reuse cycles with proper care.
• Are there lot-specific binding capacity data available?
  Yes. Request a COA/TDS for capacity information for your specific lot; binding capacity varies with HSA loading density.

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.
• Chubarov A, Spitsyna A, Krumkacheva O, Mitin D, Suvorov D, Tormyshev V, Fedin M, Bowman MK, Bagryanskaya E. Reversible Dimerization of Human Serum Albumin. Molecules. 2020;26(1).
• 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.