Resources

• • Quantitative Analysis of Proteomics Using Isotopic Labeling Methods

  Proteomics, the large-scale study of proteins, is a rapidly advancing field that holds the potential to unravel the complexities of biological systems. One crucial aspect of proteomics is quantitative analysis, which involves measuring the abundance of proteins in different biological samples.

• • Detection of Proteins Using SDS-PAGE

  SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) is a powerful technique for protein separation. It is widely used in biological research to analyze the composition of protein mixtures, determine the relative molecular mass of proteins, and isolate specific proteins for further study.

• • Analysis of SDS-PAGE Gel Electrophoresis Results

  SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis) is a widely used technique for protein separation and analysis. This method separates proteins based on their molecular weight under an electric field, allowing for quantitative and qualitative analysis.

• • Detection of Differential Proteins Based on Semi-Quantitative Proteomic Analysis

  Proteomics, as a vital tool in modern biology, is extensively employed to elucidate the expression, function, and interactions of proteins within biological systems. Differential protein detection constitutes a crucial component of proteomics research, offering significant insights into biological processes and disease mechanisms by comparing protein expression variations under distinct experimental conditions or biological states.

• • Detection of Differential Protein Expression Using MS-Based Quantification

  In life sciences research, the analysis of protein expression differences is a critical approach to understanding physiological and pathological changes in organisms under varying conditions. Recently, mass spectrometry (MS) has emerged as a widely used technique in this field due to its high-throughput and sensitive capabilities.

• • Identification of Protein Interactions Using Pull-Down and Mass Spectrometry

  Protein-protein interactions (PPIs) are fundamental to various cellular processes. They regulate essential biological mechanisms such as signal transduction, cell division, and metabolic control. Understanding PPIs is critical for uncovering biological principles and disease mechanisms. Target protein pull-down coupled with mass spectrometry (MS) has emerged as a pivotal technique in PPI research, offering high throughput and sensitivity, and is extensively used in proteomics.

• • Quantitative Analysis of Protein-Protein Interactions Using SILAC and MS

  Protein-protein interactions (PPIs) play a crucial role in cellular signaling, metabolic regulation, and gene expression control. Investigating these interactions not only aids in understanding the fundamental mechanisms of biological processes but also provides potential targets for drug development.

• • GST Pull-Down Assay Combined with Mass Spectrometry for Protein-Protein Interaction Analysis

  Protein-protein interactions (PPI) are integral to numerous cellular processes and functions. Elucidating these interactions is critical not only for understanding biological mechanisms but also for identifying potential drug targets. Among the various methods employed for PPI analysis, the integration of GST pull-down technology with mass spectrometry (MS) stands out as a robust approach, enabling precise identification and characterization of protein interactions.

• • Principle of Post-Translational Modification Analysis

  Post-Translational Modification (PTM) refer to the chemical modifications that proteins undergo after translation, either through enzymatic or non-enzymatic processes. PTM significantly influence protein structure, function, and interactions, serving as a key mechanism for regulating cellular biological processes.

• • Mechanism of 4D-DIA Quantitative Proteomics

  4D-DIA (Four-Dimensional Data-Independent Acquisition) quantitative proteomics is a cutting-edge technology that has gained prominence in recent years. By integrating high-resolution mass spectrometry, time, ion mobility, and data-independent acquisition, this approach enables the quantitative analysis of proteins in complex samples with unprecedented sensitivity and resolution.