Human IgM Conjugated to Agarose Beads, 2 mL – Catalog #B2025621

Human IgM Conjugated to Agarose Beads (Catalog #B2025621) combines the immunological specificity of human Immunoglobulin M with the solid support matrix of agarose beads. Supplied as 2 mL of suspension, this conjugate provides a convenient substrate for affinity chromatography, antigen capture, and immunoprecipitation protocols. IgM antibodies are ideal for detecting multiple antigens simultaneously due to their pentameric structure and high avidity.

Scientific Overview

Immunoglobulin M (IgM) is a pentameric antibody composed of five Fab units joined by a J chain, making it the largest antibody with a molecular weight of approximately 900 kDa. IgM is the first antibody produced during the primary immune response and is particularly effective at complement activation and agglutination of antigens. Its large size and multiple binding sites provide high avidity and the ability to cross-link multiple antigens simultaneously, making it a powerful tool for immunological research.

Agarose is an inert, hydrophilic polysaccharide polymer ideal for affinity chromatography and protein purification. When human IgM is conjugated to agarose beads, it creates a stable, reusable affinity support for capturing specific antigens and immune complexes from complex mixtures.

Key applications include:

• Affinity chromatography for antigen capture and purification
• Immunoprecipitation of specific antigens and immune complexes
• Isolation of complement-bound antigens
• Antibody purification and selection

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 before each use.
• Binding: Incubate sample with beads at 4°C for enhanced specificity, or room temperature for faster kinetics.
• Elution: Use standard immunoglobulin elution conditions (low pH buffer, 0.1 M glycine pH 2.5, or high salt) followed by immediate pH neutralization.
• Regeneration: Beads can be regenerated multiple times using appropriate washing and re-equilibration buffers.

What You Get

• 2 mL of human IgM conjugated to agarose beads, supplied as a suspension
• Ready-to-use affinity support for antigen capture and purification
• Stable, reusable affinity matrix for multiple cycles
• For research use only (RUO)

Why Researchers Choose It

• Pentameric structure and high avidity for sensitive antigen detection and capture
• Effective at complement activation, useful in immunological studies
• Inert agarose matrix suitable for both batch and column chromatography
• Easy handling and magnetic separation compatibility with standard lab workflows

Frequently Asked Questions (FAQ)

• What is the difference between IgG and IgM?
  IgG is a monomeric antibody present in secondary immune responses, while IgM is a large pentameric antibody produced first in the primary response. IgM has higher avidity and is more efficient at complement activation.
• Can I regenerate these beads?
  Yes. After elution, wash thoroughly with elution buffer and re-equilibrate with binding buffer. Beads can typically be used for multiple cycles, though binding capacity may decrease over time.
• What buffers should I use for binding and elution?
  Binding buffers typically include PBS, TBS, or custom buffers. For elution, standard protocols use 0.1 M glycine pH 2.5, 3 M NaCl, or other low-pH buffers depending on your antigen stability.
• How do I prevent non-specific binding?
  Pre-block beads with BSA or other carrier proteins, and optimize salt concentration and pH in your binding buffer.
• Can I use these with magnetic separation equipment?
  Confirm with us whether your batch is magnetic; some formulations are available with magnetic cores for convenient separation.

References

• Yang S, Zhao LC, Guo FZ, Xu HS, Huang MM, Fei H. Evolution of immunoglobulin M (IgM) structure and function in vertebrates: A comprehensive review. Fish Shellfish Immunol. 2025;166:110635.
• Buchner J, Sitia R, Svilenov HL. Understanding IgM Structure and Biology to Engineer New Antibody Therapeutics. BioDrugs. 2025;39(3):347-357.
• 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.