Hydrophobic Interaction Chromatography (HIC) Media is a versatile technique and can show high selectivity to individual molecules according to their exposed hydrophobic zones. It is particularly useful for intermediate and final-stage purifications.
- High sample loading capacity
- High separation power
- Available at all pack sizes from analytical up to full manufacturing scale
- Chemically stable Agarose base matrix
- Can be produced in high and low ligand densities, alternate crosslinking levels and different bead sizes to optimise the media to the separation
- All versions can be scaled up and produced for GMP use.
|4HF serial (50µm - 150µm)
|6HF serial (50µm - 150µm)
|Large Beads (150µm - 350µm)
|HighRes (25µm - 50µm)
|HIC media is designed to purify most medium to large proteins
|HIC media is designed to purify peptides or smaller proteins
|HIC media is designed to purify proteins from crude or viscous samples
|HIC media is designed to purify proteins that require high resolution
Butyl SepFast™, Phenyl SepFast™, and Octyl SepFast™ are hydrophobic interaction chromatography (HIC) adsorbents with carbon chains of C4, C6 (benzene ring), and C8, respectively. They are specially designed for the purification of biological molecules based on their hydrophobicity profiles. The longer the carbon chain, the higher the surface hydrophobicity.
HIC media requires much milder purification conditions than reversed phase chromatography (RPC) media. Hence biological activity can be maintained in HIC separations unlike RPC operations. HIC media normally binds at moderate to high salt concentrations. It is therefore logical to place a HIC step after an IEX step where molecules are usually eluted at high salt conditions.