Columns

Reversed-phase columns / packing materials for biochromatography

Reversed-phase separation with high resolution can separate various molecules, such as hydrophilic nucleotides with low molecular weights and proteins with molecular weights of up to 100,000. A wide variety of HPLC columns and packing materials, such as hybrid silica-based Triart, which can be used at high temperatures, and wide-pore columns, which can separate proteins with relatively high molecular weights, are available.

Features
  • Various chemistries packing materials
  • Excellent peak shape
  • High resolution

Application data

Lineup

Product name Base Pore size (Å) Usable pH range Characteristics
Triart C18 Hybrid silica 120 1.0-12.0
  • Suitable as a first choice ODS with excellent durability
  • Superior peak shape
  • Usable with 100% aqueous mobile phase
Triart C18 ExRS 80
  • C18 phase with high density bonding on organic/inorganic hybrid silica gel
  • Superior chemical durability
Triart Prep C18-S 120 2.0-10.0
  • Preparative ODS packing allows the effective cleaning of the gel with alkaline solution
Triart Prep C8-S 200
  • Preparative C8 packing allows the effective cleaning of the gel with alkaline solution
Meteoric Core C18 Core-Shell type silica 80 1.5-10.0
  • Core-Shell type ODS
Meteoric Core C18 BIO 160
  • Core-Shell type ODS with wide pore size
ODS-A Silica 200 2.0-7.5
  • Standard ODS from analytical to preparative
  • ODS with wide pore size available, useful for separation of protein and peptide
300
ODS-AQ 200
  • Usable with 100% aqueous mobile phase
  • Superior hydrophillic compounds
C8 200
  • Useful for separation of relatively highly hydrophobic compounds, useful for separation of proteins and peptides.
300
C4 200
  • C4 with wide pore size available, useful for separation of proteins and peptides
300
CN 300
  • CN with wide pore size
  • Unique selectivity due to cyano group
YMCbasic 200
  • Superior separation of proteins and peptides, especially of insulin
PROTEIN-RP 200 1.5-7.5
  • Useful for separation of proteins and peptides