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PDF Antibody (Center)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • WB - PDF Antibody (Center) AP19023c
    PDF Antibody (Center) (Cat. #AP19023c) western blot analysis in MDA-MB453 cell line lysates (35ug/lane).This demonstrates the PDF antibody detected the PDF protein (arrow).
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  • SPECIFICATION
  • CITATIONS
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, E
Primary Accession Q9HBH1
Other Accession NP_071736.1
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 27013 Da
Antigen Region 125-151 aa
Additional Information
Gene ID 64146
Other Names Peptide deformylase, mitochondrial, Polypeptide deformylase, PDF, PDF1A
Target/Specificity This PDF antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 125-151 amino acids from the Central region of human PDF.
Dilution WB~~1:1000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPDF Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name PDF {ECO:0000303|PubMed:19236878}
Function Removes the formyl group from the N-terminal Met of newly synthesized proteins.
Cellular Location Mitochondrion
Tissue Location Ubiquitous..
Research Areas
Citations (0)
citation

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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.

References

Escobar-Alvarez, S., et al. J. Mol. Biol. 387(5):1211-1228(2009)
Wang, L., et al. Cancer Epidemiol. Biomarkers Prev. 17(12):3558-3566(2008)
Lee, M.D., et al. J. Clin. Invest. 114(8):1107-1116(2004)
Serero, A., et al. J. Biol. Chem. 278(52):52953-52963(2003)
Lee, M.D., et al. Biochem. Biophys. Res. Commun. 312(2):309-315(2003)

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$ 365.00
$ 140.00
Cat# AP19023c
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