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PDF / PLAB

Peptide Deformylase (mitochondrial)

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.

Gene Name: Peptide Deformylase (mitochondrial)
Synonyms: PDF, MIC1, PDF1A, PLAB, Polypeptide deformylase
Target Sequences: NM_022341 NP_071736.1 Q9HBH1

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PDF / PLAB Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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HEK 293 Cells
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19.4 kDa
100 µg/$494
PDF / PLAB Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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293T Cells
Myc-DDK (Flag)
19.4 kDa
20 µg/$150
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PLEASE NOTE

For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.

The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).