Downstream process purification of proteins requires a resin with optimized bead size for ideal pressure/flow properties and decent dynamic binding capacity (DBC) that provides production efficiencies and good process economics. Our newly developed metal chelate affinity resin — Nuvia™ IMAC — provides the mechanical strength, pore structures, ligand density, and particle size distribution required for an operation run at 300 cm/hr with a DBC of > 40 mg/ml at < 2 bar column backpressure. Protein purification can efficiently be scaled up from milligrams in the lab to kilograms in bioprocess manufacturing. The chemical stability of Nuvia IMAC ensures efficient column regeneration, reproducibility between purification runs, and extended column lifetime. It tolerates more than 100 clean-in-place cycles without significant change in DBC or product purity and is compatible with reagents typically employed for histidine-tagged protein purification. In summary, Nuvia IMAC overcomes the challenges associated with process purification of proteins using metal affinity chromatography.

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