Immobilized metal ion affinity chromatography is based on a high affinity binding of an immobilized metal ion by chelating a part of the target protein. Performed on a preparative chromatographic medium, IMAC is a highly efficient procedure to purify histidine-tagged proteins from a cell extract in just one step. Typical metal ions such as nickel and cobalt selectively retain histidine-tagged proteins. In general, IMAC purification is used as the primary capture step when high yields of pure and active protein are required.

Biofox™ IMAC resins are available with iminodiacetic acid (IDA) or Tris(2-ethylaminoethyl) amine (TREN) chelating chemistries. Proteins can exhibit different binding affinities depending on the chelation chemistry and the type of metal ion used. Ni and Co are the most commonly used metal ions, however, other divalent cation metals including Cu, Zn, Ca, Fe and Pb can be employed. A proprietary manufacturing process is used to produce a 40 (32-60) µm agarose bead that is highly porous that can withstand up to 580 psi. The resins are chemically stable from pH 2 to 14 and resistant to 100% ethanol, 100% methanol, 8M urea, 6M Guanidine HCl, 30% acetonitrile, 70% formic acid and 30% trifluoroacetic acid.

• Chelating Group: Tris(2-ethylaminoethyl)amine
• Ion Capacity (Low): 10-20 µeqv
• Ion Capacity (High): 50-60 µeqv
• pH Stability: 2-14

• Chelating Group: Iminodiacetic Acid
• Ion Capacity (Low): 10-20 µeqv
• Ion Capacity (High): 40-50 µeqv
• pH Stability: 2-14