Quantitative Plant Proteome Analysis

Label-Free Based Quantitative Plant Proteome Analysis
Label-Free quantitative analysis is a quantitative proteomics technique based on this experimental need. The area of the mass spectrometry peak directly represents the amount of the peptide with the same ionization efficiency during the mass spectrometry analysis, so the relative quantitative information of the protein represented by the peptide can be directly obtained by comparing the area of the mass spectrometry peak of the same peptide.

SWATH Quantitative Plant Proteomics Service
SWATH is a new mass spectrometry acquisition mode technology. It is capable of quantifying almost all detectable molecules in complex samples. SWATH combines the characteristics of high-throughput detection of shotgun proteomics and the advantages of accurate quantitative analysis and is a real panoramic mass spectrometry detection method MS/MS ALL.

DIA Quantitative Plant Proteomics Analysis
DIA is a new, holographic independent data acquisition and quantitative technique based on the trajectory of the electrostatic field. Compared with the traditional proteomics using Data Dependent Acquisition (DDA) strategy, DIA technology avoids the bias of DDA strategy for high-abundance peptide collection and fragmentation, and DIA technology has a significant advantage for the quantification of low-abundance peptides.

Label-Based Quantification of Plant Proteomes
iTRAQ technique and TMT technique use multiple (2-10) stable isotope tags and specifically label the amino groups of peptides for tandem mass spectrometry analysis, which can be used to compare the relative content of proteins in as many as 10 different samples at the same time. It can be used to study the differences in protein expression levels in tissue samples under different developmental stages.

2D-DIGE Quantitative Plant Proteomics
2D-DIGE is a quantitative proteomics technique developed from traditional two-way electrophoresis. 2D-DIGE separates mixed proteins based on the same principle as two-way electrophoresis, using the difference in isoelectric point and molecular weight of proteins to separate proteins.