Resources

Proteomics Databases



Metabolomics Databases

• • Reasons for High Protein Recovery Rates in Mass Spectrometry

  Mass spectrometry is a powerful tool used for the detection and identification of molecules and their structures, widely employed in protein mass spectrometry analysis. However, during practical operations, we often encounter issues such as high protein recovery. This may be caused by several reasons.

• • 4D-DIA Proteomics Analysis

  4D-DIA proteomics technology is an advanced protein profiling technique based on ion mobility and data-independent acquisition. With high sensitivity and high throughput analysis, it allows for comprehensive and accurate study of the proteome. Currently, it has been widely applied in various fields including basic biology, medicine, and agriculture.

• • 2D-DIGE Quantitative Proteomics

  2D-DIGE is a new proteomic quantification technique developed based on traditional two-dimensional gel electrophoresis (2-DE). Its fundamental principle is consistent with 2-DE, both of which utilize the differences in protein charge and relative molecular weight to separate protein mixtures. The difference lies in the fluorescent labeling of proteins before electrophoresis, and the analysis of protein expression abundance changes through imaging techniques after electrophoresis.

• • Proteomic Analysis of TMT Technology

  TMT proteomic analysis technology is a protein quantification method based on mass spectrometry. Its core is the use of chemical labeling strategies to label peptides in different protein samples. The labeled peptide signals are then detected by a mass spectrometer to achieve protein quantification analysis. Due to its advantages of high throughput, high sensitivity, and high resolution, it is widely used in the field of proteomics research.

• • Protein Sequencing for TMT

  TMT (Tandem Mass Tag) protein sequencing is an advanced mass spectrometry technique used to quantitatively compare protein expression levels in different samples. TMT tags are a group of chemical labels that can covalently bind to the amino terminus and lysine side chains of proteins or peptides. Through mass spectrometry analysis, these tags allow for simultaneous quantitative analysis of protein expression differences in up to 16 different samples.

• • Linear Ubiquitination Quantitative Mass Spectrometry

  Linear ubiquitination is an important protein modification in organisms that regulates various biological processes, including immune response, inflammatory response, cell signaling, and DNA damage repair. However, due to its uniqueness and complexity, the study of linear ubiquitination has faced technical challenges in the past. Fortunately, recent technological advancements have allowed us to investigate linear ubiquitination in more depth.

• • How to Detect the Quantity of Cell Surface Glycoproteins?

  Cell surface glycoproteins play a crucial role in many cellular processes, including cell adhesion, immune response, and signal transduction. Therefore, it is important to understand how to detect the quantity of cell surface glycoproteins in order to study their functions and regulation.

• • Is Histone Methylation Part of Proteomics?

  Histone methylation belongs to proteomics, but it leans more towards epigenetics. Histones are structural proteins of eukaryotic chromosomes and are a class of small, basic proteins. Histone methylation refers to the addition of one, two, or three methyl groups to certain amino acids in histones, and it is an important histone modification.

• • Infrared Spectroscopy for Protein Secondary Structure Analysis

  The secondary structure of a protein refers to the specific conformation formed by the peptide backbone atoms, which can be either in a helical or folded arrangement along a certain axis. It does not involve the side chains of the amino acid residues. The main types of protein secondary structure include α-helix, β-sheet, β-turn, and random coil, with hydrogen bonds playing a major role in maintaining these structures.

• • Chiral Circular Dichroism Spectrum

  Chirality is one of the fundamental physical and chemical properties in nature. Chiral symmetry phenomena typically represent an important symmetric characteristic, namely mirror symmetry, in the field of physical chemistry research. If an object cannot completely overlap with its mirror image, it is considered to possess chirality, also known as handedness. We refer to this kind of molecule that cannot be superimposed onto its mirror image as a chiral molecule.