Pierce™ Strong Cation Exchange and Strong Anion Exchange Spin Columns

Realize shorter diffusion times, higher protein recovery, and intact biological activity of eluted samples with Pierce Strong Cation Exchange and Strong Anion Exchange spin columns. Unlike resin-based column chromatography, these columns utilize ion exchange chromatography to separate molecules based on differences in their accessible surface charges.

Pierce Strong Cation Exchange and Strong Anion Exchange spin columns use membrane-adsorption as the chromatographic method of choice to fractionate proteins based on their charge differences. The column matrix has a highly porous structure, with pores larger than 3000 nm, giving proteins ready accessibility to the membrane's charged ligands. These adsorptive membranes maintain high efficiencies at high flow rates and during fractionation of large biomolecules with small diffusivities.

Ion chromatography is widely preferred in the pre-fractionation or purification of a target protein from crude biological samples. Interactions between molecules and active sites on the ion exchange membrane occur in a convective manner via pores, which shortens diffusion time when compared with fluid inside the pores of a resin particle. Also, the relatively mild binding and eluting conditions of this separation method produce high protein recovery with intact biological activity.Pierce strong ion exchange spin columns enable rapid protein fractionation and sample preparation based on charge differences. There are two available formats:
• Mini Format: for binding up to 4 mg (500 μL capacity)
• Maxi Format: for binding up to 80 mg (20 mL capacity)

Features of Pierce strong ion exchange spin columns:
• Fast and simple—membrane-based spin format eliminates column packing
• Convenient and expandable—centrifugal format enables convenient processing of multiple samples in parallel
• Robust—membrane adsorber spin columns do not crack or run dry
• Low bed volume—small membrane adsorber bed volumes make working with low buffer volumes possible, leading to concentrated elution fractions

Strong ion exchange spin column applications
• Pre-fractionation of proteins in lysate
• Scouting purification conditions for new protein preparation protocols
• Removal of endotoxins from monoclonal antibodies
• Polishing His-tagged proteins after metal chelate chromatography
• Purification and concentration of proteins
• Purification of antibodies from serum, ascites, or tissue culture supernatant
• Removal of detergent from protein solutions
• Sample preparation before 1D or 2D PAGE
• Purification of phosphopeptides before MS analysis