Background：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.
仕様
Synonyms：CG6496,DEFM,mitochondrial,Pdf,PDF1A,Peptide deformylase,Peptide deformylase like protein,Peptide deformylase, mitochondrial,Polypeptide deformylase
Host：Rabbit
Reactivity：Human,Mouse,Rat
Applications：WB
Concentration：1mg/ml
Immunogen：Recombinant protein of human PDF
Purification Method：Affinity purification
Clonality：Polyclonal
Conjugation：Unconjugated
Buffer：Buffer： PBS with 0.02％ sodium azide, 50％ glycerol, pH7.3.
Dilution：WB1：500 - 1：2000
Gene_ID（human）：64146
Swissprot：Q9HBH1
Isotype：IgG
Research Areas：Cancer, Cell Biology, Epigenetics and Nuclear Signaling, Metabolism, Signal transduction
