Servicecore – Do not remove
Service Cores
Indiana CTSI Research Service Cores and Resources
IU Indianapolis
Chemical Genomics Core Facility
The CGCF is located in the Van Nuys Medical Science Building in Indianapolis. The core is equipped with five hoods for chemical synthesis, a microwave reactor, a parallel synthesizer and preparative HPLCs, LC-QTOF and 600 MHz NMR; a collection of 227,680 diversified small molecules, CRISPR libraries, liquid handling, assay detection and cell image systems.
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.
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 …