Protein Prenylation ranks among the most common lipid modifications of proteins, affecting up to 2 % of the proteins in the mammalian proteome.
Three different protein prenyltransferases (FTase, GGTase-I and RabGGTase) catalyze the attachment of either a 15-carbon farnesyl or 20-carbon geranylgeranyl moiety to one or two cysteine residues near the C-terminus of the target protein.
Monitoring of protein prenylation in vivo and in vitro has become an important topic since prenylation affects a number of signal transduction cascades in cell cycling, apoptosis, glycogen metabolism and cell movement. Conjugating lipid donors with functional groups has emerged as a promising approach for such analyses.
The universal lipid donor - Biotin-labeled Geranyl Pyrophosphate B-GPP - is now available from Jena Bioscience:
B-GPP is tolerated by RabGGTase and engineered mutants of FTase and GGTase-I and introduces a biotin group during prenylation. This allows detection of femtomolar amounts of all prenylated proteins in eukaryotic cells and tissues and thereby offers next generation prenylome studies [1,2].
Please view our Protein Prenylation Section for all corresponding products such as native and engineered protein prenyl transferases, natural and synthetic lipid donors, substrates and selective inhibitors.
 Hougland et al. (2009) Getting a handle on protein prenylation. Nat. Chem. Biol. 5 (4):197.
 Nguyen et al. (2009) Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nat. Chem. Biol. 5 (4):227.