Description
Anti-IgM Latex Particles (High Specificity)
| Catalog number: | B2010396 |
| Lot number: | Batch Dependent |
| Expiration date: | Batch Dependent |
| Amount: | 1 mL |
| Concentration: | 0.5% solid suspension |
| Supplied as: | Liquid Suspension |
| Appearance: | White particle suspension |
| Storage: | 28C |
| Keywords: | anti-IgM-latex, anti IgM latex, anti human IgM latex beads |
| Grade: | Biotechnology grade. All solid components are highly pure (95%). Solutions made with Type I ultrapure water (resistivity>18 Mcm), filtered through 0.22 m. |
Anti-IgM Latex Particles are designed for high-specificity capture of human IgM antibodies in immunoassay, purification, and depletion workflows. Each particle is composed of ~0.35 m latex beads conjugated to a polyclonal mix of anti-human IgM antibodies, forming a stable white suspension in ultrapure water. This reagent is ideal for researchers working in immunology, autoimmunity, and diagnostic assay development, offering robust performance across ELISA, biosensor calibration, and multiplex detection platforms.
These particles enable efficient one-step capture of IgM-class antibodies, antigens, and immune complexes. Their small size and high surface area allow for rapid binding kinetics, while the latex matrix ensures stability and reproducibility across a range of pH and temperature conditions. Recovery is straightforward via centrifugation, making them compatible with both manual and automated platforms.
Anti-IgM Latex Particles are particularly useful in studies of rheumatoid factor detection, B-cell profiling, and immunoglobulin purification. Their specificity supports applications in post-rituximab monitoring, FcR binding assays, and IgM glycosylation analysis. The reagent is supplied as a 0.5% solid suspension in 1 mL volume and should be stored at 28C for optimal performance.
Key benefits:
- Latex particles (~0.35 m) conjugated to polyclonal anti-human IgM antibodies
- High specificity and stability for IgM-targeted capture
- Compatible with purification, depletion, and assay development workflows
- Recoverable by centrifugation; supplied in ultrapure water
- Biotechnology grade; filtered through 0.22 m membranes
Products are for in vitro research use only (RUO).
References
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- Nyamboya RA, Sutton BJ, Calvert RA. Mapping of the binding site for FcR in human IgM-Fc. Biochim Biophys Acta Proteins Proteom. 2020 Jan;1868(1):140266.
- Kridin K, Ahmed AR. Post-rituximab immunoglobulin M (IgM) hypogammaglobulinemia. Autoimmun Rev. 2020 Mar;19(3):102466.
- Hennicke J, Reinhart D, Altmann F, Kunert R. Impact of temperature and pH on recombinant human IgM quality attributes and productivity. N Biotechnol. 2019 May 25;50:2026.
- Lloyd KA, Wang J, Urban BC, Czajkowsky DM, Pleass RJ. Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor. Sci Rep. 2017 Feb 23;7:42989.
- Chinnadayyala SR, Park J, Abbasi MA, Cho S. Label-free electrochemical impedimetric immunosensor for sensitive detection of IgM rheumatoid factor in human serum. Biosens Bioelectron. 2019 Oct 15;143:111642.
- Reese H, Bordelon T, Shanahan C, Crapanzano M, Sly J, Menegatti S. Novel peptoid-based adsorbents for purifying IgM and IgG from polyclonal and recombinant sources. J Chromatogr B Analyt Technol Biomed Life Sci. 2020 Jan 15;1137:121909.
- Akhouri RR, Goel S, Furusho H, Skoglund U, Wahlgren M. Architecture of Human IgM in Complex with P. falciparum Erythrocyte Membrane Protein 1. Cell Rep. 2016 Feb 2;14(4):723736.
- Monica TJ, Williams SB, Goochee CF, Maiorella BL. Characterization of the glycosylation of a human IgM produced by a human-mouse hybridoma. Glycobiology. 1995 Mar;5(2):175185.
- Miyazaki T, Yamazaki T, Sugisawa R, Gershwin ME, Arai S. AIM associated with the IgM pentamer: attackers on stand-by at aircraft carrier. Cell Mol Immunol. 2018 Jun;15(6):563574.
