How to start
First-time users. Please browse this website to learn about our services. Reach out to us by email at MassSpec@wustl.edu to set up a meeting to go over your project. Alternatively, scroll down on this page to submit a Collaboration Request. Someone will be in touch to schedule an in-person one-on-one, live video, or telephone conference. We will provide the best experimental and study design for your mass spectrometry needs.
Room 4200, 4444 Forest Park Ave, St. Louis, MO63108
Routine Core Services
Washington University Mass Spectrometry Technology Access Center (MTAC) has a set of routine analyses for rapid turnaround that require minimal customization. These are typically samples requiring qualitative or semi-quantitative analysis.
Proteins are identified after in-gel or in-solution digestion. Proteins can be optionally fractionated prior to digestion. The cost for this analysis depends on the complexity of sample preparation and the number of samples that are being analyzed.
Co-immunoprecipitation (CO-IP) is a popular technique to identify physiologically relevant protein-protein interactions by using target protein-specific antibodies to indirectly capture proteins that are bound to a specific target protein. These protein complexes can then be analyzed to identify new binding partners, binding affinities, the kinetics of binding and the function of the target protein.
Proximity Labeling Proteomics
Proximity labeling relies on a labeling enzyme that can biotinylate nearby biomolecules promiscuously. Using the high affinity of “biotin-streptavidin”, this technique has been used for identifying the components of novel cellular structures and for determining protein-protein interaction partners. Depending on the species of labeling enzyme, biotin labeling can be achieved through several different methods.
Specialized Core Services
Washington University Mass Spectrometry Technology Access Center (MTAC) provides a set of specialized services that require more study design and deeper staff commitment to provide a comprehensive view of qualitative or quantitative analysis.
Quantitative Proteomics, 2014, pp. 1-25
Untargeted Quantitative Proteomics
Protein quantification requires a consultation to help design the experiment first. Depending on the project and budget, we can use a variety of methods to achieve the protein quantification analysis.
Targeted Quantitative Proteomics
When you want quantify specific target peptides or proteins, 'Targeted Proteomics' can be used. It requires a method development for the most accurate quantification of targets. After the protocol is established, it offers a high throughput at low cost to quantify up to hundreds of proteins.
There is a method development cost and heavy peptide cost to consider in order to establish the assay. The cost would vary depending on the number of analytes and whether or not you want absolute quantitation (i.e. There are exactly 10.25 picomoles of your peptide in this sample) or relative quantitation (i.e. The level of your peptide in sample A is four-fold higher than in sample B). Depending on the experiment design, we can either use MRM or PRM.
Typically, discovery experiments using untargeted methods lead to targeted methods for a validation stage which require less sample and less time on high throughput scale
Epiproteomic Histone Modification Panel
The Epiproteomic Histone PTM Panel provides rapid profiling of site-specific methylation and acetylation states on histones. At present, more than 9o modification states on Lysine residues can be tracked and quantified by triple-quadrupole based MRM assay.
Phosphorylation is a key reversible modification that regulates protein function, subcellular localization, complex formation, degradation of proteins, and therefore cell signaling networks. In this assay, Phosphopeptides are enriched using titanium dioxide (TiO2 ) and high pH reverse phase fractionation into four fractions prior to being analyzed by orbitrap-based MS. The phosphopeptides are identified and site-specific quantification of phosphorylation is achieved by MaxQuant software.
PTMScan® Technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific bead-conjugated antibody in conjunction with LC-MS for quantitative profiling of post-translational modification (PTM) sites in cellular proteins. These include ubiquitination (UbiScan®), acetylation (AcetylScan®), methylation (MethylScan®), and phosphorylation (PhosphoScan®) among others.
IgG Glycosylation Analysis
IgG heavy chain carries an N-glycan attached to each Asn297 residue of the IgG1-Fc modulating its biological function. The heterogeneity of glycan moieties has implicated on the stability, conformation, aggregation, and effector function of (therapeutic) antibodies. At present, we can detect and quantify 17 different glycoforms (attached to the IgG1-Fc) simultaneously in one MS acquisition.
Top-down proteomics include the ability to detect degradation products, protein isoforms, sequence variants, combinations of post-translational modifications. (Native) TD is tailored to the analysis of semi-pure proteins with minimal non-target protein contamination. Examples of good candidates for this approach include recombinant-expressed proteins, in vitro enzyme assay experiments, and the characterization of bioactive peptides.
J Ind Microbiol Biotechnol, 2014 Feb;41(2):451-9.
Targeted or Untargeted Metabolomics
We provide targeted metabolomics, the measurement of defined groups of chemically characterized and biochemically annotated metabolites. Nitrogenous metabolites, including the amino acids, lipids, and intermediary metabolites, including the TCA cycle oxoacids, from blood plasma, can be measured. There is a method development cost to establish the assay that varies depending on the number of metabolites to target and whether or not you want quantitation
Untargeted metabolomics, an intended comprehensive analysis of all the measurable analytes in a sample including chemical unknowns, requires more in-depth commitment.
WashU: Starting at $ (Once assay has developed)
External Academic/Nonprofit: Starting at $ (Once assay has developed)
External For-Profit Industry: Starting at $ (Once assay has developed)
Imaging mass Spectrometry has proven immense value in studying molecular distributions in tissue sections in a variety of application areas, ranging from clinical research to environmental sciences, and the pharmaceutical industry. We support applications to capture the spatial proteome/metabolome - the localizations of proteins/small molecules and their dynamics at the subcellular level - for a more complete understanding of cell biology.
Developing Core Services
Imaging MS - Peptide
Epiproteomic Histone Modification Panel - PRM
The Epiproteomic Histone PTM Panel provides rapid profiling of site-specific methylation and acetylation states on histones. At present, more than 40 modification states on Lysine residues can be tracked and quantified by high mass accuracy Orbitrap-based Parallel Reaction Monitoring (PRM) assay. More sites will be added to the list as they get developed.
Mol Cell Proteomics, 2012 Dec;11(12):1758-67.
Top-Down Antibody Profiling
We can provide relative quantitation of antibodies, detect a number of modifications, and tandem MS information to confirm its sequence.
Ask for a Project Consultation
Initiate a new project, start a new collaboration or request a services consultation to discuss your Mass Spectrometry needs.
Select your service. Download the service PDF form and complete.
Submit a Sample
Notify us of your sample submission by uploading your PDF form or email the form to us. Let us know if you have any inquiries.