A current priority in protein analysis is the comprehensive analysis of larger (>200 KDa) proteins -- quantitatively characterizing heterogeneity in posttranslational modifications, including sites and sequences of glycosylation. Equally important is the capability to do this at trace levels, using separation methods that both provide higher efficiency to resolve similar species, and lower limits of detection in mass spectrometric analysis.

Other recent projects of the laboratory have focused on optimizing many different aspect of the proteomic workflow, including sample preparation, high-resolution LC separations, interfaces to mass spectrometry, mass spectrometric methods, data processing, database searching, and validating biomarkers. Applications include the analysis of biopharmaceuticals and biosimilars, and the discovery of biomarkers for cancer in either tissues or blood.

Learn About:
	Porous Layer Open Tubular (PLOT) Columns
	Electron Transfer Dissociation (ETD) in Characterization of Protein Modifications
	Extended Range Proteomic Analysis (ERPA)
	Monolithic Capillary Columns Improve LC-MS Sensitivity
	Collection and Preparation of Trace Samples:  LCM, derivatization
	New Data Processing Algorithms and Software

Instrumentation, Karger Group 

• Linear Ion Trap (LTQ) with electron transfer dissociation (ETD) source
• Thermo Electron LTQ-FT: Hybrid Linear Ion Trap-Fourier Transform MS
• Applied Biosystems AB 4700 TOF/TOF MS
• Thermo Electron LTQ Linear Ion Trap
• Thermo Electron LCQ DecaXP : 3D ion trap
• Thermo Electron  LCQ Classic : 3D ion trap

Learn about the Barnett Institute Instrumentation>>

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