Sepromax® S50 Strong Cation Exchange Resin (50 μm)

Sepromax® S50 is a sulfonic acid-based strong cation exchange resin primarily used for the separation and purification of monoclonal antibodies. Sepromax® S50 features excellent pressure resistance, a pore structure suitable for mass transfer of monoclonal antibody molecules, and excellent hydrophilicity. The Sepromax® S50 resin utilizes "tentacle" surface derivatization technology, which not only has a greater number of effective functional groups than traditional resins, allowing biomolecules to bind more effectively to these functional groups, but also reduces non-specific interactions between biomolecules and the packing substrate, thereby improving the recovery rate of target molecules.

Sepromax® S50 offers excellent protein resolution:
• Higher protein separation compared to similar products
• Resolution remains unchanged with increased flow rate
• Resolution remains unchanged with increased sample loading volume

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Background

Sepromax® IEX is a series of ion exchange packings developed based on PS-DVB microspheres. Its matrix structure is completely different from hydrophilic polysaccharide substrates such as agarose and cellulose. Firstly, it possesses excellent mechanical properties, capable of withstanding pressures up to 10 MPa; secondly, its large 1000 Å pore size ensures the free entry and exit of biomolecules; finally, its unique coating technology imparts sufficient hydrophilicity, guaranteeing excellent biocompatibility.
Sepromax® IEX packings all employ "tentacle" surface derivatization technology, where functional groups are covalently bound to the substrate surface in the form of linear polymer chains. Compared to traditional ion exchange packings that are directly modified on the surface or only use short-chain bound functional groups, Sepromax® IEX not only has a greater number of effective functional groups, but its reduced steric hindrance allows macromolecular proteins, antibodies, viruses, and plasmids to bind more effectively to the packing's functional groups, significantly increasing binding capacity. Furthermore, the "tentacle" structure effectively reduces non-specific interactions between biomolecules and the packing matrix, thereby improving the recovery rate of target molecules.