Resources

Proteomics Databases



Metabolomics Databases

• • LC-MS/MS MRM

  LC-MS/MS MRM integrates liquid chromatography and mass spectrometry technologies for the quantitative and qualitative analysis of multiple components within complex samples. The MRM mode is a highly selective scan mode of mass spectrometry, capable of reliably detecting target compounds within complex matrices. LC-MS/MS MRM is extensively utilized in areas such as drug metabolism research, environmental monitoring, food safety testing, and biomarker identification. In drug metabolism studies, it measu......

• • Co-Immunoprecipitation Analysis

  Co-immunoprecipitation analysis is a robust experimental technique employed to investigate protein-protein interactions. This methodology enables researchers to selectively isolate and enrich specific protein complexes from complex biological samples. Fundamentally, co-immunoprecipitation analysis leverages specific antibodies for the recognition and binding of target proteins, which are subsequently separated from the solution along with their interacting partners using a solid-phase carrier, such as......

• • SDS-PAGE Quantification

  SDS-PAGE quantification builds upon this principle by applying specialized imaging technologies and software to quantitatively analyze proteins. This technique offers precise measurements of protein concentration and purity, which are essential during protein expression and purification processes. SDS-PAGE quantification enables researchers to determine protein concentrations post-separation, facilitating comprehensive functional and structural analyses. It also plays a critical role in proteomics res......

• • SDS-PAGE Gel Image Analysis

  SDS-PAGE gel image analysis is a technique used to separate and analyze protein samples. Known fully as Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis, SDS-PAGE separates proteins by molecular weight under an electric field. Proteins are denatured in the presence of SDS, which allows them to migrate through the gel based solely on size, irrespective of their shape or charge. This process results in protein bands that are visualized using staining techniques such as Coomassie Brilliant Blue ......

• • SDS-PAGE Protein Identification

  SDS-PAGE protein identification is a widely utilized technique in biochemical and molecular biology research, primarily for the analysis and identification of complex protein mixtures. The acronym SDS-PAGE refers to Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis, a method that employs SDS, an anionic detergent, to denature proteins, thereby disrupting their native conformations and facilitating separation based on molecular weight. The principal function of SDS-PAGE protein identification i......

• • N-Terminal Sequence Analysis of Proteins and Peptides

  In the linear structure of proteins, the N-terminus (amino terminus) serves as both the starting point for polypeptide chain synthesis and a crucial determinant of protein function. From post-translational modifications and subcellular localization to enzymatic activity regulation and molecular interactions, even minor alterations in the N-terminal sequence can have profound effects on protein stability and functionality. As such, N-terminal sequence analysis of proteins and peptides is not only ........

• • SDS-PAGE Analysis of Purified Protein

  SDS-PAGE analysis of purified protein is a widely used method for examining and identifying polypeptide chains in protein samples. This technique enables the separation of proteins based on molecular weight by denaturing them and imparting a uniform negative charge, allowing for electrophoretic migration in a gel matrix. SDS-PAGE analysis of purified protein plays a crucial role in biochemistry and molecular biology, facilitating the separation and identification of proteins in research. It allows for......

• • De Novo Protein Sequencing: How to Improve Accuracy and Data Analysis Efficiency

  De novo protein sequencing is a mass spectrometry-based approach for determining protein amino acid sequences without relying on a reference genome or known protein database. Compared to database-dependent protein identification methods, this technique enables the characterization of novel proteins, peptide modification variants, and protein sequences from non-model organisms. However, due to the complexity of mass spectrometric data, the diversity of fragment ions, and the presence of background noise.....

• • Steps and Common Pitfalls in De Novo Protein Sequencing

  De novo protein sequencing is a mass spectrometry-based approach for determining protein amino acid sequences without relying on database references. This technique is widely employed in novel protein identification, antibody sequencing, and post-translational modification (PTM) analysis. While it has significant potential in studies of non-model organisms and protein engineering, challenges persist regarding data quality, algorithmic interpretation, and experimental execution. This review provides a ......

• • Overview of Protein De Novo Sequencing: Break Through Traditional Analysis Limitations

  In proteomics and biopharmaceutical research, determining the amino acid sequence (primary structure) of proteins is essential for elucidating their functions and biological significance. However, conventional protein sequencing methods primarily rely on database searches, making them inadequate for characterizing unknown proteins, novel variants, or unannotated species. As research advances, addressing this limitation has become increasingly critical. Protein de novo sequencing, a technique that dedu......