Mass Spectrometry Facility
This Core is housed within the MUSC Mass Spectrometry Facility which provides expertise, services, education, and training to enhance biomedical research endeavors through mass spectrometry-based proteomics. Currently there are over 50 investigators which utilize the facility for protein identification, quantitation, and characterization. Protein analysis includes in-gel or in-solution protease digestion, chromatographic separation, and tandem mass spectrometric analysis of the resulting peptides, and interpretation of MS/MS data using Sequest, Mascot, MaxQuant, and other search algorithms. The facility also assists in the development of customized applications for the isolation, detection and characterization of posttranslationally modified peptides (e.g. phosphorylation, glycosylation, acetylation, oxidation, glutathionylation, and O-GlcNAc modification). With the acquisition of the Orbitrap Elite Mass Spectrometer we have expanded our services to couple quantitative approaches (SILAC, iTRAQ®, TMT®, and LFQ) to modification-specific experiments (eg., phosphoproteomics, redox proteomics). We are developing methodology to analyze alterations in posttranslational regulation that impact signal transduction, epigenetic modulation, and the response to therapeutics with the goal of enabling investigators to discover molecular mechanisms underlying disease progression and therapeutic responses that may not be revealed through genomic studies.
MALDI-TOF MS, LC-MS, and LC-MS/MS tandem mass spectrometry analyses are offered for protein analysis. Protein identification and quantitation services include in-gel or in-solution protease digestion, chromatographic separation and tandem mass spectrometric analysis of the resulting peptides, and interpretation of MS/MS data using Sequest®,Mascot®, or Maxquant software. The facility will also assist in the development of customized applications for the isolation, detection and characterization of posttranslationally modified peptides (e.g. phosphorylation, glycosylation, oxidation, glutathionylation, acetylation and O-GlcNAc modification). Sites of modification are verified by manual inspection of the data. Please consult facility staff for feasibility and pricing of quantitative proteomic experiments (SILAC, Label Free, TMT, or iTraq), the implementation of specialized approaches with quantitative proteomics (e.g. phosphoproteomics, O-GlcNAc proteomics), and MALDI-imaging mass spectrometry for tissue imaging experiments.
Director, Mass Spectrometry Facility
Mass spectrometers and associated proteomic applications available include:
- Thermo Orbitrap Elite with VelosPro Ion Trap MS (CID, HCD, ETD Fragmentation).
LC-MS/MS for identification, characterization of modifications, quantitation of differential protein expression or posttranslational modification using SILAC, iTRAQ®, TMT® , or label free approaches. Protein-Protein Interaction Studies.
- Bruker Rapiflex MALDI Tissuetyper
MALDI Tissue Imaging
- Bruker Solarix 7T Dual Source MALDI/ESI FT-ICR MS (CID and ECD Fragmentation)
MALDI Tissue Imaging, Top-Down Protein Characterization
- Bruker Autoflex III MALDI-TOF-TOF MS
MALDI Tissue Imaging
- Associated HPLC systems (5 LC Packings nano-LC systems and 2 Dionex Probot MALDI Spotters for LC-MALDI)
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