Professor Matthias Wilm directs the UCD Conway Proteomics Core, which involves the large scale study of proteins and their modifications that play important roles in the fundamental biology of health and disease. Our instrumentation is capable of covering all aspects of modern proteomic science including quantitative proteomics, protein post-translational modifications and protein-protein interactions. We offer the dedicated strategic support of our team, both on the analytical and bioinformatics side, to enable our research and commercial partners to take full advantage of their results.
The Mass Spectrometry Resource (MSR) is a state-of-the-art biologic mass spectrometry facility providing access to all the necessary instrumentation for high-throughput, high accuracy protein identification, quantification and characterisation.
Instrumentation:
In terms of equipment, MSR avails of several mass spectrometers in order to be able to cover almost all possible experimental workflows in mass spectrometry-based proteomics. These include:
The AB Sciex 4800 MALDI-Tof/Tof mass spectrometer with a CovalX HM2 high mass-range detector is applied to gel-based and off-line liquid chromatography (LC)-based, high throughput MALDI-MS/MS proteomic workflows or, in linear mode, to accurate determination of the mass of intact proteins or protein complexes up to 1.2 Megadaltons.
The Q-Exactive, LTQ-Orbitrap, the ion traps, the quadrupole time-of-flight and a triple quadrupole mass spectrometers cover all possible needs in liquid-chromatography-tandem mass spectrometry.
Furthermore, the MSR offers access to LC-based workflows supporting the multi-dimensional protein identification technology (MudPIT) and a nano-LC system coupled to a MALDI target loading robot to support off-line LC MALDI-MS.
Software suite
Raw data files generated by each mass spectrometer are subjected to database search with the appropriate algorithm (Mascot, TurboSequest, Spectrum Mill) and database.
The Mass Spectrometry Resource (MSR) is a state-of-the-art biologic mass spectrometry facility providing access to all the necessary instrumentation for high-throughput, high accuracy protein identification, quantification and characterisation.
Instrumentation:
In terms of equipment, MSR avails of several mass spectrometers in order to be able to cover almost all possible experimental workflows in mass spectrometry-based proteomics. These include:
The AB Sciex 4800 MALDI-Tof/Tof mass spectrometer with a CovalX HM2 high mass-range detector is applied to gel-based and off-line liquid chromatography (LC)-based, high throughput MALDI-MS/MS proteomic workflows or, in linear mode, to accurate determination of the mass of intact proteins or protein complexes up to 1.2 Megadaltons.
The Q-Exactive, LTQ-Orbitrap, the ion traps, the quadrupole time-of-flight and a triple quadrupole mass spectrometers cover all possible needs in liquid-chromatography-tandem mass spectrometry.
Furthermore, the MSR offers access to LC-based workflows supporting the multi-dimensional protein identification technology (MudPIT) and a nano-LC system coupled to a MALDI target loading robot to support off-line LC MALDI-MS.
Software suite
Raw data files generated by each mass spectrometer are subjected to database search with the appropriate algorithm (Mascot, TurboSequest, Spectrum Mill) and database.
The Mass Spectrometry Resource (MSR) is a state-of-the-art biologic mass spectrometry facility providing access to all the necessary instrumentation for high-throughput, high accuracy protein identification, quantification and characterisation.
Instrumentation:
In terms of equipment, MSR avails of several mass spectrometers in order to be able to cover almost all possible experimental workflows in mass spectrometry-based proteomics. These include:
The AB Sciex 4800 MALDI-Tof/Tof mass spectrometer with a CovalX HM2 high mass-range detector is applied to gel-based and off-line liquid chromatography (LC)-based, high throughput MALDI-MS/MS proteomic workflows or, in linear mode, to accurate determination of the mass of intact proteins or protein complexes up to 1.2 Megadaltons.
The Q-Exactive, LTQ-Orbitrap, the ion traps, the quadrupole time-of-flight and a triple quadrupole mass spectrometers cover all possible needs in liquid-chromatography-tandem mass spectrometry.
Furthermore, the MSR offers access to LC-based workflows supporting the multi-dimensional protein identification technology (MudPIT) and a nano-LC system coupled to a MALDI target loading robot to support off-line LC MALDI-MS.
Software suite
Raw data files generated by each mass spectrometer are subjected to database search with the appropriate algorithm (Mascot, TurboSequest, Spectrum Mill) and database.
The Protein Separations Laboratory (PSL) is a facility dedicated to electrophoretic gel separation of proteins prior to their identification by downstream mass spectrometric analysis, with particular expertise in the running and subsequent analysis of large format 2D-DIGE gels.
Instrumentation:
Full equipment for protein separation by 2-D gel electrophoresis (2-DE) including
Imagers (both visible and fluorescent):
Image analysis software:
Expertise & Services:
The Protein Separations Laboratory provides expertise and full training in two dimensional gel electrophoresis (2D-E)
The Mass Spectrometry Resource (MSR) is a state-of-the-art biologic mass spectrometry facility providing access to all the necessary instrumentation for high-throughput, high accuracy protein identification, quantification and characterisation.
Instrumentation:
In terms of equipment, MSR avails of several mass spectrometers in order to be able to cover almost all possible experimental workflows in mass spectrometry-based proteomics. These include:
The AB Sciex 4800 MALDI-Tof/Tof mass spectrometer with a CovalX HM2 high mass-range detector is applied to gel-based and off-line liquid chromatography (LC)-based, high throughput MALDI-MS/MS proteomic workflows or, in linear mode, to accurate determination of the mass of intact proteins or protein complexes up to 1.2 Megadaltons.
The Q-Exactive, LTQ-Orbitrap, the ion traps, the quadrupole time-of-flight and a triple quadrupole mass spectrometers cover all possible needs in liquid-chromatography-tandem mass spectrometry.
Furthermore, the MSR offers access to LC-based workflows supporting the multi-dimensional protein identification technology (MudPIT) and a nano-LC system coupled to a MALDI target loading robot to support off-line LC MALDI-MS.
Software suite
Raw data files generated by each mass spectrometer are subjected to database search with the appropriate algorithm (Mascot, TurboSequest, Spectrum Mill) and database.
The Mass Spectrometry Resource (MSR) is a state-of-the-art biologic mass spectrometry facility providing access to all the necessary instrumentation for high-throughput, high accuracy protein identification, quantification and characterisation.
Instrumentation:
In terms of equipment, MSR avails of several mass spectrometers in order to be able to cover almost all possible experimental workflows in mass spectrometry-based proteomics. These include:
The AB Sciex 4800 MALDI-Tof/Tof mass spectrometer with a CovalX HM2 high mass-range detector is applied to gel-based and off-line liquid chromatography (LC)-based, high throughput MALDI-MS/MS proteomic workflows or, in linear mode, to accurate determination of the mass of intact proteins or protein complexes up to 1.2 Megadaltons.
The Q-Exactive, LTQ-Orbitrap, the ion traps, the quadrupole time-of-flight and a triple quadrupole mass spectrometers cover all possible needs in liquid-chromatography-tandem mass spectrometry.
Furthermore, the MSR offers access to LC-based workflows supporting the multi-dimensional protein identification technology (MudPIT) and a nano-LC system coupled to a MALDI target loading robot to support off-line LC MALDI-MS.
Software suite
Raw data files generated by each mass spectrometer are subjected to database search with the appropriate algorithm (Mascot, TurboSequest, Spectrum Mill) and database.
Proteomics Core has not received any reviews.
Proteomics Core has not received any endorsements.