Description
PDF Antibody | 13-663 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 40-243 of human PDF (NP_071736.1) .
Research Area: Cancer, Cell Cycle, Signal Transduction
Tested Application: WB
Application: WB: 1:500 - 1:2000
Specificiy: N/A
Positive Control 1: MCF7
Positive Control 2: SW620
Positive Control 3: A-549
Positive Control 4: HepG2
Positive Control 5: K-562
Positive Control 6: Mouse heart
Molecular Weight: Observed: 20kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: Peptide deformylase, mitochondrial, Polypeptide deformylase, PDF, PDF1A
User Note: Optimal dilutions for each application to be determined by the researcher.
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.