Sartobind Phenyl HIC 150 ml
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 chromatograp…
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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.
- The first Membrane Adsorbers for HIC
- Simple handling
- Fast operation
- For capturing and polishing
- Less buffer consumption
Purification of Adeno-Associated Virus using Affinity Chromatography with Sartobind® Membrane Adsorbers
Adeno-associated viruses (AAV) belong to the family Parvoviridae, subfamily Parvovirus, genus Dependovirus. They are used as gene delivery vectors for human gene therapy. The advantages of AAV as a vector include e.g. its lack of pathogenicity, high titer, ease of manipulation, and ability to infect non-dividing cells. This application note describes the purification of adeno-associated virus using affinity chromatography with Sartobind® Membrane Adsorbers.
Phenyl Membrane Adsorber for Bioprocessing
In this application note by Sartorius, conditions are optimised for the use of chromatographic membranes in large scale capturing and impurity removal. The low substitution of the phenyl ligand on the membrane allows for mild elution of biomolecules whilst preserving their biological functions. The influence of flow rate, salt type and concentration on the protein binding capability of phenyl membrane are analysed. In addition, aggregate removal, monoclonal antibody binding and separation of cytochrome c, myoglobin, lysozyme and α-chymotrypsinogen are assessed.
Sartorius Stedim Biotech Introduces Sartobind® Cassettes
New modular membrane chromatography solution for large-scale applications
