Services
How to start
First-time users. Browse our website to learn about our services and reach out to us by email at MassSpec@wustl.edu to schedule a meeting to discuss your project. You can also submit a Collaboration Request by scrolling down on this page. We will provide the best experimental and study design for your mass spectrometry needs through an in-person meeting, live video conference, or telephone call.
Returning-users. If you have worked with us before and know what you need, download and fill out a Sample Submission PDF Form from the options available for proteomics, metabolomics, lipidomics, or imaging MS samples. Email the completed form to MassSpec@wustl.edu and drop off your sample at our drop-off locations. Note that we cannot start work until a WashU CC# or purchase order is provided.
Drop-off Locations
CWE Campus:
Room 4200, 4444 Forest Park Ave, St. Louis, MO63108
Samples can be dropped off Monday-Friday 8:30-4:30pm
Acknowledgement
Work performed by the MTAC should be acknowledged as shown below:
"Mass Spectrometry analyses were performed by the Mass Spectrometry Technology Access Center (MTAC@MGI) at the McDonnell Genome Institute at Washington University School of Medicine."
Contact MassSpec@wustl.edu to get more information
Routine Core Services
Washington University's Mass Spectrometry Technology Access Center (MTAC) offers a set of routine analyses for rapid turnaround that require minimal customization. These services are typically for samples requiring qualitative or semi-quantitative analysis.
Note: The prices listed on this page are for budget estimation only. For approved pricing, click here. For an accurate quotation, please submit a Collaboration Request or contact MTAC at MassSpec@wustl.edu
Work performed by the MTAC should be acknowledged as shown below:
"Mass Spectrometry analyses were performed by the Mass Spectrometry Technology Access Center (MTAC@MGI) at the McDonnell Genome Institute at Washington University School of Medicine."
Protein Identification
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.
Pricing
WashU: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
External Academic/Nonprofit: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
External For-Profit Industry: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
Instruments Used
IP-MS
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.
Pricing
WashU: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
External Academic/Nonprofit: Starting at $ (depending on the umber of samples submitted and length of LCMS gradient)
External For-Profit Industry: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
Instruments Used
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.
BioID: BioID is a mutant E. coli biotin ligase that catalyzes the activation of biotin by ATP. The activated biotin is short-lived and thus can only diffuse to a region proximal to BioID. Labeling is achieved when the activated biotin reacts with nearby amines, such as the lysine sidechain amines found in proteins.
TurboID: TurboID is a biotin ligase engineered via yeast surface display directed evolution. TurboID enables ~10 minute labeling times instead of the ~18 hour labeling times required by BioID.
APEX: APEX is an ascorbate peroxidase derivative reliant on hydrogen peroxide for catalyzing the oxidation of biotin-tyramide, also known as biotin-phenol, to a short-lived and reactive biotin-phenol free radical.
APEX2: APEX2 is a derivative of APEX engineered via yeast surface display directed evolution. APEX2 shows improved labeling efficiency and cellular expression levels.
RIME: RIME can be used in parallel with ChIP-seq experiments to provide information on both the cistrome and interactome for a given protein. It uses formaldehyde fixation to stabilize the protein complex, and cross-linked protein complexes are affinity purified by bead-bound antibodies and analyzed by MS.
ChIP-MS: ChIP-mass spectrometry captures chromatin bound protein interactions and modified histones associated with a protein of interest (a bait protein). We provide consultation for study design and MS analysis.
Pricing
WashU: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
External Academic/Nonprofit: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
External For-Profit Industry: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
Instruments Used
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.
Note: Prices listed here are for budgetary estimation only. To see approved pricing, click here. For an accurate quotation, please submit a Collaboration Request or contact MTAC at MassSpec@wustl.edu.
Work performed in the MTAC should be acknowledged as shown below:
"Mass Spectrometry analyses were performed by the Mass Spectrometry Technology Access Center at McDonnell Genome Institute (MTAC@MGI) at Washington University St. Louis School of Medicine"
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.
