Phosphorylation of proteins is one of the most important covalent modifications in living organisms. The simplicity, flexibility, and reversibility of phosphorylation modification itself, as well as the availability of ATP, a donor of phosphate groups, make phosphorylation modification a common regulatory means. The reversible process of protein phosphorylation and dephosphorylation almost regulates the process of life activities including cell proliferation, development, differentiation, cytoskeleton regulation, apoptosis, neural activity, muscle contraction, metabolism and tumorigenesis. And reversible protein phosphorylation is the major signal transduction mode currently known. It is now known that many human diseases are caused by abnormal phosphorylation modifications, and some phosphorylation modifications are the consequences of certain diseases.
Our Phosphoproteomics Service
Creative Proteomics uses Thermo Fisher's Q ExactiveHF mass spectrometry platform, Orbitrap Fusion mass spectrometry platform, etc., to launch phosphorylation quantitative proteome analysis service technology packages, including protein extraction, proteolytic digestion, phosphorylated peptide enrichment, peptide separation, mass spectrometry analysis, mass spectrometry Raw data analysis, bioinformatics analysis.
Our phosphoproteomics platform provides highly sensitive protein phosphorylation detection and accurate quantification. Identification of phosphorylation sites is available (optional).
Phosphoproteomics Service Workflow
Comprehensiveness: Phosphoproteomics takes the whole cell protein as the research object, which includes proteins with life functions in the cell, such as cell proliferation, cell division and cell differentiation and other related proteins, so the analysis is more comprehensive.
Reliability: Traditional biological studies of protein phosphorylation often target specific conditions and start with interactions between two or more proteins, which has limitations and lacks holistic understanding. Phosphoproteomics, on the other hand, can detect the effects of different protein kinases and phosphatases on the phosphorylation level of the same protein, thus making the results universal and reliable.
Validity: Phosphoproteomics reflects what is actually happening in the cell, taking into account different variables, overcoming the drawbacks of incrementally adding variables in biology.
Exploratory: Phosphoproteomics studies intracellular proteins. Compared with traditional biological research and protein chips, it is easier to find unknown phosphorylation sites and phosphorylated proteins. If combined with biological techniques, enzymes with phosphorylation or dephosphorylation functions can be found.
High sensitivity: Fluorescent phospho-tag offers sensitivity higher than mass spectrometry
High resolution: Effective separation of phospho-proteins from their unmodified form
Kinase/phosphatase substrate mapping
Screening and identification of kinase/phosphatase activators (eg drug-induced protein phosphorylation)
Screening and identification of kinase/phosphatase inhibitors
Signal transduction studies (regulation of protein function through phosphorylation)
Triple TOF 5600, Q-Exactive, Orbitrap Fusion™ Tribrid™
Tissue samples: animal, microbial tissue wet weight > 30mg; plant fresh tissue > 300mg.
Cell samples: cell volume > 107.
Body fluid samples: Serum volume > 1500 μL.
Protein extract: total protein >900 μg and concentration >1 μg/μL.