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The basic principle of mass spectrometry proteomics is to analyze the physical and chemical properties of the measured sample ions, and obtain qualitative and quantitative results based on the mass spectrum and related information of the sample. At present, mass spectrometry analysis of proteomics generally identifies and quantifies peptide proteins based on three dimensions: retention time, mass-to-charge ratio (m/z), and ionic intensity (intensity), that is, 3D proteomics. On the basis of 3D proteomics, 4D proteomics adds the fourth dimension, ion mobility, which mainly separates ions according to their shape and cross-section, and can distinguish peptides with very small m/z differences, enabling low-abundance protein signals to be differentiated and identified. 4D has greatly improved the identification accuracy, identification depth, quantitative accuracy, and detection cycle, and the sample size requirement has been greatly reduced.