Chelating Agarose (IDA) 6FF

Immobilized Metal Ion Affinity Chromatography (IMAC) is a widely used technique for the purification of proteins and peptides. It relies on the specific interactions between certain amino acid side chains—primarily histidine, and to a lesser extent, cysteine and tryptophan—and transition metal ions such as Zn²⁺, Ni²⁺, Cu²⁺, or Co²⁺. These metal ions are chelated by ligands, which are covalently attached to an insoluble polymer matrix, typically agarose.

The strength of interaction between the immobilized metal ions and a given protein or peptide depends on the type, number, and spatial distribution of relevant side chains, as well as on the nature of the metal ion itself. Chromatographic conditions, including pH, salt type and concentration, and the presence of specific additives, can also significantly influence binding affinity. In recent years, IMAC has become increasingly important for the purification of recombinant proteins carrying histidine tags, and it is now regarded as a key tool in modern protein purification workflows.

MCE Chelating Agarose (IDA) 6FF is prepared by covalently coupling tridentate iminodiacetic acid (IDA) to an agarose matrix. It features high binding capacity, excellent specificity, and superior ligand stability. The resin allows flexible chelation with metal ions such as Zn²⁺, Ni²⁺, or Cu²⁺, and is suitable for the purification of His-tagged recombinant proteins expressed in bacterial, mammalian, insect, and baculovirus systems.

This product is a chelating resin without preloaded metal ions. The binding capacity depends on the type of metal ion used and specific experimental conditions, and should be evaluated by the user after metal ion loading.

Each 1 mL of total volume contains 0.5 mL of resin. Thoroughly resuspend the resin before use and mix well before aliquoting.

The specifications of the product correspond to the actual resin volume, with the resin content of 50%.