Immobilized metal ion affinity chromatography (IMAC) was developed by Porath (1975) and is based on the association of certain protein residues (histidine, cysteine and to some extent tryptophan) with transition metals cation interactions. G-Sep™ Ni IDA Agarose Fast Flow is designed for purification of recombinant proteins fused to a 6x Histidine (6XHis) tag.
This resin is designed for purification of recombinant proteins fused to a 6-fold histidine (6XHis) tag for expression in bacterial, insect, and mammalian cells. The resin has high affinity and selectivity for recombinant fusion proteins tagged with 6 tandem histidine residues.
G-Sep™ Ni IDA Agarose Fast Flow (FF) Resin is nickel ion immobilized to highly cross-linked 6% agarose beads using iminodiacetic acid (IDA). G-Sep™ IDA Sepharose Fast Flow (FF) Resin is highly chemically stable, allowing for well-validated cleaning-in-place (CIP) and sanitation protocols. G-Sep™ Co IDA Agarose Fast Flow (FF) resin using cobalt is also available
Specification
Size: 100ml Matrix: Cross-linked agarose beads, 6% Bead form: Spherical, diameter 50-160μm Spacer: Epichlorohydrin Chelating Agent: Iminodiacetic acid Active group: Ni2+ Ni2+ density: 20-40μmol /ml Binding Capacity: 5-10mg His-tagged protein/ml medium pH stability Working Range: 3-12 pH stability Cleaning-in-Place (CIP): 2-14 Maximum Flow Velocity: 450cm/h Exclusion limit(globular proteins): 4 x 106 Physical Stability: Negligible volume variation due to changes in pH or ionic strength Chemical Stability: Stable to all commonly used aqueous buffers: 6M urea, 8M guanidine hydrochloride, Autoclavable: 121°C, pH 7, for 30 min Storage Conditions: 2 to 8°C, 20% Ethanol