1. Heavy Isotope label-based Quantification
1) Metabolic Label: SILAC (Stable Isotope Labeling of Amino Acids in Cell Culture)
Best suited for cell culture system, up to 3 states to compare.
2) Isobaric Label: TMT/iTRAQ
Comparison for >10 states, fewer MS runs, please add reagents cost
2. Label-free Quantification (LFQ)
Technical replicates required, no reagent needed.
Pricing
WashU: Contact us for a quote
External Academic/Nonprofit: Contact us for a quote
External For-Profit Industry: Contact us for a quote
Instruments Used
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
Pricing
WashU: Contact us for a quote
External Academic/Nonprofit: Contact us for a quote
External For-Profit Industry: Contact us for a quote
Instruments Used
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.
Sample requirements for histone assay:
1) Cells Requirement: 1 – 5million
2) Tissue Requirement: 25 – 100mg
Pricing
WashU: $
External Academic/Nonprofit: $
External For-Profit Industry: $
Instruments Used
Phosphoproteomics
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.
Sample requirements for phosphoproteomics:
Start soluble protein amount, 5-6mg
Pricing
WashU: $
External Academic/Nonprofit: $
External For-Profit Industry: $
Instruments Used
PTMScan
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.
Sample requirements for PTMScan:
Grow approximately 1-2 x 108 cells for each experimental condition (enough cells to produce approximately 10-20 mg of soluble protein).
Pricing
WashU: $ (Plus PTMSCan Kit)
External Academic/Nonprofit: $ (Plus PTMSCan Kit)
External For-Profit Industry: $ (Plus PTMSCan Kit)
Instruments Used
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.
Pricing
WashU: $
External Academic/Nonprofit: $
External For-Profit Industry: $
Instruments Used
Top-Down Proteomics
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.
Pricing
WashU: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
External Academic/Nonprofit: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
External For-Profit Industry: Starting at $ (depending on the number of samples submitted and length of LCMS gradient)
Instruments Used
Orbitrap Eclipse Tribrid with FAIMS
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.
Pricing
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)
Instruments Used
Bruker.com
Imaging MS
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.
Pricing
WashU: Contact us for a quote
External Academic/Nonprofit: Contact us for a quote
External For-Profit Industry: Contact us for a quote
Instruments Used
Developing Core Services
Washington University Mass Spectrometry Technology Access Center (MTAC) also develops new service lines with a collaboration on grant support or based on the fee structure. Please submit a Collaboration Request below to initiate a consultation or contact MTAC at MassSpec@wustl.edu.
Work performed in the MTAC should be acknowledged as shown below:
"Mass Spectrometry analyses were performed by the Mass Spectrometry Technology Access Center at McDonnell Genome Institute (MTAC@MGI) at Washington University School of Medicine"
Spatially resolved MALDI mass spectrometric imaging of human brain tissue for metabolites, lipids, and peptides. Link
Imaging MS - Peptide
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.
Pricing
WashU: Contact us for a quote
External Academic/Nonprofit: Contact us for a quote
External For-Profit Industry: Contact us for a quote
Instruments Used
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.
Sample requirements for histone assay:
1) Cells Requirement: 1 – 5million
2) Tissue Requirement: 25 – 100mg
Pricing
WashU: Contact us for a quote
External Academic/Nonprofit: Contact us for a quote
External For-Profit Industry: Contact us for a quote
Instruments Used
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.
Typical amounts of material required are 50 uG solution of each antibody dialyzed against 100 mM ammonium acetate overnight at 4°C.
Pricing
WashU: Contact us for a quote
External Academic/Nonprofit: Contact us for a quote
External For-Profit Industry: Contact us for a quote
Instruments Used
Orbitrap Eclipse Tribrid with FAIMS
Ask for a Project Consultation
Initiate a new project, start a new collaboration or request a services consultation to discuss your Mass Spectrometry needs.
Download Form
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.
*PDF upload requires Google Drive sign-in however MTAC does NOT collect, sell, or share your Google sign-in information. Alternatively, PDFs can be submitted to MassSpec@wustl.edu
