PDF Mouse Monoclonal Antibody [Clone ID: OTI3C12]

CAT#: TA502989S

PDF mouse monoclonal antibody, clone OTI3C12 (formerly 3C12)

Product Images

HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY PDF (RC205788, Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-PDF. Positive lysates LY411712 (100ug) and LC411712 (20ug) can be purchased separately from OriGene.

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  Western blot analysis of extracts (35ug) from 9 different cell lines by using anti-PDF monoclonal antibody (HepG2: human; HeLa: human; SVT2: mouse; A549: human; COS7: monkey; Jurkat: human; MDCK: canine; PC12: rat; MCF7: human) (1:200).

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  Anti-PDF mouse monoclonal antibody (TA502989) immunofluorescent staining of COS7 cells transiently transfected by pCMV6-ENTRY PDF (RC205788 ).

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  HEK293T cells transfected with either RC205788 overexpress plasmid (Red) or empty vector control plasmid (Blue) were immunostained by anti-PDF antibody (TA502989), and then analyzed by flow cytometry.

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  Flow cytometric Analysis of Hela cells, using anti-PDF antibody (TA502989), (Red), compared to a nonspecific negative control antibody (TA50011), (Blue).

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Specifications

Product Data

• Clone Name: OTI3C12
• Applications: FC, IF, WB
• Recommended Dilution: WB 1:500, IF 1:100, FLOW 1:100
• Reactivities: Human
• Host: Mouse
• Isotype: IgG1
• Clonality: Monoclonal
• Immunogen: Full length human recombinant protein of human PDF (NP_071736) produced in HEK293T cell.
• Formulation: PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
• Concentration: 1 mg/ml
• 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.
• Predicted Protein Size: 19.4 kDa
• Gene Name: peptide deformylase, mitochondrial
• Database Link:
  NP_071736
  Entrez Gene 64146 Human
  UniProt ID 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]