Resources

Proteomics Databases



Metabolomics Databases

• • Palmitoylation Proteomics

  Palmitoylation is a critical post-translational modification in which a palmitoyl group (a 16-carbon fatty acid) is covalently attached to specific amino acid residues, such as cysteine, within proteins. Palmitoylation: The primary function of palmitoylation is to enhance protein hydrophobicity, thereby promoting membrane association. This modification is essential for the correct localization and function of various proteins, including signaling proteins, membrane receptors, and cytoskeletal components.

• • Phosphoproteome Sequencing of Plants

  Phosphoproteomics sequencing in plants is an important method to study the molecular mechanisms of plant responses to environmental changes by analyzing the phosphorylation modifications of plant proteins. Through phosphoproteomics sequencing, the degree of protein phosphorylation under specific conditions can be quantitatively analyzed, thereby investigating its function and regulatory mechanisms.

• • Identification of Protein Oxidative Modifications

  Oxidative modification represents a prevalent form of post-translational protein modification, significantly contributing to key physiological and pathological processes, including cell signaling, protein degradation, aging, and disease progression. Comprehensive identification and quantitative analysis of these modifications are pivotal for elucidating their roles in these mechanisms. However, the identification process is inherently complex, necessitating the integration of advanced techniques such as....

• • Can Mass Spectrometry Detect Types of Protein Modifications

  Mass spectrometry (MS) is a powerful technique for detecting and quantifying proteins and their post-translational modifications in biological samples. In mass spectra, modified peptides exhibit distinct mass-to-charge ratios compared to their unmodified counterparts. Analyzing these differences allows for the identification of modification sites and enables the inference of both the type and extent of modifications.

• • Types and Applications of Modified Proteomics

  Protein modification proteomics, an emerging field derived from proteomics, focuses on the changes proteins undergo post-translation through the addition or removal of chemical groups. This field encompasses various types of modifications, including phosphorylation, acetylation, ubiquitination, methylation, and glycosylation. These modifications have significant implications in fields such as life sciences, medical research, and drug development.

• • Proteomics Mass Spectrometry Identification of Malonylated Proteins

  Malonylation is a significant post-translational modification of proteins, playing regulatory roles in various biological processes such as gene expression, cell cycle, and apoptosis. Mass spectrometry-based proteome-wide analysis of protein malonylation is an effective approach for detecting and analyzing malonylated proteins, facilitating a deeper understanding of malonylation's biological functions.

• • What Antibody Is Used to Detect Acetylation

  Acetylation is a widely occurring protein modification in organisms, playing an important regulatory role in protein function and localization. In organisms, acetylation mainly manifests as N-terminal acetylation and lysine acetylation. Detection of acetylation is primarily achieved through antibodies, and the selection of acetylation antibodies mainly includes site-specific antibodies corresponding to acetylation sites and pan-acetylation antibodies.

• • Which Antibody Is Used for Immunoprecipitation in Protein Ubiquitination

  Anti-ubiquitin antibodies serve as vital tools for investigating protein ubiquitination. They are particularly valuable in immunoprecipitation assays for the enrichment and detection of ubiquitinated proteins. This paper presents a detailed immunoprecipitation protocol using anti-ubiquitin antibodies aimed at exploring protein ubiquitination processes, essential for understanding mechanisms such as protein degradation and signal transduction.

• • Phosphorylation Mass Spectrometry of Cell Samples

  Mass spectrometry is a technique for identifying chemical compounds by determining the mass-to-charge ratio of ions. In biological research, it is frequently employed to investigate biochemical processes, including protein phosphorylation. The workflow for phosphorylation mass spectrometry of cell samples comprises four key steps: preparation of cell samples, protein separation and detection, phosphorylation-specific mass spectrometry analysis, and subsequent data interpretation.

• • iTRAQ and TMT Label-Based Quantitative Proteomics Utilize Mass Spectrometry Information for Quantitative Analysis

  In proteomics research, iTRAQ (Isobaric Tag for Relative and Absolute Quantitation) and TMT (Tandem Mass Tags) are widely used for quantitative analysis. These methods involve labeling proteins or peptides with tags of identical mass, allowing quantification through the intensity of reporter ions during mass spectrometry.