Rabbit PDF Polyclonal Antibody | anti-PDF antibody

PDF Polyclonal Antibody

Cat. Num. AAA9130962

• Reactivity: Human, Mouse, Rat
• Applications: Western Blot
• Purity: Affinity Purification
• Synonyms: PDF; Polyclonal Antibody; PDF Polyclonal Antibody; anti-PDF antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Affinity Purification
• Sequence Length: 243

• Applicable Applications for anti-PDF antibody: Western Blot (WB)
• Application Notes: WB: 1:500 - 1:2000
• Immunogen: Recombinant protein of human PDF
• Storage Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
• Preparation and Storage: Store at -20 degree C. Avoid freeze/thaw cycles.

Western Blot (WB)

(Western blot analysis of extracts of various cell lines, using PDF antibody at 1:1000 dilution.Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (MBS128200) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Basic Kit.Exposure time: 30s.)

Related Product Information for anti-PDF antibody

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.

Product Categories/Family for anti-PDF antibody

Primary antibody

NCBI and Uniprot Product Information

• NCBI GI #: 17433054
• NCBI GeneID: 64146
• UniProt Accession #: Q9HBH1; Q8WUN6
• Molecular Weight: 27kDa
• NCBI Official Full Name: Peptide deformylase, mitochondrial
• NCBI Official Synonym Full Names: peptide deformylase (mitochondrial)
• NCBI Official Symbol: PDF
• NCBI Protein Information: peptide deformylase, mitochondrial
• UniProt Protein Name: Peptide deformylase, mitochondrial
• Protein Family: Protein
• UniProt Gene Name: PDF
• UniProt Synonym Gene Names: PDF1A

NCBI Description

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, Nov 2008]

Uniprot Description

PDF: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Belongs to the polypeptide deformylase family.

Protein type: EC 3.5.1.88; Hydrolase; Mitochondrial

Chromosomal Location of Human Ortholog: 16q22.1

Cellular Component: mitochondrion

Molecular Function: peptide deformylase activity

Biological Process: co-translational protein modification; N-terminal protein amino acid modification; peptidyl-methionine modification; positive regulation of cell proliferation