Immobilised metal ion affinity chromatography (Imac) is based on the specific coordinate covalent binding between histidine or other metal binding amino acids with various metal ions
Immobilised metal ion affinity chromatography (Imac) has shown great potential in selective binding and purification of polyhistidine-tagged recombinant proteins and peptides.
Purification of phosphopeptides, glycopeptides and metal binding proteins can also be performed using the Imac method.
Imac is based on the specific coordinate covalent binding between histidine or other metal binding amino acids (either naturally present on the surface of the protein or grafted) with various metal ions, such as copper, nickel, zinc, or iron immobilised or chelated to a polymeric binder or resin.
The bound sample can be eluted from the resin by reducing the pH, increasing the ionic strength or by including EDTA or imidazole in the elution buffer.
Since target protein can be enriched from a large volume of crude lysate in a single step, Imac purification offers significant time savings over less selective multi-step procedures.
Harvard Apparatus offers two convenient ready-to-use Imac formats: single sample SpinColumns and 96-well SpinColumns which allow processing of single or multiple samples in volumes from 10ul to 150ul.
