Prenylation is a post-translational lipid modification that targets membrane proteins and plays a key role in cell signaling pathways in cancer and microbial infection.
Most prenylated proteins are localized at cell membranes, at least for a portion of their lives, and the isoprenoid modification is generally essential for membrane association.
Most prenylated proteins play important roles in signal transduction. A major question in the field is whether protein-protein interactions in pathways involving prenylated proteins depend on prenylation. However, this on-demand concern has not been addressed since the modification effects regarding protein-protein interactions are challenging to examine separately from their effects on membrane association. Nevertheless, in a few cases, evidence has been discovered to prove that the prenyl group is important for protein-protein interactions.
The development of protein prenylation inhibitors is a research focus for groups from academia and the pharmaceutical industry. The primary driving force for such efforts came from the earlier finding that the oncogenic forms of Ras proteins required farnesylation for further cellular transformation. Ras proteins are key players in signal transduction associated with cell growth and development.
There is considerable interest in identifying prenylated proteins in a cellular context in order to determine which prenyltransferase protein substrates have the prenylation status. Chemical proteomic methods have been highly useful in this regard. In this approach, metabolic labeling of living cells is first carried out using isoprenoid analogs to tag prenylated proteins with a reporter group, such as azide or alkyne. These tagged proteins are then functionalized via bioorthogonal reactions to install either a fluorophore for gel-based proteomic studies or a biotin moiety for the enrichment of tagged proteins.
As an industry leader in PTMs, Creative Proteomics offers a large-scale prenylated proteome service package covering from mass spectrometry to enrichment processing. By using this service, customers will only need to send in the sample of investigation and leave the rest to our team, including but not limited to protein extraction, proteolysis, peptide separation, mass spectrometry analysis, mass spectrometry raw data analysis, and bioinformatics analysis.
Target modified protein labeling (Depending on provided sample types)
Isoprenylated peptide enrichment (Optional; Depending on the abundance of phosphorylated peptides)
HPLC separation, followed by MS/MS analysis
Prenylation site data analysis
Wide range of applications: Qualitative and relative quantitative analysis of various protein prenylation sites with reliable and reliable results
Simple and convenient operation: No radioisotope labeling or Edman degradation sequencing for amino acids
High site coverage (optional): Prenylated peptides can be labeled to enhance detection coverage
1. Distefano M.D., Albers L.N., Xu J. (2005) Protein Prenylation. In: Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine. Springer,
2. Charuta C. Palsuledesai and Mark D. Distefano Protein Prenylation: Enzymes, Therapeutics, and Biotechnology Applications ACS Chemical Biology 2015 10 (1), 51-62.
3. Fang L. Zhang and Patrick J. Casey PROTEIN PRENYLATION: Molecular Mechanisms and Functional Consequences Annu Rev. Biochem. 1996. 65:24149.