MS-based Proteomics: 4D-DIA Proteomics & 4D Phosphoproteomics
Utilize our state-of art MS facility with 20 mass spectrometers, including the Bruker timsTOF Pro and ThermoFisher Orbitrap Exploris 480, alongside ion mobility devices, to enable efficient analysis of large sample batches with swift turnaround.
A new generation of 4D-DIA proteomics technology combines 4D proteomics, which added ion mobility as the fourth separation dimension to traditional LC-MS/MS, with data-independent acquisition (DIA) strategy, which avoids data imbalance caused by randomness by realizing "lossless acquisition" of all possible data.
Technical Strengths of 4D-DIA Quantitative Proteomics:
• Improved Detection Accuracy and Reliability
• Nearly 100% Ion Utilization, Maximized Detection Sensitivity
• Significant Improvement in Detection Depth
• Better quantitative integrity
>7,500 proteins can be stably identified from a single injection of 200 ng of HeLa lysate (120-minute run time), and ~7,000 proteins can be quantified with 96% data completeness in triplicate runs. In comparison, the conventional LC-MS/MS proteomics analysis usually requires μg-level samples to detect about 5,000 proteins
• Immobilized metal affinity chromatography (IMAC) strategy: using proprietary targeted antibodies to enrich phosphopeptides, to reduce sample complexity
• Additional ion mobility separation enables more reliable and deeper coverage for phosphorylation
• Strict dual quality control to remove low confident data: false discovery rate (FDR, 1%); false localization rate (FLR, 0.75)
• Upgraded bioinformatic analysis available: kinase prediction, signaling analysis, and data mining
>10,000 phosphorylation sites (localization probability > 0.75) can be identified with high confidence in various cell tissues, 50% higher than the traditional method.