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Showing posts with the label TMT

Q&As About Proteomics (Q16-Q20)

Q16 . What bioinformatics analys es  do the proteome results usually need? At present, the analys es  in general literature mainly include Venn d iagram analysis, h ea t map a nalysis,  v olcano plot a nalysis, h ierarchical c luster A nalysis, p rotein f unction a nalysis (GO classification), p rotein m etabolic p athway e nrichment a nalysis (KEGG-based pathway), d ifferential p rotein  i nteraction n etwork c onstruction, t ranscription f actor p rediction , etc . Other relatively high-level analyses include multiple sets of data association analysis, multi-pathway extension analysis, phosphoprotein kinase predictive analysis, interaction networks, and biocontrol model construction analysis. Q1 7. What are the differences between iTRAQ and other proteomics techniques? Two-dimensional electrophoresis is the earliest and most classic proteomic s   technique . It is suitable for most samples, but strong acid or strong basic protein, and protein ...

Q&As About Proteomics (Q11-Q15)

Q11 . In which  journals are proteomics experiment  related articles ususlly published ? W hat are the difference s ? MCP  (M olecular & C ellular P roteomics ): impact factor  7 JPR   (journal of proteome research ): impact factor  5 Proteomics : impact factor  5 Journal of Prteomics : impact factor  5 Electrophoresis : impact factor  5 Plos One : impact factor  5 Other magazines : BMC Genomics, Expert Rev Proteomics, BMC Syst Biol, OMICS, Proteomics Clin Appl, Proteome Sci , etc. Q12 . What techniques need to be repeated ? Which one is used in the repeated experiment, biological repetition or technical repetition? Label free needs to be repeated for three times, so do iTRAQ and TMT . If a large number of verification experiments such as WB or ELISA are designed in the experiment, it is better  to repeat them twice. If the experiment  is not repeated and there are onl...

Part II: Detailed Description of iTRAQ/TMT Tag Structure and Relative Quantification Principle

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As shown below, the reporter group whose  mass is 114 contains one  C13 ,  and the mass of the reporter group is increased by 1 Da. At the same time, the balance group contains one  C13 and one  O18, and the total mass is increased by 3 Da, so that the total mass of the 114 label is increased by 4 Da. By analogy, the reporter group of 115   increase s   by 2   Da, the balance  group will increase by 2   Da .   T he reporter group of 116 increase s  by 3   Da, the balance  group will increase by 1   Da .   T he reporter group of 117 increase s  by 4Da, the balance  group will increase by 0   Da.  After t he above four tags are labeled with different isotopes for its  reporter group   and balance group, the respective report er  group and balance group have different masses . However, as the total mass   added   is the same,   the total mass of...

Part I: Detailed Description of iTRAQ/TMT Tag Structure and Relative Quantification Principle

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Introduction to iTRAQ and TMT T ag Speaking of iTRAQ  ( Isobaric Tag for Relative and Absolute Quantitation )  and TMT  ( Tandem Mass Tag ) , many of us may think that they are  two differen t quantitative pr o teo mics t echniques, but in fact, except the difference s  in labeling specifications and label molecular structure  as well as developer , the principle of their labeling peptides are b asically the same. iTRAQ was firstly developed by AB SCIEX ,  followed by whcih TMT  was developed by Thermo Fisher .   Although they have  different patents, the y   use almost the same   principle. Th e iTRAQ and TMT  marker a re essentially a chemical in vitro  labeling reagent that specifically labels peptides produced by protein digestion. The iTRAQ and TMT-labeled protein samples are available in different sizes. In contrast, TMT can label a wider range of samples and simultaneously quantify multiple sets of 2 p...