Ni-NTA Agarose Resin uses nitrilotriacetic acid (NTA), a tetradentate chelating ligand, in a highly cross- linked 6% agarose matrix. NTA binds Ni2+ ions by four coordination sites. His-tagged proteins expressed in E. coli can be purified and detected easily because the histidine residues bind metal ions like nickel immobilized on a column matrix under specific buffer conditions and bound proteins are eluted out by changing the pH or by adding a competitive molecule like imidazole. Ni-NTA Agarose Resin utilizes nitrilotriacetic acid to coordinate nickel ions for the high affinity capture of polyhistidine tags. This matrix is essential for HIS tagged protein purification during affinity chromatography and molecular protein purification research.
Ni-NTA Agarose Resin uses nitrilotriacetic acid (NTA), a tetradentate chelating ligand, in a highly cross-linked 6% agarose matrix. NTA binds Ni2+ ions by four coordination sites. His-tagged proteins expressed in E. coli can be purified and detected easily because the histidine residues bind metal ions like nickel immobilized on a column matrix under specific buffer conditions and bound proteins are eluted out by changing the pH or by adding a competitive molecule like imidazole. Ni-NTA Agarose Resin has an orientative binding capacity of up to 50 mg/ml gel.