The site-specific synthesis of phosphorylated peptides(phospho peptides) is crucial for investigating phosphorylation events. Phosphopeptides are produced by the specific incorporation of protected phospho-amino acids or the "post-assembly" peptide phosphorylation at serine, threonine or tyrosine residues. Using the best suited approach for each phospho peptide, JPT has successfully synthesized thousands of phosphorylated peptides in recent years.
- Plays a major role in many physiological processes
- Is one of the most studied post-translational modifications
- It regulates cell cycle, apoptosis and signal transduction pathways
- It occurs mainly on the hydroxyl side chain of serine and threonine residues
- It occurs to a lesser extent on the phenolic side chain of tyrosine residues
- Function as control peptides for kinase profiling
- Are used as phosphatase substrates
- Serve as lead structures for phosphatase inhibitor discovery
In addition to traditional phosphopeptide synthesis, JPT provides a number of innovative solutions for kinase and phosphatase inhibitor design, screening and optimization, which are among the most efficient in industry.
Phosphorylated peptides have limited stability in biological fluids due to the presence of phosphatases. To circumvent this problem, hydrolytically stable phosphate analogs can be incorporated into peptides. Here we show some examples of such phosphate mimetics.
Please also have a look at our PTM Reference & Kits for direct usage as reference material in mass-spectrometry based proteomics to support PTM proteomics.
Depending on the peptide sequence and specification, JPT is able to incorporate the above mentioned analogs into many peptides.
Please contact us to discuss all options.
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