Resources

Proteomics Databases



Metabolomics Databases

• • Label Transfer Protein Interaction Analysis Overview

  Label transfer protein interaction analysis is an efficient technique for studying protein-protein interactions, widely applied in research fields such as cell biology, molecular biology, and proteomics. This method introduces specific labels (such as fluorescent labels, radioactive labels, or chemical labels) into the target protein or its interacting partners. By analyzing the transfer of these labels, protein-protein interactions can be revealed. When two proteins interact, the label on one protein......

• • Immunoprecipitation Protein Interaction

  Immunoprecipitation protein interaction is a technique widely used in the fields of molecular biology and biochemistry, primarily employed to study protein-protein interactions. Through this technique, researchers can use specific antibodies to recognize and capture target proteins, precipitating them along with their interacting partners from complex cellular samples, thereby revealing protein interaction networks. The greatest advantage of immunoprecipitation Protein Interaction lies in its high..........

• • BiFC Protein Interaction

  BiFC protein interaction is a fluorescence-based protein reconstitution technique used to study protein-protein interactions. This method exploits the fragmentable nature of fluorescent proteins, such as yellow fluorescent protein (YFP), green fluorescent protein (GFP), or red fluorescent protein (mCherry), by splitting them into two non-fluorescent fragments, which are individually fused with the proteins of interest. When these two proteins interact within the cell, the fluorescent protein fragments......

• • APEX Protein Labeling

  APEX protein labeling (ascorbate peroxidase-based proximity labeling) is a technique that utilizes a plant-derived peroxidase, ascorbate peroxidase (APEX), to achieve proximity-based protein labeling. APEX catalyzes the oxidation of biotin-phenol (BP) or other phenolic substrates in the presence of hydrogen peroxide (H₂O₂), resulting in the formation of highly reactive radicals. These radicals have an extremely short half-life and a limited diffusion range of approximately 20 nm, enabling selective la......

• • TMT-Based Quantitative Proteomics

  Tandem Mass Tag (TMT)-based quantitative proteomics is a technique that utilizes isotopic labeling for multiplex protein quantification. Its primary advantage lies in high throughput, enabling the simultaneous analysis of multiple samples, thus improving experimental efficiency and minimizing batch effects. Compared to LFQ methods, TMT labeling at the peptide level reduces technical biases, enhancing quantification stability and reproducibility. However, TMT also has limitations, such as co-isolation.......

• • Tissue Proteomics

  Tissue proteomics is the study of protein types, structures, modifications, and biological functions across different tissues. Unlike single-cell or fluid proteomics, this approach preserves cellular microenvironments and spatial information, revealing protein expression changes and interactions. Since tissues are complex systems composed of diverse cells, protein dynamics are influenced by genetics, metabolism, and disease states. Tissue proteomics is widely used in disease mechanism research, biomarker...

• • Tandem Mass Spectrometry Proteomics

  Tandem mass spectrometry proteomics is a powerful technique that enables the comprehensive analysis of proteins within biological systems. This method focuses on separating, identifying, and quantifying complex protein mixtures to gain deeper insights into protein structures, functions, and their roles in biological processes. The applications of tandem MS proteomics are extensive, including but not limited to the discovery of disease biomarkers, identification of drug targets, analysis of cellular.........

• • Specific Protein Quantification

  Specific protein quantification is a technique used to precisely measure the concentration of target proteins in complex biological samples. This process involves multiple methods and technologies, with mass spectrometry (MS) being one of the most widely used techniques. MS is commonly applied in proteomics research, biomarker discovery, and drug mechanism studies. Enzyme-linked immunosorbent assay (ELISA) is another method for specific protein quantification. ELISA utilizes high-affinity antibody binding..

• • SILAC-Based Proteomics

  SILAC-based proteomics is a powerful and precise technique used to study protein expression and modifications in cell biology and molecular biology. SILAC, or Stable Isotope Labeling by Amino Acids in Cell Culture, is a method that enables quantitative protein analysis by incorporating stable isotope-labeled amino acids into cells during culture. The core principle of SILAC-based proteomics is the replacement of natural amino acids with stable isotope-labeled ones (e.g., ¹³C or ¹⁵N-labeled lysine and.......

• • Glycoprotein Enrichment

  Glycoprotein enrichment refers to the selective extraction and concentration of glycosylated proteins from complex biological samples using specialized techniques. Glycoproteins are proteins that contain covalently attached glycan structures and are fundamental components of various biological systems, including cell membranes, secreted proteins, and serum proteins. As a major post-translational modification, glycosylation significantly influences protein function, stability, localization, and interactions.