Protein Prenylation – one Target for multiple Diseases

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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.

Selected references:
[1] Hougland et al. (2009) Getting a handle on protein prenylation. Nat. Chem. Biol. 5 (4):197.
[2] Nguyen et al. (2009) Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nat. Chem. Biol. 5 (4):227.


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