PDF Mouse Monoclonal Antibody [Clone ID: OTI3C12]

SKU CF502989

Carrier-free (BSA/glycerol-free) PDF mouse monoclonal antibody, clone OTI3C12 (formerly 3C12)

Product Data

• Clone Name: OTI3C12
• Application: FC, IF, WB
• Recommended Dilution: WB 1:500, IF 1:100, FLOW 1:100
• Reactivity: Human
• Antibody Host: Mouse
• Isotype: IgG1
• Clonality: Monoclonal
• Immunogen: Full length human recombinant protein of human PDF (NP_071736) produced in HEK293T cell.
• Buffer: Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose)
• Reconstitution Method: For reconstitution, we recommend adding 100uL distilled water to a final antibody concentration of about 1 mg/mL. To use this carrier-free antibody for conjugation experiment, we strongly recommend performing another round of desalting process. (OriGene recommends Zeba Spin Desalting Columns, 7KMWCO from Thermo Scientific)
• Purification: Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)
• Conjugation: Unconjugated
• Storage: Store at -20°C as received.
• Stability: Stable for 12 months from date of receipt.
• Shipping: Ambient
• Predicted Protein Size: 19.4 kDa
• Gene Name: peptide deformylase, mitochondrial
• Database Link:
  NP_071736
  Q9HBH1
• 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. [provided by RefSeq]

Reference Data