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I'm currently working on the paper regarding proteomics research. I've listed a lot of questions that freshmen may have during their study. Can anyone explain (based on your experience in the lab) the advantages and disadvantages of iTRAQ/TMT technology and electrophoresis? Which technique is better?

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I believe this paper can answer your question: Q&As About Proteomics (Q1-Q5). It says that 2-DGE is a protein separation technology developed along with MALDI-TOF technology. In theory, the total protein can be separated one by one with the difference of isoelectric point (IEF) and molecular weight (SDS-PAGE). The actual situation is not that ideal, because the low-abundance protein cannot be successfully stained and seen, and the protein is deviated from the theoretical position after post-translational modification. A 2-DGE can identify a total of 1000–2000 proteins. Compared to electrophoresis-based techniques such as 2-DE and DIGE, iTRAQ/TMT has a high resolution. MtoZ Biolabs found 6,000 proteins at most in the cell samples it has treated, most of which have quantitative and qualitative information. Moreover, its iTRAQ has high flux and can complete up to 8 samples at a time. If TMT technology is used, it can complete up to 10 samples at a time, which is especially suitable for simultaneous comparison between multiple samples and dynamic detection of biological processes.

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