
Protrin G Affinity Resin
Protrin G Affinity Resin
Protein G Affinity Chromatography Resin Native Protein G is a bacterial cell surface protein originally isolated from Lancefield groups C and G Streptococcus species. It binds immunoglobulin G (IgG) via highly specific recognition of the antibody Fc region, and is widely used for antibody purification workflows. Compared to Protein A, Protein G exhibits broader species cross-reactivity and superior coverage of diverse IgG subclasses.
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Protein G Affinity Chromatography Resin Native Protein G is a bacterial cell surface protein originally isolated from Lancefield groups C and G Streptococcus species. It binds immunoglobulin G (IgG) via highly specific recognition of the antibody Fc region, and is widely used for antibody purification workflows. Compared to Protein A, Protein G exhibits broader species cross-reactivity and superior coverage of diverse IgG subclasses. This commercial variant has been rationally engineered to deliver high caustic (alkali) stability for extended operational use.
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Protein A Affinity Resin
Protein A Affinity Chromatography Resin This resin leverages specific binding interactions between its immobilized Protein A ligand and the Fc region of antibodies to achieve rapid capture and purification of target antibodies. Through targeted protein engineering of the Protein A ligand, the resin demonstrates high tolerance to 0.5–1.0 M sodium hydroxide (NaOH), which greatly extends its operational lifespan.
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Mild Elution Protein A Affinity Resin
Mild-Elution Protein A Affinity Chromatography Resin Developed via targeted engineering and optimization of the Protein A ligand, this resin elevates its elution pH to 5.0. It resolves the well-documented purification bottleneck for low-pH-sensitive antibodies, and is fully compatible with purification of complex bispecific antibody (bsAb) modalities.
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Protein L Affinity Resin
Protein L Affinity Chromatography Resin This resin enables rapid capture and purification of target antibodies via the highly specific binding interaction between its immobilized Protein L ligand and the kappa (κ) light chain of immunoglobulins.
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