Resources

Proteomics Databases



Metabolomics Databases

• • Application of Post-Translational Modification Analysis

  Post-Translational Modification (PTM) refer to enzymatic or spontaneous chemical changes that occur after protein synthesis, altering the structure and function of proteins. These modifications play a pivotal role in regulating biological processes such as cell signaling, gene expression, and metabolic control. Most eukaryotic proteins undergo at least one form of PTM, highlighting their significance in both biomedicine and biotechnology.

• • Mechanism of Post-Translational Modification Analysis

  Post-translational modification (PTM) are one of the key steps in protein function regulation, widely involved in biological processes such as cell signaling, protein stability, enzymatic activity, and cell cycle regulation. The mechanisms of PTM are diverse, and different types of modifications have profound impacts on protein function, structure, and interactions with other molecules.

• • Workflow of Post-Translational Modification Analysis

  Post-translational modification (PTM) refer to the modifications of proteins after their synthesis, mediated by enzymes or other chemical reactions. These modifications play a critical role in cell signaling, regulation of protein functions, and disease mechanisms. Therefore, studying the molecular mechanisms and biological significance of PTM is a crucial step in uncovering cellular functions and pathological processes.

• • Protein Ubiquitination Site Detection Methods

  Ubiquitination is an important cellular regulatory process that involves the chemical modification of a target protein by the binding of the protein ubiquitin. This modification can regulate the stability, activity, subcellular localization, and interaction with other proteins of the target protein. Here are some common methods for detecting ubiquitination sites in proteins:

• • Protein Phosphorylation Assay

  Protein phosphorylation is a crucial cellular signaling mechanism, involving various cellular functions such as growth, division, death, and response. Phosphorylated proteins play a pivotal role in cellular signal transduction. Therefore, the study of protein phosphorylation is of great importance for understanding cell biology and disease progression.

• • Protein Modification and Detection Methods

  Protein modification is a series of chemical changes that occur in a protein after its transcription and translation. These changes play a decisive role in the function, location, and stability of the protein. There are many types of protein modifications, and the most common ones include phosphorylation, acetylation, ubiquitination, glycosylation, acylation, etc.

• • Protein Glycosylation Site Analysis

  Glycosylation is a key post-translational modification of proteins, which involves attaching a sugar moiety to specific amino acid residues of proteins. Glycosylated proteins (glycoproteins) play crucial roles in multiple cellular processes such as cell-cell interactions, cell signaling, immune responses, etc.   Types of Glycosylation 1. N-linked Glycosylation Typically occurs at the asparagine-N position in proteins.

• • Western Blot Detection of Protein Phosphorylation Level

  Protein phosphorylation is a key post-transcriptional modification in cells, playing a crucial regulatory role in many cellular processes, such as signal transduction, metabolism, and gene expression. Therefore, accurately detecting the level of protein phosphorylation has become an important research direction in the field of life sciences. Among them, Western Blot (WB) technology, due to its high sensitivity and accuracy

• • Mechanism of Quantitative Glycoproteomics

  Glycoproteomics, the study of glycosylation-modified proteins, is of significant value in biomedical research. By analyzing the glycosylation status and changes in the proteome, quantitative glycoproteomics uncovers key regulatory mechanisms in biological processes. With the advancement of mass spectrometry, this field has become an essential tool for investigating protein functions and interactions within complex biological systems.

• • Application of Quantitative Glycoproteomics

  Quantitative glycoproteomics is a powerful technique that elucidates cellular functions through the analysis of protein glycosylation, a critical post-translational modification significantly influencing protein stability, function, and localization. With recent advancements in mass spectrometry, this technique has seen increasing utilization in biomedical research.