Protein synthesis proceeds after formylation of methionine by methionyl-tRNA formyl transferase (FMT) and transfer of the charged initiator f-met tRNA to the ribosome. In eubacteria and eukaryotic organelles the product of this gene, peptide deformylase (PDF), removes the formyl group from the initiating methionine of nascent peptides. In eubacteria, deformylation of nascent peptides is required for subsequent cleavage of initiating methionines by methionine aminopeptidase. The discovery that a natural inhibitor of PDF, actinonin, acts as an antimicrobial agent in some bacteria has spurred intensive research into the design of bacterial-specific PDF inhibitors. In human cells, only mitochondrial proteins have N-formylation of initiating methionines. Protein inhibitors of PDF or siRNAs of PDF block the growth of cancer cell lines but have no effect on normal cell growth. In humans, PDF function may therefore be restricted to rapidly growing cells. [provided by RefSeq]

Alternate Names

EC 3.5.1.88, GDF15, MIC1, PDF1A, peptide deformylase (mitochondrial), peptide deformylase, mitochondrial, peptide deformylase-like protein, PLAB, Polypeptide deformylase

Gene Symbol

PDF

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Product Specific Notices for PDF Antibody (OTI3F3) [DyLight 755]

DyLight (R) is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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PDF Antibody (OTI3F3) [DyLight 755]

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-73301IR

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Background: PDF

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Additional PDF Products

Product Documents for PDF Antibody (OTI3F3) [DyLight 755]

Product Datasheets

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Product Specific Notices for PDF Antibody (OTI3F3) [DyLight 755]

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