Pre-packed Columns

Affinity chromatography is based on the principle of specific and reversible binding between biological macromolecules and the functional groups (ligands) of affinity chromatography resins. These resins are prepared by covalently immobilizing ligands on the surface of the matrix. This reversible binding relies primarily on the recognition of the spatial structure of the ligand by biological macromolecules. Commonly used bioaffinity types include enzyme–substrate, substrate analogs, inhibitors, activators, cofactors, antibody–antigen, hormone–receptor protein, carrier proteins, lectin–polysaccharide, glycoproteins, cell surface receptors, nucleic acid–complementary nucleotide sequences, histones, and nucleic acid-binding proteins.

Ion-exchange chromatography is based on the reversible binding and dissociation between ionizable sample components and ions of the same charge on the ligands of ion-exchange chromatography resins, thereby separating components that differ in the type, amount, and distribution of their surface charges. The ligands of ion-exchange chromatography resins consist of one or more ionizable groups, such as quaternary ammonium, tertiary amine, sulfonate, and carboxyl groups. NanoMicro offers multiple series of ion-exchange chromatography resins based on monodisperse polymer microspheres and polydisperse polysaccharide microspheres to meet various application needs, including capture, intermediate purification, polishing, and sample analysis.

Multimodal chromatography is a chromatography mode that combines multiple chromatography principles, with common combinations such as ion exchange plus hydrophobic interaction, and ion exchange plus hydrophobic interaction plus size exclusion. In multimodal chromatography, two or more chromatography modes work together synergistically. This mode broadens and enriches the separation and purification methods for biological macromolecules, enhances salt tolerance, provides more selective combinations for chromatographic separation, and creates more possibilities for chromatographic separation and purification.

Hydrophobic interaction chromatography (HIC), similar to reverse-phase chromatography (RPC), is a method for separating biological macromolecules based on differences in their surface hydrophobicity. The hydrophobic ligands of HIC resins bind reversibly with the hydrophobic molecules or groups of sample components. Because sample components differ in hydrophobicity, they bind to the ligands with different strengths, and are therefore separated by elution under different conditions. Common ligands for HIC include phenyl, butyl, octyl, and ether groups, while common ligands for RPC include C18, C8, and C4. The ligand hydrophobicity and ligand density of HIC resins are generally lower than those of reverse-phase chromatography.

Gel filtration chromatography, also known as size exclusion chromatography or molecular sieve chromatography, is a chromatography method that separates and purifies molecules based on differences in their size and shape. Gel permeation chromatography resins are inert substances with porous network structures, typically cross-linked polysaccharides (such as dextran or agarose), which separate the components of a mixture according to their molecular size. Generally, larger molecules do not enter the interior of the resin, or enter it but travel a shorter path, and are therefore eluted first; smaller molecules enter the resin and travel a longer path, and are therefore eluted later.

Premium column tubes and accessories, designed to be used with chromatography resins.