This immobilized-metal affinity chromatography medium is designed for purification of His-tagged recombinant proteins. It uses a high-flow agarose matrix functionalized with iminodiacetic-acid groups. The IDA ligand can chelate suitable metal ions for affinity capture. Histidine residues on target proteins interact with the immobilized metal during loading. The medium can serve as a reusable platform for compatible metal-affinity processes. Spherical particles support uniform packing and consistent chromatographic performance. A maximum flow rate of at least 370 cm/h enables efficient sample processing. Broad pH stability and compatibility with selected aqueous solutions support repeated purification cycles.
Specification
Model: IMAC Seplife FF(IDA) Appearance: Spherical gel, odorless and tasteless Matrix: Seplife 6FF Ligand: Iminodiacetic acid Shape: Spherical Particle size: 45-165 µm Maximum flow rate: ≥370 cm/h Pressure resistance: 0.3 MPa Long-term pH stability: 3-13 Short-term CIP pH stability: 2-14 Chemical compatibility: 0.1 M sodium hydroxide, 0.1 M hydrochloric acid, and 8 M urea Application: His-tagged recombinant protein purification
Features
IDA chelating functionality Selective metal-affinity capture ≥370 cm/h flow High-flow agarose matrix Broad CIP pH range Uniform particle distribution Urea-compatible operation Suitable for recombinant proteins