This immobilized-metal affinity medium is designed for purification of His-tagged recombinant proteins and other metal-binding biomolecules. It uses a polymethyl methacrylate matrix with a hydrophilically modified surface. Chelating NTA groups coordinate nickel ions to form selective affinity-binding sites. Histidine residues on target proteins interact with the immobilized nickel during sample loading. The hydrophilic surface reduces nonspecific adsorption and supports product recovery. The 1000 Å pore structure permits access by proteins, peptides, nucleotides, and phosphorylated proteins. The rigid 80 µm particles support high flow and operation up to 0.8 MPa. The medium is compatible with selected denaturants, reducing agents, detergents, alcohols, acids, and alkaline solutions under the stated conditions.
Specification
Model: Seplife® LXPM Ni 5504 NTA Matrix: Polymethyl methacrylate Appearance: Light-blue opaque spherical particles Chelating chemistry: NTA with Ni²⁺ Median particle size d50v: 80 µm Pore size: 1000 Å His-tagged protein capacity: ≥20 mg/mL Recommended linear flow: 100-800 cm/h Maximum pressure: 0.8 MPa pH stability: 2-12 Storage solution: 20% ethanol with stated sodium chloride preservative Chemical compatibility: 0.1 M sodium hydroxide, 0.1 M hydrochloric acid, 8 M urea, 6 M guanidine hydrochloride for 24 h, 30% isopropanol, 2% SDS, 5 mM DTT for 24 h, and 70% ethanol after nickel removal
Features
NTA nickel affinity chemistry ≥20 mg/mL His-protein capacity Low nonspecific adsorption Hydrophilic particle surface High-resolution affinity separation Up to 800 cm/h flow Denaturant-compatible operation Rigid 0.8 MPa matrix