Resources

Proteomics Databases



Metabolomics Databases

• • 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.

• • Principle of Quantitative Glycoproteomics

  Glycoproteomics explores glycosylated proteins and their roles. Glycosylation, a significant post-translational modification, affects protein structure, stability, and function. Quantitative glycoproteomics aims to detect, identify, and quantify glycoprotein glycosylation and expression levels, uncovering dynamic changes during cellular processes.

• • Workflow of Quantitative Glycoproteomics

  Glycoproteomics investigates glycosylation modifications within the proteome and their functional significance. Glycosylation, a widespread post-translational modification of proteins, is pivotal in various biological processes, including cell communication, signal transduction, and immune responses. Quantitative glycoproteomics merges the capabilities of glycoproteomics and quantitative proteomics, enabling comprehensive glycoprotein analysis through mass spectrometry.

• • Mechanism of Quantitative Ubiquitinomics

  In the post-genomic era, the study of protein modifications has become an essential approach for unraveling the mechanisms of various biological processes. Ubiquitination, a crucial post-translational modification, plays a role in regulating numerous cellular processes, including protein degradation, signal transduction, cell cycle control, and stress responses.

• • Application of Quantitative Ubiquitinomics

  Ubiquitinomics is a crucial area of study focused on understanding how proteins are regulated through ubiquitination. This process involves enzymatically attaching ubiquitin molecules to target proteins, affecting their stability, localization, activity, and interactions within the cell.

• • Workflow of Quantitative Ubiquitinomics

  Ubiquitination is a widely conserved post-translational modification in eukaryotes, where small ubiquitin proteins are covalently attached to target proteins, regulating various cellular processes. This modification plays a pivotal role in protein degradation, signal transduction, and DNA repair. With advancements in mass spectrometry (MS) technologies, quantitative ubiquitinomics has emerged as a crucial tool for uncovering the molecular mechanisms and dynamic changes of ubiquitination in cellular systems.