Resources

Proteomics Databases



Metabolomics Databases

• • 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.

• • Protein Methylation Modification Sequencing

  Protein methylation modification sequencing is a biotechnological method used to detect and analyze methylation modifications on proteins. This modification typically involves the addition of a methyl group (-CH3) to a specific amino acid residue on the protein, which plays a crucial role in regulating protein function and cellular processes.

• • Quantitative Proteomics and Phosphoproteomics Combined Analysis

  Quantitative proteomics combined with phosphoproteomics is a method that integrates various bioinformatics and experimental techniques to study protein expression and phosphorylation states in cells or biological samples.

• • Confirming N-Glycosylation Sites via Mass Spectrometry

  N-glycosylation is a key post-translational modification that affects protein folding, stability, and function. Identification of N-glycosylation sites is crucial for understanding protein structure and function, and mass spectrometry (MS) has become a critical tool in this field. The process typically involves the following steps.

• • Protein Sequencing Sample Requirements

  Proteomics sequencing is a technique used to analyze protein expression, modifications, and interactions, often relying on mass spectrometry. In order to carry out effective proteomics analysis, sample preparation must meet certain requirements. Here are some common requirements for proteomics sequencing samples.

• • Does Mass Spectrometry Identify Specific Amino Acid Sequences?

  Proteomics Mass Spectrometry refers to the use of mass spectrometry technology for the analysis of protein or peptide mass, in order to identify their amino acid sequence. In theory and in practice, mass spectrometry can provide specific amino acid sequence information of proteins or peptides. This is achieved by measuring the mass of the peptide and the fragments generated in the mass spectrometry.

• • Explore De Novo Protein Sequencing

  De novo protein sequencing refers to a method of deriving the amino acid sequence of a protein or peptide directly from experimental data, without relying on known DNA or protein database information. It is particularly useful for studying proteins in species without a reference sequence or exploring new variants and modifications of proteins.

• • Recent Advances in N-Terminal Protein Sequencing

  Protein N-terminal sequencing is the process of determining the amino acid sequence at the N-terminus of a protein or peptide chain. This is crucial for protein identification, analysis of signal peptide cleavage sites, and post-translational modification studies, among other areas. Recent advances in the field have been seen, particularly in the application of mass spectrometry and bioinformatics.