Modified Proteome

Protein Quantification

Protein Identification

Modified Proteome

Modified Proteome

Different from conventional proteomics, post-translational modification proteomics is concerned with the effects of protein post-translational modification on life activities, including the identification of drug targets and the screening of clinical markers.


Advantages of Technology

Phosphorylation is the most important, abundant, and most deeply studied modification method in organisms. Many methods were first developed and utilized in phosphoproteomic analysis. Among them, the enrichment methods include titanium dioxide(TiO2), IMAC-Fe and motif antibody enrichment methods.


Acetylation Modification Proteomics

Acetylation is a highly conserved and reversible post-translational modification. It mainly participates in the regulation of gene expression by modifying nuclear proteins, and also regulate a variety of metabolic enzymes and metabolic pathways. In proteomic studies, tens of thousands of acetylated proteins have been found. However, the abundance of most acetylated proteins was low. The enrichment of acetyl peptides helps to improve the sensitivity of mass spectrometry. Acetylation-specific antibodies of CST were used to enrich the acetylpeptide, and 2-3 different enzymes were used to digest the protein to ensure the complete scanning of the acetylpeptide.


Ubiquitination Modification Proteomics

Ubiquitin modification is an important posttranslational modification proteasome system that mediates 80%~85% protein degradation in eukaryotes. In addition to being involved in protein degradation, ubiquitinated modification is also involved in cell cycle, proliferation, apoptosis, differentiation, transcriptional regulation, gene expression, transcriptional regulation, signal transduction, injury repair, inflammatory immunity and so on. Ubiquitination is closely related to the pathogenesis of tumor and cardiovascular diseases. Therefore, as an important achievement of biochemical research in recent years, it has become a new target for research and development of new drugs.


Glycosylation Modification Proteomics

Glycosylation modification affects the spatial conformation, biological activity, transport and localization of proteins, and plays a crucial role in specific biological processes such as molecular recognition, cellular communication, and signal transduction. Glycoproteins are mainly classified into N-glycoproteins and O-glycoproteins according to their sugar chain structure and glycosylation sites. It is inferred that more than 50% of proteins are glycosylated, but due to the high complexity of glycosylation, the vast majority of glycoproteins have not yet been discovered, and only about 10% of proteins in the existing data are annotated as sugars protein. Oligosaccharide chains composed of just 6 different monosaccharides can up to an astonishing 1012 structures.


Methylation Modification Proteomics

Protein methylation is a common post-translational modification of proteins, mainly occurring on arginine and lysine residues. Arginine methylation can regulate processes such as RNA processing, gene transcription, DNA damage repair, protein translocation, and signal transduction. Arginine methylation is mainly involved in histone function, transcription and epigenetic regulation.

© Copyright 2015-2022 Suzhou PANOMIX Biomedical Tech Co.,Ltd