Protein Columns

Protein Analyses and Lab Scale Purifications

The development and successful commercialization of protein-based biopharmaceuticals and diagnostic reagents frequently depends on the ability to adequately characterize these complex biomolecules. Waters columns and methods can help solve your protein separation and characterization challenges.

Waters technology utilizes reversed-phase, ion-exchange, hydrophilic-interaction, and size-exclusion chromatography modes for peptide separation applications such as the analysis and purification of synthetic peptides, the characterization of complex proteolytic digests, and bioanalysis. These orthogonal separation techniques help provide the critical characterization data and isolated material required to produce the next generation drug.

 


HILIC for Large Biomolecules It is now possible to use HILIC to glean previously unattainable information from intact proteins (with or without glycosylation), protein fragments, and complex, released glycans.
Protein Hydrophobic Interaction Chromatography (HIC) Columns Functionalized with a butyl ligand coating and are well suited for the characterization of proteins and biotherapeutics including monoclonal antibodies (mAb) and antibody drug conjugates (ADC).
Protein Ion-Exchange Columns Ion-exchange chromatography separates proteins based on surface charge differences and is used for both purification and analysis applications.
Protein Reversed-Phase Columns Reversed-phase chromatography of proteins using ion-pairing reagents such as TFA or FA can be used to separate protein mixtures based on relative hydrophobic differences between species.
Protein SEC Columns Size exclusion, also known as gel filtration, chromatography separates proteins based on their sizes (hydrodynamic radii) in solution and not by absolute molecular weight with larger sized species eluting before smaller proteins