Chelating Bestarose FF - Tag Affinity Chromatography Columns

Chelating Bestarose FF is an immobilized metal affinity chromatography resin, which is made by covalently crosslinking ligand Iminodiacetic acid (IDA) into Bestarose FF matrix. The target protein is based on the separation of side chain histidine, cysteine and tryptophan with the transition metal ions (Cu2+,Co2+,Ni2+,Zn2+ etc.)immobilized on the resin.
The ligand of Chelating Bestarose FF resin can provide 3 coordination sites to chelate with metal ions while provide three ionic bond binding sites to purify the target protein with high affinity. The same type of IMAC Bestarose FF resin provides 4 coordination sites to chelate with metal ions, and 2 ionic bond binding sites to purify the target protein, that is to say, Chelating Bestarose FF resin has the same ligand density and same metal ion conditions. IMAC Bestarose FF has a stronger affinity. All samples that cannot be adsorbed in IMAC Bestarose FF resin can be combined with Chelating Bestarose FF. However, because IMAC Bestarose FF resin has one more metal ion chelation site, it has stronger binding strength to metal ions, and can also be compatible with DTT β-mercaptoethanol. Thus, when purifying recombinant histidine-tagged protein, the resin should be selected according to the characteristics of the protein.