| Field | Specification |
|---|---|
| Alternative Names | Magnetic particles, protein G functionalized |
| Concentration | |
| Form | liquid |
| Product Type | |
| Relative Density | |
| Shipping | |
| Storage |
Overview
MonoMag Protein G Beads are Protein G conjugated magnetic beads. The Protein G is covalently coupled to their surface makes most of the binding sites sterically available for binding of IgG. Attribute to their uniform size, narrow size distribution, short magnetic separation time, and unique surface coating, Mono Mag exhibit significantly low non-specific binding and fast magnetic separation.
Key Features
- Narrow size distribution, CV≤5%
- Significantly low non-specific binding
- Fast magnetic separation
Applications
- Immunoprecipitation
- Cell separation
Physical & Chemical Properties
- Surface Functional Group: Protein G
- pH: 6.0 - 8.0 at 25 °C (77 °F)
- Water Solubility: Completely miscible
- Magnetic Content: ~35% (1 µm), ~25% (3 µm)
- Chemical Stability: Stable under recommended storage conditions.
- Appearance / Color: brown/black
MonoMag Protein G Beads are monodisperse superparamagnetic beads (1 µm, 3 µm; CV ≤ 5%) with Protein G covalently coupled to their surface. The uniform bead size enables consistent and reproducible antibody capture kinetics for immunoprecipitation, antibody purification, and assay applications.
Protein G binds broadly to IgG from human, mouse, rat, rabbit, goat, bovine, and other species. It shows strong affinity for mouse IgG1 and human IgG3 — subclasses that Protein A binds poorly. Specific subclass binding affinities vary by species; confirm Protein G compatibility using the antibody supplier's datasheet.
Use low-pH elution buffer (e.g., 100 mM glycine, pH 2.0–2.5) and collect the eluate immediately into a neutralization buffer (e.g., 1 M Tris-HCl, pH 9.0). For SDS-PAGE or Western blotting, Laemmli sample buffer (with boiling) can be used to denature and elute the captured antibody–antigen complex.
The 1 µm size provides more surface area per mg and is recommended for solution-phase immunoprecipitation where maximizing binding capacity is important. The 3 µm size enables faster magnetic separation and may be preferable when separation speed matters more than total binding capacity.
Beads may be regenerated by washing with PBS and re-blocking with BSA, but re-use is generally not recommended for quantitative assays due to potential loss of Protein G activity or carryover contamination between samples.
The following customization and add-on services are available for this product through the supplier. For inquiries and pricing, contact support@biohippo.com.
Customization Options
- Custom Particle Sizes: Magnetic beads in sizes beyond the standard catalog range, with narrow size distribution from nanometers to micrometers, can be manufactured for specific assay geometries and separation requirements.
- Custom Surface Functionalization: Customized surface coatings and functional group densities are available to optimize binding capacity, non-specific binding profiles, and colloidal stability for specific applications.
- Custom Conjugation Service: Pre-conjugated magnetic bead–antibody, bead–protein, or bead–streptavidin conjugates prepared using your supplied biomolecule are available. The supplier specializes in bioconjugation chemistry across magnetic beads, iron oxide nanoparticles, quantum dots, and latex beads.
- Assay Development Services: Support for magnetic bead-based chemiluminescent assay, lateral flow immunoassay, and custom immunoassay platform development is available.
- Bulk & OEM Manufacturing: OEM magnetic beads for chemiluminescent assay, lateral flow immunoassay, CTC (circulating tumor cell) isolation for liquid biopsy, and T-cell isolation and activation for immunotherapy are available at production scale.
To inquire about customization options, request a quote, or discuss OEM manufacturing, contact support@biohippo.com.
- Jensen P et al. (2021). Improved Immunoprecipitation to Mass Spectrometry Method for the Enrichment of Low-Abundant Protein Targets. Methods Mol Biol. DOI: 10.1007/978-1-0716-1186-9_14 PMID: 33420993
- Guo L et al. (2026). Thread-Designed Vascular Scaffold with Magneto-Optical Probes Capture and Elimination of Circulating Tumor Cells In Vivo. Adv Mater. DOI: 10.1002/adma.202516675 PMID: 41546398
- Zhang C et al. (2026). Multivalent capture of circulating tumor cells using tetrahedral DNA framework-targeted nanomagnetic beads integrated microfluidic device. Colloids Surf B Biointerfaces. DOI: 10.1016/j.colsurfb.2025.115142 PMID: 40972107
- Zeng T et al. (2025). Integrated Biomimetic Platform for Enhancing the Efficient Capture and Visual Identification of Circulating Tumor Cells. Anal Chem. DOI: 10.1021/acs.analchem.5c06259 PMID: 41384307
- Su LT et al. (2025). A Dual Nano-Signal Probe-Based Electrochemical Immunosensor for the Simultaneous Detection of Two Biomarkers in Gastric Cancer. Biosensors (Basel). DOI: 10.3390/bios15020080 PMID: 39996982
- Faresjö M (2026). A Useful Guide for Analysis of Biomarkers in Cancer by Fluorochrome (Luminex) Technique. Methods Mol Biol. DOI: 10.1007/978-1-0716-4901-5_1 PMID: 41478962
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