| BioProcess resin | Yes |
|---|---|
| Certificate of Analysis | Yes |
| Chemical stability | Stable in commonly used aqueous buffers - 1.0 M NaOH, 1 M Acetic acid, 30% Acetonitrile, 70% Ethanol, 30% Isopropanol, 6 M guanidine-hydrochloride, 8 M Urea, , 3 M ammoniumsulfate, ionic detergents, non-ionic detergents, polar organic solvents, 2% sodium dodectyl sulfate |
| Ligand | Phenyl |
| Ligand density | Approx. 25 µmol phenyl/ml gel |
| Matrix | cross-linked agarose, spherical |
| Particle size, d 50V | ~34 µm |
| Pressure/Flow Specification | Base matrix: 100-200 cm/h, 300 kPa, BioPilot 60/600 column, bed height 30 cm |
| Storage | 4 to 30°C, 20% Ethanol |
| pH stability, CIP | 2–14 |
| pH stability, operational | 3–13 |
Answer:It is hydrophobic interaction chromatography, which separates proteins based on surface hydrophobicity under appropriate buffer conditions.
Answer:The cross-linked agarose beads are approximately 34 µm in diameter.
Answer:It supplies 5 L of bulk hydrophobic interaction chromatography resin for packing suitable columns.
Phenyl Sepharose™ High Performance is an aromatic hydrophobic interaction chromatography resin used for intermediate purification and polishing of proteins. Its cross-linked agarose matrix carries phenyl hydrophobic groups, and the approximately 34 µm bead size provides higher resolution than coarser hydrophobic interaction media. The 5 L format supports packing larger columns after a separation has been established at development scale. During hydrophobic interaction chromatography, proteins are commonly loaded in a higher-salt buffer that promotes hydrophobic binding, then eluted by lowering the salt concentration or adjusting other suitable conditions. Selectivity depends on protein surface hydrophobicity, salt identity and concentration, buffer composition and operating temperature. The resin is suited to polishing strategies that require discrimination between closely related protein species. It is chromatography media, not a prepacked column.
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