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PRM (parallel reaction monitoring) is currently the mainstream method for targeted proteomic data acquisition. It enables targeted relative or absolute quantification of specific peptides or modified peptides by selective detection.
PRM technology utilizes a high-resolution and high-precision mass spectrometer, such as the Q-Exactive HF-x. It selectively detects the parent ion information of the target peptide using the four-pole mass analyzer's selective detection ability. The target peptide then undergoes fragmentation in the HCD collision pool and enters the Orbitrap analyzer with high resolution and accuracy to detect all fragments' information in the selected parent ion window. This enables accurate and specific analysis of target proteins/peptides in complex samples.
PRM combines the selectivity of the quadrupole and the high resolution of Orbitrap, providing several advantages:
(1) High-resolution ion monitoring, and MS/MS identification for target peptides.
(2) The chromatographic peak of the parent and ion pair can be extracted for quantification, and the linear range can be up to 5-6 orders of magnitude, with minimal background interference.
(3) PRM enables both qualitative and quantitative analysis.
Compared with the traditional protein quantitative method (western/elisa):
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PRM has become a powerful tool for accurate identification and quantification, and it is widely used in life science research. It can be used not only for validation of high-throughput quantitative proteomic data such as label-free, TMT, iTRAQ, and SILAC, but also for relative and absolute quantification of target proteins.
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