ProPac HIC-10

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Hydrophobic Interaction Chromatography separates biomolecules in a decreasing salt gradient, based on differences in surface hydrophobicity. This method preserves the biological activity of proteins. The HIC separation mechanism is complementary to those of ion-exchange and gel filtration chromatography.

Based on 5 µm ultrahigh purity spherical silica gel particles, with 300 Å pores
Proteins separated under non-denaturing conditions
High protein loading capacity for protein purification applications
Proprietary multidentate silica bonding for enhanced hydrolytic stability
High-resolution HPLC separation of proteins and peptides
Wide range of applications

The ProPac® HIC-10 column is a high-resolution, high-capacity, silica-based HIC column that provides greater hydrolytic stability under the highly aqueous conditions used in HIC. Examples include the separation of bovine serum proteins, snake venom proteins, enzymes, human skeletal muscle protein (HSMP), monoclonal antibodies, pancreatin, and thrombin and peptide applications including tryptic digests of proteins.

Specification Compare to others

Vendor Dionex Poresize, Ã… 300

Brand ProPac HIC-10 pH stability 2.5 - 7.5

Mode HIC Max pressure, psi / bar N/A

Modification N/A Surface area, m²/g N/A

Internal diameter, mm 7.8 Carbon load, % N/A

Length, mm 75 Operating temperature N/A

Particle size, µm 5.0 Endcapped N/A

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