High Resolution Mass Spectrometry
We utilize state-of-art, high resolution mass spectrometry to fulfill all your proteomic analysis needs.
We offer the following mass spectrometric testing services. Please contact us to discuss the optimum analysis approach and for any questions on sample requirements.
• Peptide mapping
• Protein identification
• Antibody (Ab) and protein characterization
• Characterize protein conjugation (e.g. ADC)
• Intact protein analysis (intact mass analysis)
• Accurate mass measurement of peptides and proteins
• Identify and localize protein post translational modifications
• Disulfide bond mapping
• Protein/peptide quantitation
• Purity and heterogeneity of proteins and antibodies
• Protein aggregation, polymerization, and higher order structural (HOS) characterization
• Glycan and glycosylation analysis
• Protein and Antibody stability analysis
• HCP (host cell protein) analysis
• Small molecule analysis
Discovery and Targeted Proteomics
- Discovery proteomics: Confidently identify hundreds to thousands of proteins in complex samples. Global profiling of your samples allows comparison of changes in protein expression (relative quantitation) across the entire proteome. This discovery mode often proceeds more in-depth characterization of key proteins using targeted proteomic approaches.
- Targeted proteomics: Characterize and quantify (absolute quantitation) the proteins of interest in your samples. Additionally, confidently identify and quantitate a wide range of post-translational modifications. Our Mechanism of Action (MOA) studies detail the pharmacological effect of drug dosing by quantifying changes in key proteins in a given pathway.
We apply state-of-the-art mass spectrometry (MS) techniques and instrumentation while following USP 1055 and 621 and ICH Q6B guidelines.
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 molecular weight of reduced and/or non-reduced proteins/antibodies
- Peptide mapping
- Localize post-translational modifications including deamidation, acetylation, oxidation, glycosylation, ubiquitination, and phosphorylation
- Assess antibody critical quality attributes (CQA)
- Characterize structural attributes including of N- and C-termini (e.g. pyroglutamic acid, and lysine at the C-terminus of the heavy chain, etc.), free sulfhydryl and disulfide bridge structure, and glycosylation.
- Disulfide bonding mapping and characterize any disulfide scrambling
- Degradation products induced by pH, temperature, light photostability, oxidation, agitation, freeze-thaw, etc. including aggregates and charge variants in samples
- Epitope mapping of antibodies
- Characterize antibody-drug conjugation (ADC) and drug-to-antibody ratio (DAR) with either covalent or non-covalent payloads
- Characterize proteins using top-down and middle down proteomics
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.