Reversed-phase Chromatography |
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Recombinant proteins, monoclonal antibodies and therapeutic peptides represent the largest portion of biopharmaceuticals in development, with their molecular weight size and complexity necessarily requiring a variety of bioanalytical techniques for accurate and reproducible characterisation. Peptide mapping remains an important technique in any comprehensive protein characterisation workflow. Used for the identification of proteins from the resulting elution pattern of observed peptide fragments, peptide mapping is also employed to derive structural information, locate sites of post-translational modification, oxidation, deamidation, deletions, “clipping” etc. Confirmation of the presence of a modified peptide reflects the presence of a modified protein in the original sample, allowing information on the mixture of protein forms present at any one time to be determined. Reversed-phase is a hydrophobic separation technique, which utilises the interaction of the protein or peptide’s non-polar amino acid side chain groups with the stationary phase. Elution is achieved by the use of an organic modifier, whose strength can be varied by a gradient, with the most hydrophilic molecules eluting first. Reversed-phase provides for high resolution separations, and is an important separation step when further downstream sequencing or structural analysis is required. |
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Suitable for protein samples requiring further fractionation or desalting. High sample loadability and recovery for increased downstream processing sensitivity.
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Fast flowrate enabled separations which
maintain sharp, efficient peaks for even
the largest biomolecules. Optimised
selectivity with four different
bonded phases to meet method development criteria.
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Excellent retention reproducibility and different separation selectivity achievable through high and low pH variability. High efficiency and excellent recovery of hydrophobic and transmembrane-located peptides in high pH mobile phases.
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Effective 1-D or 2-D proteomic-based separations of proteins, polypeptides and peptide digest samples. Extra dense bonding chemistry provides highly stable, reproducible surface for improved resolution and efficiency.
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Unique selectivity and improved resolution for a variety of “difficult” protein samples including membrane, hydrophobic and less-soluble proteins and peptides.
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New C18 bonding technology provides high resolution and unique selectivity for complex peptide digest separations. Increased shielding of the base silica reduces the amount of TFA required.
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Ultra fast protein and peptide separations using high efficiency
1.5μm size particles with conventional HPLC systems.
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High capacity separations of small peptides (Mw <3.5kDa) and ultrafast peptide mapping using Ultra-HT ProC18. Fully endcapped, C18 bonded phase on ultra-high purity silica base.
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Separation of high Mw proteins (~450kDa) and small peptides with very high sample recovery. Fully endcapped C4 bonded phase on a wide pore high purity silica base.
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