We are a full-service Core and provide proteomics support from scientific consultation/experimental design and sample preparation all the way to data analysis and interpretation.
We accept a wide range of sample formats, including complex biological and clinical research samples in unprocessed form (e.g., broad variety of tissues, cells, cell supernatants and conditioned media, blood serum, urine) as well as routine samples (e.g., SDS-PAGE gel bands, eluates from affinity chromatography or IP, beads). Pathway Analysis, N-terminal (Edman) sequencing services, and Amino Acid Analysis of proteins and peptides are also available.
When you are ready to submit samples for analysis, please download and complete the form below. Please email with any questions.
We accept research samples and clinical samples at any stage and prepare them for qualitative and quantitative proteomics experiments. Examples are cells or cell lysates, tissues, blood vessels, blood plasma, biopsies, and more!
Protein Identification, Profiling and shotgun proteomics
- From single gel bands to complex protein mixtures, proteins are identified based on unique internal peptides.
Post-Translational Modifications
- Phosphorylation site mapping (including phospho-enrichment as needed)
- Analysis of other modifications such as methyl, acetyl, ubiquitin, citrulline, lipids, glycosylation and more!
Protein Quantitation
- Changes in protein expression in complex protein mixtures (label free)
- Relative and absolute quantitation (TMT, iTRAQ, selected-, multiple- and parallel reaction monitoring)
- Metabolic labeling (SILAC)
Characterization of Intact Proteins
- Accurate molecular weight determination
- Protein complexes and interactions
Protein Cleavage Sites
- N-terminal sequencing (Edman chemistry)
Quantitation of protein/peptide content
- Amino Acid Analysis
Sample Preparation Guidelines
Questions about how to prepare your samples? Select the document below based on your desired analysis.
Expert scientific consultation and experimental design
Qualitative Proteomics
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protein identification,
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protein profiling and interactome analysis,
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protein sequence confirmation,
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localization of post-translational modifications (PTMs).
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Histone profiling
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Glycoscreen (localization of N-Glycosylation sites)
Quantitative Proteomics
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Protein Expression Profiling using label-free quantitation, SILAC, or TMT (labeled quantitation)
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Targeted Proteomics (parallel reaction monitoring, PRM, “absolute” quantitation),
- Data Independent Analysis (DIA, fast and sensitive differential quantitation for sample cohorts with at least 3 replicates)
- Quantitation of phosphorylation sites
- Quantitative Histone Profiling
Pathway Analysis (biological pathways, gene ontology terms, miRNAs and diseases for differentially expressed proteins)
N-terminal (Edman) protein sequencing
Quantitative Amino Acid Analysis (quantitation of total protein versus non-protein components) for proteins or peptides
Data analysis, interpretation, discussion and reporting
Q-Exactive mass spectrometer coupled to UPLC (Waters)
- High throughput screening (post-translational modifications)
- Protein ID
- Label-free quantitation by spectral counting
- Targeted quantitative proteomics (PRM)
The Orbitrap Exploris 4800
- Increased sensitivity and dynamic range
- Used for Data independent acquisition (DIA) and targeted MS/MS (PRM, “absolute” quantitation)
Ultraflextreme MALDI-TOF/TOF mass spectrometer (Bruker)
- Protein intact molecular weight analysis by MALDI-TOF and more
1150 West Medical Center Drive
Ann Arbor, MI 48109
