Proteomics
The MSU Proteomics Facility provides resources and expertise to assist researchers in the identification and characterization of proteins and peptides. Experiments from simple protein discovery to complex differential proteome profiling, post-translational modification mapping and protein/peptide quantification can be performed using our state-of-the art instrumentation and software.
We’re happy to consult with you, free of charge, on your project to ensure the best possible results.
Contact us at: RTSF.Proteomics@msu.edu
Services and Pricing
- Confirm protein identity from a purified column fraction or gel band. Requires nanogram quantities of purified protein for identification. More extensive characterization/mapping of a protein sequence may require tens of micrograms and several replicates for multi-enzymatic approaches.
- Identify post translationally modified peptides in a purified or complex protein sample, ex. phosphoproteomics. Site localization may be possible. Almost always requires enrichment of the modified proteins/peptides. Replication is recommended to confirm modified residues. Usually requires >1mg total protein.
- Identify protein interactors from an affinity pulldown. Control sample(s) and a minimum of 3 replicates are strongly recommended to enhance confidence in assignments. Pull-down conditions should be optimized prior to sample submission. Usually requires microgram quantities of proteins. Analyzing 5-10% of the product by SDS-PAGE with Coomassie staining is a great way to check if you’ve isolated enough protein for analysis.
- Deep proteome mining for candidate generation or protein profiling. Extensive sample fractionation is performed prior to mass spectrometry analysis to provide the highest possible number of protein identifications. Usually requires hundreds of micrograms of protein.
- Quantitate protein expression differences in a complex sample between two or more conditions using either label-based (TMT) or label-free techniques. Replicates (minimum of 3) are strongly recommended for confident quantification and statistical analysis. Labeled (TMT) techniques require a minimum of 50 micrograms protein, Label-Free techniques require a minimum of 10 micrograms protein.
- 1D gel/Coomassie Staining
- $70/up to 12 sample per gel, on-campus; $88.20, off-campus.
- Peptide Fractionation
- $100/sample, on-campus; $126/sample, off-campus.
- Phosphopeptide Isolation
- $100/sample, on-campus; $126/sample, off-campus.
- Sample Clean Up (C18 SPE)
- $8/sample, on-campus; $10.28, off-campus.
- Enzymatic Digestion
- $25/sample, on-campus; $31.50, off-campus.
- Manual Data Analysis
- $75/hr, on-campus; $94.50, off-campus
- Costs can vary widely depending on sample complexity and therefore the amount of time spent on the mass spectrometer. We charge a flat rate of $200/hr, on-campus, $252/hr, off-campus. Discounted rates applied based on sample volume. Projects usually range between $75 for a simple protein ID to $3000 for a large quantitative comparison. Please contact us for a specific quote for your project.
