Chromatography Resins

Affinity chromatography is a purification technique that utilizes specific interactions for separation. Commonly used affinity resins include Protein A affinity resins for recombinant monoclonal antibody (mAb) purification, immobilized metal ion affinity chromatography resins for His-tagged protein purification, and plasmid affinity resins for plasmid purification, among others.

Ion-exchange chromatography is a purification technique that separates molecules based on charge differences. It can be divided into two types: anion exchange and cation exchange.

Multimodal chromatography utilizes multiple interactions for synergistic separation. As chromatography resins, they are suitable for efficient purification of complex samples.

Hydrophobic interaction chromatography (HIC) is a chromatography technique that exploits the surface hydrophobicity of proteins to bind with ligands on resins under high salt conditions and elute under low salt conditions.

Gel filtration chromatography is a chromatography method that utilizes the molecular sieve effect to separate molecules based on size and shape. It is suitable for desalting, buffer exchange, and molecular weight determination.

Silica-based chromatography resins feature high mechanical strength and excellent separation efficiency, and are widely used in normal-phase, reverse-phase, and hydrophilic interaction chromatography (HILIC). They are commonly used for the purification of GLP-1, peptides, oligonucleotides, antibiotics, and other drugs.

Polymer-based reverse-phase chromatography resins feature a broad pH tolerance range and good chemical stability. They are suitable for the purification of peptides, antibiotics, contrast agents, chemical drugs, and other drugs.