Resources

Proteomics Databases



Metabolomics Databases

• • Analysis of Protein-Protein Interactions Using Pull-Down Assays

  Pull-down assays are in vitro techniques used to study and validate PPIs. These assays rely on the affinity purification principle, where a bait protein is used to "pull down" a prey protein from a mixture, allowing for the identification and analysis of protein complexes. The method is versatile and can be used to confirm known interactions or discover novel ones.

• • Workflow for Phospho Proteomics Analysis

  Phospho proteomics involves the identification and quantification of phosphorylated proteins and peptides. This analysis provides insights into the dynamics of phosphorylation and its role in cellular functions. The workflow for phospho proteomics is complex and involves several critical steps, including sample preparation, protein digestion, phosphopeptide enrichment, mass spectrometry analysis, and data interpretation.

• • Procedure for Protein Identification Using LC-MS/MS

  Liquid chromatography-tandem mass spectrometry (LC-MS/MS) is a highly sophisticated and powerful technique used for protein identification and characterization. LC-MS/MS combines liquid chromatography (LC) with tandem mass spectrometry (MS/MS), allowing for the separation, detection, and identification of complex protein mixtures. LC separates peptides based on their physical and chemical properties, while MS/MS provides detailed information about the peptides' mass and structure.

• • Procedure for Protein Mass Measurement Using MALDI-TOF

  MALDI-TOF MS combines two technologies: matrix-assisted laser desorption/ionization (MALDI) and time-of-flight (TOF) mass spectrometry. This technique is known for its high sensitivity, speed, and ability to analyze large biomolecules, making it particularly suitable for protein analysis. MALDI-TOF MS is widely used in proteomics for protein identification, characterization, and quantification.

• • Procedure for Mass Spectrometry-Based Protein Identification

  Mass spectrometry is an analytical technique that measures the mass-to-charge ratio (m/z) of ions to identify and quantify molecules. In proteomics, MS is used to analyze protein samples, enabling the identification of proteins, determination of their post-translational modifications (PTMs), and elucidation of their structural and functional properties.

• • Impurity Detection Based on SEC and RPLC Methods

  In protein purity analysis, detecting impurities is crucial for assessing the quality of the sample. Reverse-phase high-performance liquid chromatography (RP-HPLC) and size exclusion chromatography (SEC) are widely used techniques, each offering specific advantages in detecting and separating impurities in protein samples.

• • Detection and Analysis of Protein Post-Translational Modifications

  Protein post-translational modifications (PTMs) are crucial for the regulation of cellular processes and the functional diversification of proteins. PTMs occur after protein biosynthesis, altering protein properties such as activity, localization, stability, and interactions. Understanding PTMs is essential for comprehending cellular mechanisms and disease pathogenesis.

• • Quantitative Analysis of Low-Abundance Proteins Using DIA-PRM

  In modern biological research, the quantitative analysis of low-abundance proteins has always been a challenge. These proteins are usually present at extremely low concentrations in biological systems, but they play crucial roles in various physiological processes, disease progression, and drug responses. As a result, accurately and efficiently quantifying these low-abundance proteins has become a hot and challenging topic in proteomics research.

• • Analysis of Post-Translationally Modified Peptides Using LC-MS/MS

  Proteins undergo various post-translational modifications (PTMs), which are crucial for regulating protein function and stability. These modifications, including phosphorylation, acetylation, ubiquitination, and others, add layers of functional diversity to the proteome. With the advancement of mass spectrometry, Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) has become an indispensable tool for the detailed study of PTMs.

• • Detection and Analysis of Low-Abundance Proteins Using 4D Proteomics

  The rapid advancement of proteomics has enabled scientists to explore protein networks within organisms in greater depth. However, detecting and analyzing low-abundance proteins remains a major challenge in proteomics research. These proteins often play pivotal roles in biological processes and disease states, making their study crucial for understanding underlying biological mechanisms. The advent of 4D proteomics technology offers new avenues for overcoming this challenge.