High Resolution Mass Spectrometry

We utilize state-of-art, high resolution mass spectrometry to fulfill all your proteomic analysis needs.


We utilize an optimized range of digestion enzymes to maximize coverage of your protein using high resolution mass spectrometry. This can confirm a protein sequence, identify unknown proteins, and detail any sequence variants. This is often the first optimization step when localizing sites of post translational modification.

An optimized digestion of your proteins is performed and searched against protein databases. Identify unknown proteins in your liquid sample and gel bands

  • Accurate mass measurement
  • Confidently identify proteins individually or a proteome-wide level
  • Confirm sequence
  • Peptide mapping
  • Assess sequence variants
  • Identify and localize posttranslational modifications
  • Identify protein glycoforms (glycans attached to protein)
  • Disulfide bond mapping and assessment of disulfide bond scrambling
  • Characterize protein aggregation (using native SEC mass spectrometry)
  • Quantify peptides and proteins using both label free and absolute quantitation (MRM/PRM) methods
  • Identify and characterize Host Cell Proteins (HCP)
  • CMC report produced from subset of above Protein characterization assays
  • Fully characterize antibodies (Ab) at intact protein and peptide level

We analyze antibodies at the protein and peptide level to characterize antibody-drug conjugation (ADC) and drug-to-antibody ratio (DAR) with either covalent or non-covalent payloads.

Obtain accurate molecular weight of intact proteins such as antibodies using state-of-the-art high resolution mass spectrometry. Characterize the post translational modifications of a protein including glycosylation, oxidation, phosphorylation, deamidation, etc. along with assessing peptide/small molecule ligand binding. Accurately detail the mass and size heterogeneity of protein in solutions using SEC-UV-HPLC-MS.

Measure the molecular weight of your peptides and proteins with high accuracy and high resolution.

We utilize an optimized range of digestion enzymes to maximize coverage of your protein’s termini using high resolution mass spectrometry. This can confirm a protein termini sequence and detail any sequence variants.

Identify and localize phosphorylation and a range of post translation modifications on your protein at both the protein and peptide level. Expertise in localizing and quantifying phosphorylation and any other post translational modifications.

We utilize high resolution mass spectrometry and an optimized range of digestion enzymes to map disulfide bonds of any protein and characterize any disulfide scrambling.

The quantitation of proteins is essential to understand biological processes. Mass spectrometry is a key technology in protein quantitation due to its accuracy and high degree of multiplexing. Protein quantitation is offered at both relative (quantity of a given protein relative to other proteins) and absolute (the actual quantity of target proteins) level. Isobaric mass tag labeling provides proteome-wide quantitation for relative quantitation. Absolute quantitation, utilizes stable isotope heavy labeled peptide and/or proteins (Protein Standard Absolute Quantification (PSAQ) quantitation) to determine concentration of a target protein or group of proteins in your sample.

Characterize the aggregation and polymerization of proteins using both SEC-UV-HPLC-MS and complementary methods. Orthogonal methods to assess protein aggregation include SEC-HPLC, FlowCam, DLS, RALS. Please contact us to discuss the best analysis approach for your proteins.

Protein higher order structure (HOS) (higher order than primary structure) analysis is a key component in defining a biologic’s critical quality attributes (CQAs) and understanding the structure of a protein. We can use a range of methods to probe HOS including HPLC (UV-VIS/DAD/ELSD/MALS/FL/RI), FTIR, gel densitometry, and high resolution mass spectrometry. Each method has a different degree of accuracy and turnaround time. Please contact us to discuss the best analysis approach.

Glycosylation is a common post-translational modification that occurs during the production of therapeutic monoclonal antibodies (mAb) and many other protein therapeutics. Reversed-phase liquid chromatography (RP-HPLC) combined with high resolution mass spectrometry is a powerful technique for analyzing glycosylation on antibody and other proteins. Characterize the glycosylation of your proteins at both the protein and peptide level. Identify heterogeneity of glycans (glycoform distribution). Detail the structure of glycans attached to a protein. Identify released glycan (n-glycan profiling).

Host cell proteins are endogenous impurities from host organisms that are introduced during manufacturing. These residual contaminant proteins are identified and quantitated using high resolution mass spectrometry. Comparison against prior samples allows batch-to-batch assessment of HCPs.

Obtain accurate molecular weight and characterize/identify your small molecules using high resolution mass spectrometery.

Please send me information about your High Resolution Mass Spectrometry capabilities.

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