This immobilized-metal affinity chromatography medium is designed for purification of His-tagged recombinant proteins. It uses a high-flow agarose matrix functionalized with nitrilotriacetic acid groups. The NTA ligand chelates nickel ions to create selective binding sites for histidine residues. The medium can also separate compatible metal-binding peptides, proteins, nucleotides, and phosphorylated proteins. Stable nickel chelation reduces metal-ion leakage during operation. The spherical particles provide uniform packing and reproducible chromatographic performance. High flow capability supports efficient processing with relatively low backpressure. The matrix tolerates the listed denaturants, alcohols, acid, and alkaline cleaning solutions. Broad pH stability supports repeated purification and cleaning-in-place cycles.
Specification
Model: Ni Seplife FF(NTA) Appearance: Spherical gel, odorless and tasteless Matrix: Seplife 6FF Shape: Spherical Ligand: Nitrilotriacetic acid chelated with Ni²⁺ Maximum flow rate: ≥370 cm/h Pressure resistance: 0.3 MPa Particle size: 45-165 µm Nickel-ion binding amount: Approximately 20 µmol Ni²⁺/mL Long-term pH stability: 3-13 Short-term CIP pH stability: 2-14 Chemical compatibility: Common aqueous solutions, 0.1 M sodium hydroxide, 0.01 M hydrochloric acid, 8 M urea, 70% acetic acid, and 30% isopropanol Primary application: His-tagged recombinant protein purification