Interested in our services
Contact our experts to provide further information
Glycosylation is a prevalent and significant post-translational modification of proteins. Over half of the proteins in organisms undergo glycosylation modification, including transcription factors, enzymes related to glucose metabolism, and more. Glycosylation modification is crucial in maintaining the normal physiological functions of the human body, and has long been a major focus of modification omics research.
O-glycosylation is connected to the side chain hydroxyl group of serine or threonine. Unlike N-glycosylation, O-glycosylation lacks a strict consensus sequence and the sugar chain composition can vary greatly, making it more heterogeneous. In addition, O-glycosylation can be further classified into mucin-type and non-mucin-type based on the protein backbone structure. The diversity and complexity of glycosylation make it an important factor in protein structure and function, and dysregulation of glycosylation has been linked to various diseases such as cancer and neurodegenerative disorders.
The principle of N-glycosylation modification omics is to enzymatically remove glycans from the modified peptides and analyze the resulting sugar chains separately. This allows for the quantitative analysis of N-glycosylation sites and their associated sugar chains.
PTM-Bio offers comprehensive glycoproteomics research programs, which include N-glycoproteomics, O-glycoproteomics and intact N-glycopeptide analysis. These programs provide powerful research tools for biomarker discovery and investigating disease pathogenesis.
1. Physiological mechanism studies
Glycosylation modification affects the spatial conformation, activity, transport, and localization of proteins, and is widely involved in various physiological processes, such as intercellular recognition, regulation, signaling, immune response, and cell transformation.
2. Pathological research
Aberrant protein glycosylation modifications are often associated with pathological progression in various diseases, such as cancer, neurodegenerative diseases, lung diseases, blood disorders, and genetic disorders. Many glycoproteins are potential targets for drug action, highlighting their importance as a class of targets in clinical and biological research.
3. Disease biomarkers
Glycosylated proteins are typically located on the surface of cells and are easily secreted into the circulatory system, making them great candidates as biomarkers for disease diagnosis.
4. Agriculture and forestry
Glycosylation modification has been extensively studied in the field of agriculture and forestry, and it has been demonstrated to be involved in regulating critical biological processes such as plant immunity, growth and development, and stress response.
Interested in our services
Contact our experts to provide further information