Pancreatic cancer-related molecular events and signaling can induce changes driven by pathways such as protein synthesis, post-translational modifications, structure, degradation, and subcellular localization. It also affects the interactions between proteins and other biomolecules, profoundly affecting cellular functions and biological processes at different levels. Such disease-associated protein alterations are independent of genomic changes, are structurally or quantitatively reflected at the proteome level, and can be detected in relevant body fluids. Proteomics analyzes the dynamically changing protein composition, expression levels and modification status in cells to understand the interactions and connections between proteins. In this way, we can study the composition and regulatory activities of proteins as a whole, thereby gaining an overall and comprehensive understanding of disease occurrence, cell metabolism and other processes at the protein level. In this context, proteomics is increasingly used in pancreatic cancer research, from disease mechanism studies to biomarker discovery.
Fig. 1. Pancreatic cancer proteomic research. (Huang P, et al., 2023)
Services We Offer
Alfa Cytology's high-throughput and high-depth proteomics research based on liquid chromatography and tandem mass spectrometry (LC-MS/MS) can obtain information such as protein expression, protein post-translational modifications, quantitative differentially expressed protein profiles, and protein interactions. It can be used for gene expression research, auxiliary gene annotation and correction, protein marker research, functional protein mining, signaling pathways and molecular mechanism research, etc.
- Protein quantitative analysis
Mass spectrometry analysis of protein enzymatic peptide fragments was performed through liquid mass spectrometry (LC-MS/MS) and Tandem mass tag (TMT). It can identify and quantify proteomes, and obtain information such as the source of peptides, proteins, species, and changes in protein expression.
- Protein identification analysis
Use mass spectrometry technology to identify all or specific proteins in cells, tissues, body fluids, or protein gels/liquids that have been separated, purified, and enriched. Fully understanding the protein types in a specific environment is the basis for proteomics research, providing intuitive protein identification results for studying the occurrence and development of diseases.
- Protein modification analysis
Protein phosphorylation is the most common and important post-translational modification of proteins. It occurs on the proteins serine, threonine, and tyrosine. It is regulated by two enzyme systems with opposite effects - protein kinases and phosphatases. Alfa Cytology's protein phosphorylation modification analysis technology mainly includes protein phosphorylation identification (purified protein phosphorylation identification/phosphorylated protein full spectrum identification) and protein phosphorylation quantification.
Alfa Cytology is committed to providing customers with one-stop basic research services on pancreatic cancer. If you are interested in our pancreatic cancer proteomics research services, please contact us for more details.
Reference
- Huang P, et al. Functional and Clinical Proteomic Exploration of Pancreatic Cancer. Mol Cell Proteomics. 2023 Jul;22(7):100575.