|Other Names||Peptide deformylase, mitochondrial, Polypeptide deformylase, PDF, PDF1A|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Removes the formyl group from the N-terminal Met of newly synthesized proteins.|
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Provided below are standard protocols that you may find useful for product applications.
Protein synthesis proceeds after formylation of methionineby methionyl-tRNA formyl transferase (FMT) and transfer of thecharged initiator f-met tRNA to the ribosome. In eubacteria andeukaryotic organelles the product of this gene, peptide deformylase(PDF), removes the formyl group from the initiating methionine ofnascent peptides. In eubacteria, deformylation of nascent peptidesis required for subsequent cleavage of initiating methionines bymethionine aminopeptidase. The discovery that a natural inhibitorof PDF, actinonin, acts as an antimicrobial agent in some bacteriahas spurred intensive research into the design ofbacterial-specific PDF inhibitors. In human cells, onlymitochondrial proteins have N-formylation of initiatingmethionines. Protein inhibitors of PDF or siRNAs of PDF block thegrowth of cancer cell lines but have no effect on normal cellgrowth. In humans, PDF function may therefore be restricted torapidly growing cells.
Escobar-Alvarez, S., et al. J. Mol. Biol. 387(5):1211-1228(2009)Wang, L., et al. Cancer Epidemiol. Biomarkers Prev. 17(12):3558-3566(2008)Lee, M.D., et al. J. Clin. Invest. 114(8):1107-1116(2004)Serero, A., et al. J. Biol. Chem. 278(52):52953-52963(2003)Lee, M.D., et al. Biochem. Biophys. Res. Commun. 312(2):309-315(2003)
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