Resources

Proteomics Databases



Metabolomics Databases

• • Detection of Protein Oxidation Stress Modifications

  Protein oxidative stress modifications represent a critical mechanism by which biological systems respond to various biological and environmental stresses. Assessing these modifications provides insight into the organism's health and disease progression, facilitating understanding of the adaptive mechanisms to environmental changes and aiding in the development and optimization of disease prevention and treatment strategies.

• • Are Post-Translational Modifications of Proteins Reversible

  Reversible posttranslational modifications (PTMs) of proteins, such as phosphorylation, acetylation, and ubiquitination, are regulated by specific enzymes that add or remove these chemical groups during cellular physiological processes, thereby ensuring their reversibility. In contrast, irreversible modifications, including glycosylation, lipidation, and methylation, typically alter protein structure and function permanently, as they cannot be removed once established.

• • 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.

• • Lowry Method for Protein Content Measurement

  The Lowry method is a widely adopted technique for quantifying protein concentration, initially introduced by Lowry et al. in 1951. The method is premised on the reaction of proteins with copper ions in an alkaline medium, followed by an oxidation-reduction reaction with the Folin-Ciocalteu reagent, resulting in a color change. The intensity of the resultant color is directly proportional to the protein concentration and can be quantified using a spectrophotometer at a wavelength of 750 nm.

• • 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.

• • 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.

• • 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....

• • 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.

• • 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.

• • 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.