PDF Antilichaam

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.

64146

Q9HBH1

Human, Mouse, Rat

Recombinant fusion protein containing a sequence corresponding to amino acids 40-243 of human PDF (NP_071736.1) .

Unconjugated

Primary Antibodies

Cancer, Cell Cycle, Signal Transduction

Affinity purification

MCF7

Batch dependent

PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

None

Blue Ice

Store at -20˚ C. Avoid freeze / thaw cycles.

Observed: 20kDa

IgG

WB: 1:500 - 1:2000

PDF

SW620

A-549

HepG2

K-562

Mouse heart

Peptide deformylase, mitochondrial

Homo sapiens

Peptide deformylase, mitochondrial, Polypeptide deformylase, PDF, PDF1A

WB

Liquid