| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Magnetic particles, protein G functionalized |
| Concentration | |
| Form | liquid |
| Product Type | |
| Relative Density | |
| Shipping | |
| Storage |
Overview
SuperMag 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. With large surface area, excellent colloidal stability and unique surface coating, SuperMag Protein G Beads exhibit high binding capacity, low non-specific binding and fast magnetic separation.
Key Features
- High binding capacity
- Significantly low non-specific binding
- Fast magnetic separation
Applications
- Cell separation
- Immunoprecipitation
- Surface Functional Group: Protein G
- pH: 6.0 - 8.0 at 25 °C (77 °F)
- Water Solubility: Completely miscible
- Magnetic Content: ~80%
- Chemical Stability: Stable under recommended storage conditions.
- Appearance / Color: brown/black
Physical & Chemical Properties
SuperMag Protein G Beads are hydrophilic superparamagnetic beads (50–200 nm) with Protein G covalently coupled to their surface. Protein G binds specifically to the Fc region of IgG antibodies from human, mouse, rabbit, and many other species, enabling non-covalent yet high-affinity antibody capture without altering the antigen-binding Fab regions.
Protein G has broad species compatibility, with strong binding to human, mouse, rat, rabbit, horse, and cow IgG. It binds IgG1, IgG2, IgG3, and IgG4 subclasses from human sources. Binding affinity varies by species and subclass — consult your antibody supplier's datasheet to confirm Protein G compatibility for your specific IgG.
Protein G binds a broader range of IgG species and subclasses than Protein A, particularly for mouse IgG1 and human IgG3, where Protein A binding is weaker. Choose Protein G for mouse monoclonal antibodies or when working with IgG subclasses that Protein A binds poorly.
Primary applications include immunoprecipitation (IP), co-immunoprecipitation (co-IP), antibody purification from serum or hybridoma supernatants, cell sorting using antibody-coated beads, and magnetic immunoassay development.
Yes — antibody–Protein G interactions are reversible. Standard IgG elution uses low-pH glycine buffer (pH 2.0–3.0) followed by immediate neutralization. Alternatively, Laemmli sample buffer can be used when eluting for SDS-PAGE/Western blot analysis.
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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