Resources
Proteomics Databases
Metabolomics Databases
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• Strawberry Fruit Protein Parallel Reaction Monitoring Analysis
Strawberry fruit, as an important agricultural crop, not only has high economic value but also occupies an important position in people's daily diet. The quality of strawberries, including their color, aroma, taste, and nutritional components, is determined by their complex internal biological processes. Among them, proteins play a core role in regulating these biological processes.
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• Steps of Protein Interaction Mass Spectrometry Analysis
Protein-protein interaction mass spectrometry analysis has become an indispensable tool in biological research, especially in the study of protein interactions. However, this complex technical process is not simple and requires careful execution by scientists and in-depth analysis of the results.
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• How to Perform Protein Spectrometry on Liquid Samples?
How to perform proteomic analysis of liquid samples? Proteomic analysis is a key technique for understanding the functionality and dynamics of biological systems. Through proteomic analysis, we can study the structure and function of proteins, including their mass, sequence, modifications, interactions, and how they change over time and in different environments. Here are the steps involved in performing proteomic analysis of liquid samples.
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• Protein Affinity Purification Combined With Mass Spectrometry
Affinity purification combined with mass spectrometry analysis is a powerful technique used to selectively isolate and purify specific target proteins or other biomolecules using special biological molecules such as antibodies or ligands. The general steps involved in affinity purification include solution preparation, sample preparation, sample loading, elution, and analysis.
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• What Parameters to Look for in GST Pull-Down Mass Spectrometry?
In biological research, GST pull-down experiments are commonly used techniques for screening and identifying protein-protein interactions. Through this experiment, the target protein can be isolated from its potential interacting partners and further analyzed, such as using mass spectrometry for protein identification. When interpreting GST pull-down mass spectrometry analysis results, there are several important parameters to consider.
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• Reasons for High Protein Recovery Rates in Mass Spectrometry
Mass spectrometry is a powerful tool used for the detection and identification of molecules and their structures, widely employed in protein mass spectrometry analysis. However, during practical operations, we often encounter issues such as high protein recovery. This may be caused by several reasons.
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4D-DIA proteomics technology is an advanced protein profiling technique based on ion mobility and data-independent acquisition. With high sensitivity and high throughput analysis, it allows for comprehensive and accurate study of the proteome. Currently, it has been widely applied in various fields including basic biology, medicine, and agriculture.
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• 2D-DIGE Quantitative Proteomics
2D-DIGE is a new proteomic quantification technique developed based on traditional two-dimensional gel electrophoresis (2-DE). Its fundamental principle is consistent with 2-DE, both of which utilize the differences in protein charge and relative molecular weight to separate protein mixtures. The difference lies in the fluorescent labeling of proteins before electrophoresis, and the analysis of protein expression abundance changes through imaging techniques after electrophoresis.
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• Proteomic Analysis of TMT Technology
TMT proteomic analysis technology is a protein quantification method based on mass spectrometry. Its core is the use of chemical labeling strategies to label peptides in different protein samples. The labeled peptide signals are then detected by a mass spectrometer to achieve protein quantification analysis. Due to its advantages of high throughput, high sensitivity, and high resolution, it is widely used in the field of proteomics research.
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TMT (Tandem Mass Tag) protein sequencing is an advanced mass spectrometry technique used to quantitatively compare protein expression levels in different samples. TMT tags are a group of chemical labels that can covalently bind to the amino terminus and lysine side chains of proteins or peptides. Through mass spectrometry analysis, these tags allow for simultaneous quantitative analysis of protein expression differences in up to 16 different samples.
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