This immobilized-metal affinity chromatography medium is designed for purification of metal-binding biomolecules. It uses a high-flow agarose matrix functionalized with a chelating ligand. The source model identifies the medium as NTA, while the supplied description refers to an iminodiacetic-acid group. After loading with a suitable metal ion, the medium can interact with histidine-containing molecules. It is intended for purification of His-tagged recombinant proteins. The spherical particles provide uniform column packing and reproducible flow. High-flow operation supports efficient processing with relatively low backpressure. Broad pH stability and compatibility with selected aqueous reagents support repeated use.
Specification
Model: IMAC Seplife FF(NTA) Appearance: Spherical gel, odorless and tasteless Matrix: Seplife 6FF Shape: Spherical Model-designated ligand: NTA Source description: Iminodiacetic-acid chelating group 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
Immobilized-metal affinity medium ≥370 cm/h flow High-flow agarose matrix Broad pH stability Uniform spherical particles Compatible with 8 M urea Suitable for His-tagged proteins Reusable chelating platform