Resources

Proteomics Databases



Metabolomics Databases

• • TMT Phosphorylated Protein Proteomics

  TMT (Tandem Mass Tag) Phosphoproteomics is an advanced mass spectrometry analysis technique used to quantitatively analyze changes in protein phosphorylation levels. This technique combines the enrichment of phosphorylated peptides, TMT labeling, and high-resolution mass spectrometry analysis, enabling researchers to perform high-throughput, high-precision analysis of protein phosphorylation across multiple samples.

• • N-Sugar Spectrum Analysis

  N-glycan profiling is a technique used to analyze the structure and composition of protein N-linked glycans. These glycans are a common type of biomolecule widely present in eukaryotes, especially on the cell surface and in secreted proteins. N-glycan profiling is crucial for understanding protein function, cell signaling, cell recognition, and disease mechanisms.

• • Histone Methylation Detection

  Histones are a class of core proteins, mainly found in the cell nucleus of eukaryotes. They bind with DNA to form nucleosomes, thereby organizing DNA compactly into a chromatin structure. The main types of histones include H2A, H2B, H3, and H4, which play a key role in the regulation of gene expression and the protection of cellular genetic information. Histone methylation detection is an experimental method used for research and analysis of histone methylation levels.

• • Acetylation Site Mass Spectrometry Identification

  Acetylation site refers to the specific amino acid residue position on the protein molecule where acetylation modification occurs. Acetylation is a protein modification in which the acetyl group (CH3CO-) is transferred and attached to an amino acid residue in a protein molecule, typically a lysine (lysine) or serine (serine) residue. This chemical modification can regulate the structure and function of proteins, and has a significant influence on cellular processes and signal transduction.

• • How to Determine Ubiquitination Sites

  Ubiquitination is a post-translational modification process in which a small protein called ubiquitin is attached to other proteins. Determining ubiquitination sites is a complex process that can be conducted largely through the following methods:

• • Immunoprecipitation of Phosphorylated Proteins

  Immunoprecipitation (IP) is an experimental technique used for the isolation and purification of specific proteins and their interaction partners, often used in the study of phosphorylated proteins. By using an antibody to specifically bind to the target protein or phosphorylation site, specific proteins or protein complexes can be enriched from complex biological samples. When applied to the study of phosphorylated proteins, this technique is known as phosphorylated protein immunoprecipitation.

• • Tyrosine Phosphorylation Mass Spectrometry

  Tyrosine phosphorylation is one of the key steps in intracellular signal transduction. It leads to the phosphorylation of proteins on tyrosine residues through the action of tyrosine kinase, thereby changing the activity, stability, affinity, or subcellular localization of proteins and thus regulating various cellular functions.

• • Dithioether Bond and Thiol Functional Group Detection

  Services at MtoZ Biolabs 1. Detection of Disulfide Bonds (1) Ellman's test: This is a common method for detecting disulfide bonds. It uses Ellman's reagent (DTNB, 5,5'-dithiobis-(2-nitrobenzoic acid)) to react with the thiol groups in proteins, producing a yellow product that can be quantified by absorbance. (2) Mass spectrometry: Mass spectrometry can be used to identify the location and number of disulfide bonds in proteins.

• • Phosphorylation: MS vs Proteomics

  Detection of protein phosphorylation levels is mainly performed through mass spectrometry in the field of proteomics research. Proteomics is the scientific study of the combination, structure, and function of all proteins within an organism. Mass spectrometry (MS) is a key analytical tool in proteomics, particularly in studying protein modifications such as phosphorylation.

• • Protein Ubiquitination Detection

  Ubiquitination detection is a biochemical technique used to identify and analyze ubiquitination modifications on proteins. Ubiquitination is a post-translational modification process that involves the covalent attachment of the small protein ubiquitin to lysine residues on target proteins, playing a crucial role in regulating protein degradation, signal transduction, and cell cycle control.