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PDF Mouse anti-Human, Clone: OTI3F3, Invitrogen™

Mouse Monoclonal Antibody

Manufacturer:  Invitrogen MA525562

Catalog No. PIMA525562


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Description

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.
Specifications

Specifications

PDF
Monoclonal
0.78 mg/mL
PBS with 1% BSA, 50% glycerol and 0.02% sodium azide; pH 7.3
Q9HBH1
Peptide deformylase, mitochondrial, Polypeptide deformylase, PDF, PDF1A
Mouse
IgG2b
100 μL
-20° C, Avoid Freeze/Thaw Cycles
Primary
64146
Flow Cytometry, Immunocytochemistry, Immunofluorescence, Western Blot
OTI3F3
Unconjugated
PDF
Liquid
PDF
Full length human recombit protein of PDF produced in E.coli
Affinity Chromatography
RUO
Antibody
Monoclonal
Human
Documents
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