The cOmplete His-Tag Purification Column for researchers performing histidine-tagged protein purification from lysates uses nickel-chelate chemistry and is compatible with reducing agents such as dithiothreitol, metalloproteinase-inhibiting reagents such as EDTA, and different buffer and salt environments. This allows researchers to choose buffer conditions for the target protein in a prepacked format. Following the purification step, the new column does not require buffer exchange or resin recharging. In addition, the resin’s reduced nickel ion leakage not only reduces toxic nickel waste, but also stabilizes the target protein by preventing nickel ions from catalyzing protein oxidation.