SRM Targeted Proteomics Detection Technology
SRM (Selected Reaction Monitoring) is a mass spectrometry technique primarily used for the quantitative analysis of target proteins or peptides. SRM is typically performed using a triple quadrupole mass spectrometer and is a highly sensitive and specific technique.
The following are some basic principles and steps for SRM-targeted proteomics detection:
1. Target Selection: Before starting the experiment, the target proteins or peptides that need to be measured are selected.
2. Peptide Selection: To detect proteins, representative peptides (often referred to as 'peptide maps' or 'signature peptides') are chosen for quantification.
3. Conversion to Preset Ions: The sample is ionized in the mass spectrometer, and the preset precursor ions are selected in the first quadrupole.
4. Fragmentation: The selected precursor ions collide with inert gas in the collision cell, producing fragment ions.
5. Detection of Specific Fragment Ions: In the second quadrupole, specific fragment ions are selected and detected. This step provides the high specificity of SRM.
6. Quantification: By measuring the intensity of specific ions of specific peptides, the abundance of target proteins in the sample can be quantified.
Figure 1. Parallel Reaction Monitoring (PRM)
Due to its high specificity and sensitivity, SRM has become an important tool in clinical research and biomarker validation. Compared with traditional non-targeted mass spectrometry proteomics techniques, SRM provides higher quantitative accuracy, especially in the case of low-abundance proteins.
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Related Services:
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Label-based Protein Quantification Techniques - iTRAQ, TMT, SILAC
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