Resources

Proteomics Databases



Metabolomics Databases

• • UV Spectral Analysis of Recombinant Protein Vaccines

  Recombinant protein vaccines are a type of vaccines that do not contain complete pathogens and are formulated with specific protein antigens produced by heterologous expression systems. Recombinant protein vaccines have gained wide attention from researchers in recent years due to their advantages of good safety, strong stability, and relatively low cost.

• • Chiral Isomer Analysis of Peptide Drugs

  Peptide drugs are biologically active molecules composed of multiple amino acids connected by peptide bonds. Typically, they consist of 10 to 100 amino acids and have a relative molecular weight lower than 10,000. Peptide drugs have shown great potential in treating various diseases, such as cancer, autoimmune diseases, and metabolic disorders.

• • Nuclear Magnetic Resonance Analysis of Recombinant Protein Vaccines

  Recombinant protein vaccines are a class of vaccines that do not contain complete pathogens and are formulated with specific protein antigens produced by heterologous expression systems. Common heterologous expression systems include bacteria, mammalian cells, plant cells, and insect cells, among which the appropriate heterologous expression system is selected based on the type of antigen produced.

• • Analysis of Glycoproteins in Nasopharyngeal Carcinoma Tissues

  Nasopharyngeal carcinoma is one of the common malignant tumors in the head and neck region, with its incidence and mortality rates continuously rising in recent years. In order to gain a deeper understanding of the pathogenesis, diagnosis, and treatment of nasopharyngeal carcinoma, the analysis of glycoproteins in nasopharyngeal carcinoma tissues is crucial.

• • Analysis of N-Glycosylation and Modification Sites in Liver Tissues

  The liver is the main metabolic organ in the human body, responsible for a significant amount of biotransformation and excretion functions. Protein glycosylation, particularly N-glycosylation, in liver cells is crucial for ensuring normal liver function. This modification not only affects the stability, function, and interactions of proteins, but also plays a central role in liver diseases such as cirrhosis, hepatitis, and liver cancer.

• • Mechanism of Edman Degradation in Protein Sequencing

  The core of the Edman degradation method lies in its unique chemical reaction mechanism, which efficiently and accurately isolates and identifies N-terminal amino acids.

• • Application of Edman Degradation in Protein Analysis

  The Edman degradation method is a classic protein analysis technique, primarily used to determine N-terminal amino acid sequences. Developed by Pehr Edman in the 1950s, this method has been crucial in protein chemistry. Although modern mass spectrometry dominates high-throughput proteomics, Edman degradation remains uniquely valuable in specific applications due to its precision and reliability.

• • Workflow of Edman Degradation for N-Terminal Protein Sequencing

  By sequentially cleaving amino acids from the N-terminus and identifying them, the Edman degradation method provides precise sequence information without disrupting the protein's overall structure. This technique has broad applications in protein research, protein engineering, and biochemistry.

• • Application of iTRAQ/TMT in Quantitative Proteomics

  With the rapid development of proteomics technologies, quantitative proteomics has become an essential tool for revealing dynamic changes in proteins within organisms. iTRAQ (Isobaric Tags for Relative and Absolute Quantitation) and TMT (Tandem Mass Tag) are two widely used labeling techniques that enable high-throughput and accurate protein quantification.

• • Mechanism of iTRAQ/TMT and MultiNotch Labeling in Proteomics

  In modern life science research, quantitative proteomics has become a key tool for understanding the complexity of cellular biology. iTRAQ (Isobaric Tags for Relative and Absolute Quantitation) and TMT (Tandem Mass Tags) are two widely used isotope labeling-based quantitative proteomics technologies. These technologies introduce mass-differentiated tags into samples, enabling precise relative and absolute quantification across multiple samples simultaneously.