Metal affinity chromatography was developed for the purification of native proteins with an intrinsic affinity to metal ions. Immobilized metal affinity chromatography (IMAC) has a broad range of applications, although its primary application is for the purification of histidine-tagged recombinant proteins that can bind nickel, cobalt, and copper ions. IMAC is also used for isolating phosphorylated proteins and zinc finger or copper-binding proteins.
Bio-Rad’s Nuvia IMAC Resin uses a polymeric bead with a narrow particle size range (mean particle size is 50 micrometer), which enables the particles to maintain superior flow properties at any scale. The resin particle size and porosity allow constant and high binding capacity, even at high flow rates, while maintaining the low backpressure required for process-scale manufacturing. Additional benefits of Nuvia IMAC include: high productivity; broad chemical stability; and low, nonspecific binding that increases the purity of the final product because fewer non-target proteins bind to the hydrophilic polymer resin.
Along with the Nuvia IMAC, Bio-Rad offers a wide range of process resins, delivering greater flexibility for lead discovery and process development. When used together with the NGC Chromatography System and accompanying ChromLab Software, these resins simplify and expedite multicolumn purifications into a single automated step.