Resources

Proteomics Databases



Metabolomics Databases

• • 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........

• • Can Proteomics Measure Free Amino Acids

  Although proteomics is a powerful and intricate scientific discipline, its primary objective is to achieve a comprehensive understanding of proteins and their interactions, rather than focusing on the measurement of free amino acid concentrations. Techniques such as high-performance liquid chromatography (HPLC) and gas chromatography (GC) are commonly employed for this purpose, which fall under the domain of analytical chemistry—a field dedicated to studying the composition and properties of chemical.......

• • Does Edman Sequencing Technology Belong to Proteomics

  Edman degradation, also known as Edman sequencing, is a technique primarily utilized to ascertain the amino acid sequence of proteins or peptides, developed by Pehr Edman. Method Overview Edman sequencing involves a repetitive two-step chemical procedure to determine the amino acid sequence of proteins. In each cycle, the amino acid at the N-terminus of the protein is selectively labeled, detached, and subsequently identified. This process can be repeated iteratively for the removal of one amino acid at....

• • Sequencing Protein Amino Acid Sequences by Mass Spectrometry

  In biological research, sequencing is commonly employed to ascertain the precise sequence of molecules such as DNA or RNA, while protein sequences are typically elucidated using mass spectrometry. In protein mass spectrometry, proteins are initially digested into smaller peptide fragments. The mass of these fragments is then measured to infer the original amino acid sequence of the protein.

• • How Much Tissue Is Needed for TMT Protein Detection

  When performing Tandem Mass Tag (TMT) protein detection, the required tissue mass is primarily determined by the abundance of the target protein and the sensitivity of the detection method. Typically, an initial protein concentration between 100 and 500 µg is used. However, if the target protein is highly abundant in the sample, the required tissue mass may be significantly lower.

• • What Is the Normal Range for Protein Quantification

  The normal range of proteins in human blood is primarily composed of two components: albumin and globulin. The specific reference ranges are detailed below: 1. Total Protein (TP): Reference range, 60–80 g/L 2. Albumin (ALB): Reference range, 35–55 g/L 3. Globulin (GLO): Reference range, 20–30 g/L 4. Albumin/Globulin Ratio (A/G): Reference range, 1.2–2.5

• • iTRAQ/TMT Labeled Peptide Segments

  The application of iTRAQ or TMT labeling technologies is a widely used approach in quantitative proteomics analysis. These methods are based on stable isotope labeling, where isotope tags are chemically introduced to the amino groups at the N-terminus and lysine (K) side chains of peptides. This modification assigns each peptide a distinct mass tag, which can be identified during mass spectrometry analysis. Both iTRAQ and TMT are chemical labeling techniques that enable isotopic labeling of peptides........