Name: Anti-PDF antibody
Price: 297.00 USD

Overview
- 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.
  
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Properties
- Host
  
  rabbit
  
  Antibody Type
  
  polyclonal
  
  Isotype
  
  IgG
  
  Reactivity
  
  human; mouse; rat
  
  Immunogen
  
  Recombinant fusion protein containing a sequence corresponding to amino acids 40-243 of human PDF (NP_071736. 1).
  
  Purification
  
  Affinity purification
  
  Conjugate
  
  Unconjugated
  
  Formulation
  
  PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
  
  Storage
  
  Store at -20°C and avoid freeze-thaw cycles.
  
  Regulatory Status
  
  RUO
  
  Antigen
  
  Peptide Deformylase-Mitochondrial; Polypeptide Deformylase (Gene ID:64146; UniProt:Q9HBH1)
  
  * For research use only