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 chelates nickel ions to form affinity-binding sites for histidine residues. The medium can also purify compatible peptides, proteins, nucleotides, and phosphorylated proteins. Spherical particles support uniform column packing and reproducible chromatographic performance. The high-flow agarose structure permits rapid processing with relatively low backpressure. Broad pH stability supports repeated purification and cleaning-in-place cycles. The medium tolerates the listed denaturants, alkaline solutions, and reducing-agent conditions. Its chemical stability and biocompatibility support routine downstream bioprocessing.
Specification
Model: Ni Seplife FF(IDA) Appearance: Spherical gel, odorless and tasteless Matrix: Seplife 6FF Chelating ligand: Iminodiacetic acid Functional ion: Ni²⁺ Particle size: 45-165 µm Maximum flow rate: ≥370 cm/h Pressure resistance: 0.3 MPa Nickel-ion binding amount: Approximately 30 µmol/mL Long-term pH stability: 3-13 Short-term CIP pH stability: 2-14 Chemical compatibility: 0.1 M sodium hydroxide, 8 M urea for 24 h, 6 M guanidine hydrochloride for 24 h, 1 M sodium hydroxide for 24 h, and 5 mM DTT for 24 h