DIA (data-independent acquisition) is a non-discriminatory and non-random proteome analysis technology. It divides the full scanning range of mass spectrometry into several windows, and then detects and breaks all ions in each window. This is to obtain information on all ions in the sample, reduce the missing value of sample detection, and improve the quantitative accuracy and repeatability, achieving highly stable and accurate proteome quantitative analysis in a large sample queue.
- 1. By combined with PCT sample pre-processing technology, Westlakeomicscan achieve high depth protein quantitative analysis of clinical micro samples (such as FFPE, puncture biopsy, tears, etc.), and the minimum sample delivery volume of tissue samples is only 0.1mg.
- 2. Use a variety of proteomics database search software, including OpenSWATH, EncyclopeDIA, DIA-NN, etc., and be able to comprehensively analyze the results to improve the identification amount and quantitative accuracy of proteins.
Orbitrap Exploris 480
In this study, we profiled the proteomic tissue landscape of CRC evolving from normal colon to hyperplastic polyps, adenomas, adenocarcinoma not otherwise specified (AC) or mucinous adenocarcinoma (MC). We identified 69,949 peptides, 6,359 protein groups, and 4,830 unique proteins based on our previously established spectral library for DIA analysis from 170 FFPE tissue samples (85 patients, each with 2 biological replicates). Pearson’s correlation coefficient between biological replicates was 0.813, and 0.953 between technical replicates.
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