Resources

Proteomics Databases



Metabolomics Databases

• • Protein Detection for Ubiquitination

  Ubiquitinated protein detection is to identify and quantify the status of proteins after ubiquitination post-translation modification. Here are some commonly used methods to detect ubiquitinated proteins:   1. Western Blot Analysis Western blotting is a common method for detecting ubiquitinated proteins. This process usually involves: (1) Extracting protein samples. (2) Separating proteins using SDS-PAGE electrophoresis. (3) Transferring proteins onto a membrane.

• • Thermal Stability Analysis of Recombinant Protein Vaccines

  Recombinant protein vaccines are a type of vaccine that do not contain complete pathogens and are prepared by specific protein antigens produced by heterologous expression systems. The common heterologous expression systems include bacteria, mammalian cells, plant cells, and insect cells. The appropriate heterologous expression system needs to be selected according to the type of antigen produced.

• • Protein Quantification Assay

  Protein quantification is a common technique in experimental biology, used to measure the concentration or total amount of protein in a sample. This measurement is very important for biochemistry, molecular biology, medical research, and other fields.   Analysis Workflow 1. Sample Preparation Cell extract, tissue samples, serum, plasma, urine or other biological samples containing protein. Ensure the sample is clean and free of impurities.

• • Parallel Reaction Monitoring (PRM) Detection of Ubiquitination

  Parallel Reaction Monitoring (PRM) is a high-resolution mass spectrometry analysis technique commonly used in targeted proteomics research. It can be used to detect and quantify specific proteins and protein modifications, such as ubiquitination.

• • Mechanism of Protein Lactylation

  Post-translational modifications (PTMs) are pivotal in regulating the function, localization, stability, and interactions of proteins. Among these, lactylation is an emerging type of PTM that has garnered significant interest in recent years. Lactylation involves the covalent attachment of lactate molecules to lysine residues in proteins, impacting critical biological processes such as metabolism, gene expression, and immune responses.

• • Workflow of Protein Lactylation Analysis

  Protein lactylation is an emerging post-translational modification (PTM) that plays a significant role in various biological processes. As research progresses, the potential functions of lactylation in metabolic regulation, immune responses, and disease pathogenesis are gradually being uncovered. To explore the functional implications of protein lactylation, scientists have developed a precise and efficient analytical workflow.

• • Application of Protein Lactylation Analysis

  Post-translational modifications (PTMs) of proteins are crucial mechanisms that regulate protein function, localization, and interactions. In recent years, lactylation, an emerging type of protein modification, has garnered significant attention from the scientific community.

• • Principle of Protein Lactylation Analysis

  Protein lactylation is an emerging post-translational modification (PTM) that has garnered increasing attention in recent biological research. This modification, which is closely linked to cellular metabolism, particularly under hypoxic conditions where lactic acid production is enhanced, involves the covalent attachment of a lactate molecule to a lysine residue. This process plays a pivotal role in regulating protein function and cellular physiological activities.

• • Mechanism of Protein Deamidation and Its Impact on Function

  Protein deamidation is the process in which the amide groups of asparagine (Asn) or glutamine (Gln) residues within a protein are hydrolyzed, resulting in the formation of aspartic acid (Asp) or glutamic acid (Glu). This process is widespread in living organisms and has profound effects on the structure and function of proteins.

• • Application of Protein Deamidation in Disease Mechanism Studies

  Protein deamidation is a crucial post-translational modification process that plays a vital role in various biological activities. Deamidation refers to the conversion of asparagine or glutamine residues in proteins from an amide group to a carboxyl group, leading to structural alterations and functional regulation. This process is essential for maintaining cellular function, signal transduction, and protein degradation, and is closely linked to the onset and progression of multiple diseases.