IDA Chelating Separoporer (Agarose) 4B-CL, 50mL

Metal ion-chelating Separopore® 4B-CL is designed for the affinity purification of 6X Histidine-tagged proteins. Nickel, Cobalt, Copper and Zinc are used as cations for this type of purification because they provide effective binding and selectivity for a wide range of proteins. Affinity matrix for proteins with metal binding properties with exposed amino acids such as histidine and cysteine. Metal ion-chelating Separopore® 4B-CL can be charged with Zn2+, Cu2+, Co2+ and Ni2+ metal ions. Imminodiacetic acid immobilized on the matrix allows versatile chelation of divalent metal ions of choice. This is ideal for purification of recombinant proteins containing (His)6 fusion tag and small-scale affinity capture (molecular pull-down) purifications of histidine-tagged protein while exhibiting low non-specific binding of other proteins. Metal ion-chelating Separopore® 4B-CL contain a quadridentate chelate, which is bound with Zn2+, Cu2+, Co2+ and Ni2+ metal ions and covalently attached through a non-charged, hydrophilic linker to Separopore®. Low metal ion leakage means that the activity of the purified protein is retained and the risk of precipitation reduced, which results in increased purity, activity, and yield of the target protein. Leakage of metal ions into the eluted protein pool from beads is generally low under normal conditions.