Resources

Proteomics Databases



Metabolomics Databases

• • 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.

• • 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.

• • 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.

• • Antibody Sequencing and Immunome Sequencing

  Antibody sequencing is a technique that analyzes the amino acid sequences of antibodies (immunoglobulins), which helps researchers understand the specificity of antibody-antigen interactions. Immunosequencing, on the other hand, examines DNA sequences associated with the immune system, aiding researchers in understanding immune responses to various diseases and infections. These insights enable the design and development of more effective vaccines and antibody therapies.

• • 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.

• • Protein Unbiased Sequence Determination

  Unbiased protein sequencing is a technique used in biology to determine the amino acid sequence of proteins. This method is very important for studying protein function, structure, interaction and evolution. Method Overview Unbiased protein sequence determination is typically accomplished using mass spectrometry. In this process, proteins are initially cleaved into smaller peptide fragments. A mass spectrometer is then employed to measure the mass-to-charge ratio of each peptide.

• • PRM-MS Mass Spectrometry

  PRM-MS (Product Ion Monitoring Mass Spectrometry) is a mass spectrometry technique extensively applied in quantitative bioanalysis, particularly in proteomics and peptide mass spectrometry. It is highly regarded for its exceptional sensitivity, accuracy, and reproducibility. PRM-MS operates as a mode of tandem quadrupole mass spectrometry. During PRM-MS analysis, precursor ions of the target molecules are initially selected.

• • Mass Spectrometry PRM Quantification Method

  PRM (Parallel Reaction Monitoring) is a mass spectrometry quantitative technology, also known as "selective reaction monitoring". It is a highly sensitive, highly selective and highly accurate quantitative strategy based on third-order mass spectrometry. In PRM (Parallel Reaction Monitoring) experiments, precursor ions of the target peptides are selectively introduced into a collision cell for activation, followed by parallel detection of all fragment ions.

• • Amino Acid Sequence Mass Spectrometry Coverage

  Mass spectrometry coverage of amino acid sequences is a crucial indicator in assessing the quality of proteomics analysis, as it significantly impacts our comprehension of protein structures and their subsequent research applications. Definition of Mass Spectrometry Coverage Mass spectrometry coverage is defined as the percentage of a protein's sequence that is successfully identified through peptide detection in mass spectrometry analysis. For instance, a protein with 50% mass spectrometry coverage........