Membrane Chromatography

Sartobind® capsules with 4 mm bed height are perfectly suited for applications such as the removal of DNA, viruses, endotoxins and protein contaminants. They are available with ion exchange membranes (Q and S) and salt tolerant membranes (Sartobind STIC®). The void volume optimised capsules with 8 mm bed height are designed first of all for bind & elute applications. They are available with ion exchange membranes (Q and S) as well as hydrophobic interaction chromatography membranes (HIC).
  • Simple handling
  • High speed polishing
  • Less buffer consumption
  • Disposable and ready-to-use

Sartobind IEX SingleSep®

Disposable capsules with ion exchange membranes for polishing in biomanufacturing.

Sartobind® capsules are especially suited for the removal of DNA, viruses and protein contaminants in biopharmaceutical production. Sartobind® membranes contain homogenously grafted binding sites on a reinforced cross-linked cellulose matrix. The large pores (>3 um) increase the process speed and avoid diffusion limits compared to conventional bead chromatography. Membrane adsorbers feature extremely short cycle times and provide exceptionally high flow rates and throughput. A large product portfolio of Sartobind® capsules help to introduce an economical solution to production without validation.

Sartobind STIC®

Disposable capsules with salt tolerant interaction membranes are used for polishing in biomanufacturing.

Sartobind STIC® membranes are a new group of Salt Tolerant Interaction Chromatography membrane adsorbers. With the primary amine ligand they bind negatively charged impurities such as DNA, host cell proteins, endotoxins and viruses at much higher salt concentrations than known from conventional Q matrices. Sartobind STIC® membranes eliminate the need for feedstream dilution before flowthrough polishing of recombinant proteins and Mabs. The single use product reduces validation cost, consumption of buffers, footprint and speeds up time to bring products to market. The Sartobind STIC family scales linearly within the proven Sartobind SingleSep® formats of Sartobind nano 1 ml (36 cm²) up to larger capsules.

Sartobind® IEX Jumbo

Ion exchange capsules for capturing and polishing in biomanufacturing.

Sartobind® Jumbo capsules are ion exchange chromatography devices based on macroporous membranes. They can be used for chromatographic separations in the downstream processing of proteins. The ion exchange ligands are coupled to a membrane which is fitted into a plastic housing for quick handling, making ion exchange purification nearly as easy as filtration. Jumbo capsules are constructed with optimized fluid channels. They carry an internal central core to minimise void volume. Fluid models have been developed to reduce the channel width to 3 mm. Capsules with strong basic and strong acidic ion exchange Membrane Adsorber (MA) are available. These products are intended for single use to avoid carryover as well as tedious and costly cleaning validation procedures. However, they can also be reused after cleaning in place. The Jumbo capsules can be applied for contaminant removal from proteins in flowthrough mode (negative chromatography) to bind DNA, residual protein, host cell proteins, endotoxins and viruses, or capture of large proteins as well as dilute proteins in large volumes.

Sartobind® Phenyl

Hydrophobic interaction chromatography (HIC) capsules for capturing of antibodies and removal of hydrophobic impurities.

Hydrophobic interaction chromatography (HIC) separates and purifies biomolecules based on differences in their hydrophobicity. The phenyl membrane adsorber follows the same rules known from the conventional hydrophobic interaction chromatography. Due to the large pore size, membrane adsorbers show excellent flow properties. There is almost no diffusion limitation of mass transport compared with conventional bead chromatography. On average 50% of a protein or peptide surface is accessible for hydrophobic interaction. Buffers with high concentrations of salt promote the adsorption of proteins on the hydrophobic membrane matrix. Proteins are eluted by decreasing the salt concentration in the elution buffer.