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Service Cores
Indiana CTSI Research Service Cores and Resources
IU Indianapolis
Biochemical Genetics Laboratory
Our laboratory provides clinically validated liquid chromatography tandem mass spectrometry testing for researchers interested in quantifying metabolites in a wide range of biospecimens with a particular focus on amino acid, organic acid, and acylcarnitine analyses.
IU Indianapolis
Bioinformatics Core
The Bioinformatics Core provides advanced computation and informatics approaches to analyze large and complex biological datasets.
IU Indianapolis
Center for Proteome Analysis
The IUSM Center for Proteome Analysis provides numerous types of mass-spectrometry based proteomics services, including global proteome quantitation, affinity purification-mass spectrometry, targeted mass spectrometry analysis for precise quantitation, post-translational modification analysis, and a variety of consulting services.
IU Indianapolis
Clinical Pharmacology Analytical Core (CPAC)
The Clinical Pharmacology Analytical core provides drug and metabolite concentrations from a variety of biological matrices such as (but not limited to): plasma, urine, CSF, and tissue using HPLC-MS/MS. Additional services include protein binding of drugs, formulation studies, drug stability, drug metabolism, and metabolite screening.
Notre Dame
Keck Center for Transgene Research (resources)
Unique research resources available for collaboration
IU Bloomington
Laboratory for Biological Mass Spectrometry (LBMS)
The LBMS uses mass spectrometry to characterize proteins as well as other biologically-derived molecules. It specializes in the characterization of protein post-translational modifications, including glycosylation, phosphorylation, acetylation and persulfidation (S-sulfhydration). We also have an emphasis on identification of protein-interactions (including determination of protein-protein crosslinks) and quantitative comparisons of complex samples.
Notre Dame
Magnetic Resonance Research Center
The Magnetic Resonance Research Center (MRRC) supports research in chemistry, biochemistry, molecular biology, engineering and related fields. The MRRC operates six solution-state NMR spectrometers (400 to 800 MHz), a solid-state 300 MHz NMR instrument, and an X-band EPR spectrometer. Most instruments are equipped with sample changers for increased sample throughput. See the MRRC website for more information.
Notre Dame
Mass Spectrometry and Proteomics Facility
Analysis of large and small molecules using several ionization methods, low or high resolution, hyphenated techniques, proteomics, and metabolomics.
IU Bloomington
Mass Spectrometry Facility
The Indiana University Mass Spectrometry Facility (MSF) provides qualitative and quantitative small molecule mass spectrometry data. It also confirms chemical formulae of novel compounds by accurate mass spectrometry.
Purdue University
Metabolite Profiling Facility (MPF)
The Metabolite Profiling Facility (MPF) provides both qualitative (comparative analysis) and quantitative (absolute concentrations) metabolite chemical analysis in complex biological systems.
IU Bloomington
NMR Facility
The NMR Facility offers solution NMR spectroscopy services for small and large molecules.
Purdue University
Pharmaceutical Manufacturing Core Facility
Pharmaceutical Manufacturing Core Facility provides support and capabilities for a wide range of research in pharmaceutical development and manufacturing. Technical support for the Facility is provided by the faculty of Industrial and Physical Pharmacy who have extensive pharmaceutical manufacturing experience in both industrial and academic environments.
IU Bloomington
Physical and Biochemistry Instrumentation Facility (PBIF)
The PBIF provides resources to characterize particle properties as well as macromolecular interactions.
Purdue University
Proteomics Facility
The Purdue Proteomics Facility provides chromatography, mass spectrometry and bioinformatic resources for the research communities on campus and beyond for protein characterization. These services include protein identification, relative and absolute quantitation, mapping post-translational modifications, and discovering new protein complexes and protein-protein interactions from a wide variety of sample types such as gel bands, cell or tissue lysates, and plasma or …