High-Efficiency Separation of Small to Mid-sized Biomolecules
CromSil™ AxisBio columns, featuring a carefully engineered 160Å pore structure, are tailored for superior separation and purification of peptides, small to medium-sized proteins, and oligonucleotides. Utilizing fully porous particle technology, these columns ensure maximum surface interaction, providing sharper peaks, increased resolution, and reproducibility.
✔ High-resolution separations for peptides and smaller proteins (up to ~30 kDa)
✔ Improved recovery and peak symmetry for biomolecules
✔ Stable pore structure ensuring consistent results
✔ Suitable for analytical and preparative scales
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Chemistry
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Separation Mechanism
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pH Range
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Carbon Load
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Endcapping
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Performance & Benefits
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C18 USP CODE: L1)
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Strong hydrophobic reversed-phase
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2–10
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High
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Fully endcapped
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Broad selectivity; suitable for peptides, proteins, and small biomolecules
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C18 (XPH) USP CODE: L1)
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Extra phase-hydrophobicity (for strong hydrophobic binding)
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1–12
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Very High
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Fully endcapped
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Enhanced retention for highly hydrophobic proteins and peptides
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C8 USP CODE: L7)
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Moderate hydrophobic interactions
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2–10
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Moderate
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Fully endcapped
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Faster elution; suitable for mid-hydrophobic peptides and rapid analyses
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C4 USP CODE: L26
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Weak hydrophobic interactions
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2–10
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Low to Moderate
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Fully endcapped
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Ideal for protein recovery and separation of large biomolecules
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C1(TMS) USP CODE: L13)
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Minimal hydrophobicity
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2–9
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Very Low
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Fully endcapped
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Used for very weak interactions or hydrophilic compound separations
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C30 USP CODE: L62)
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Shape-selective hydrophobic interactions
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2–8.5
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High
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Fully endcapped
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Ideal for structural isomers or geometrical peptide separations
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Aqua (C18 Aqua)
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Hydrophilic endcapped reversed-phase
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2–10
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High
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Polar endcapped
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Suitable for polar peptides and bioanalytes; works well with 100% aqueous mobile phases
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Phenyl (USP CODE: L11)
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π–π interactions (aromatic selectivity)
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2–9
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Medium
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Fully endcapped
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Selectivity for aromatic amino acids or peptide fragments with phenyl groups
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Phenyl Hexyl USP CODE: L11)
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π–π + moderate hydrophobic interaction
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2–9
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Moderate to High
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Fully endcapped
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Improved selectivity for peptides with both aromatic and aliphatic residues
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Phenyl Hexyl+ USP CODE: L11)
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Enhanced π–π interactions with extended hydrophobic tail
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2–9
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High
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Fully endcapped
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Enhanced retention for complex peptides and post-translational modifications
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Biphenyl USP CODE: L11)
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Dual π–π interaction
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2–8.5
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Medium
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Fully endcapped
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Targeted for polypeptides with aromatic motifs; enhanced separation resolution
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PFP (USP CODE: L43)
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Electron-withdrawing π-system interactions (fluorinated)
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2–8.5
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Moderate
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Fully endcapped
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Excellent for halogenated and phosphorylated peptides; high selectivity in RP-HPLC
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Cyano (CN) (USP CODE: L10)
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Dipole interactions
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3–7.5
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Low
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Partially endcapped
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Polar selectivity; can be used in both RP and NP modes for oligonucleotides or modified biomolecules
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Diol (USP CODE: L20)
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Hydrogen bonding / normal-phase selectivity
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2–8
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N/A
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Not applicable
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Ideal for glycans, sugars, glycopeptides; HILIC applications for oligosaccharides
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Amino USP CODE: L8)
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Weak anion exchange / polar interactions
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3–8
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N/A
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Not applicable
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Dual RP/HILIC or ion-exchange applications; useful for acidic bio-analytes
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Silica (USP CODE: L3)
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Bare silica – normal phase interactions
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2–7
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None
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None
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Retains polar biomolecules; suitable for normal-phase and HILIC separations
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