Ni-IDA Agarose Resins



Affinity chromatography is a method of separating biochemical mixtures based on highly specific molecular interactions. The Ni-IDA agarose is developed for the purification of proteins with an affinity tag of six consecutive histidine residues. This histidine-metal ion interaction makes one-step purification possible for proteins from any expression system, under native or denaturing conditions. The His-tag sequence binds to Ni2+ cations, which are immobilized onto a solid support using iminodiacetic acid groups (IDA). Impurities are removed and the purified His-tagged proteins can be eluted by imidazole or a reduced pH solution.
Special Features
  • One-step easy purification protocol from crude lysate to >95% pure protein.
  • Purification under native or denaturing conditions.
  • Ready-to-use for any scale of purification.
  • Protein binding capacity: approx. 20-40 μmol Ni2+/ml gel.
  • Economical value.
  • Can be used for successive cycles.
  • Resins and columns formats suitable for batch and gravity purification.
Resin TypeNickel
  • Purification of His-tagged proteins.
  • Antibody purification.
  • Assays involving protein-protein and protein-DNA interactions.
  • Structural and functional investigation of proteins.

Supporting Protocol





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          • Kim , BY et al. "Corneal Dystrophy-associated R124H Mutation Disrupts TGFBI Interaction with Periostin and Causes Mislocalization to the Lysosome" J Biol Chem 284 (29):19580-19591 (2009). DOI: 10.1074/jbc.M109.013607. Application: Protein Isolation Assays.
          • How, KY et al. "Whole genome sequencing enables the characterization of BurI, a LuxI homologue of Burkholderia cepacia strain GG4" PeerJ : (2015). DOI: 10.7717/peerj.1117. Application: Protein Purification.