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The antibody against PDF was raised in rabbit using the Recombinant Human Peptide deformylase, mitochondrial protein (16-143AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC.
The antibody against PDF was raised in rabbit using the Recombinant Human Peptide deformylase, mitochondrial protein (16-143AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC.
$299.00
| Cat.No | ADC-09003A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | |
| Target Synonyms | PDF antibody; PDF1A antibody; Peptide deformylase antibody; mitochondrial antibody; EC 3.5.1.88 antibody; Polypeptide deformylase antibody | Form | Liquid |
| Species Reactivity | Human | Isotype | IgG |
| Storage Buffer | 0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4 | Purification Method | >95%, Protein G purified |
| Conjugate | Non-conjugated | Application | ELISA, IHC, WB |
| Storage | Upon receipt |
| Immunogen Description | Recombinant Human Peptide deformylase, mitochondrial protein (16-143AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | Q9HBH1 |
Uniprot Id
Q9HBH1
Target Species
Human
Target Name
Target Full Name
Peptide deformylase, mitochondrial
Target Function
Removes the formyl group from the N-terminal Met of newly synthesized proteins.
Target Subcellular Location
Mitochondrion.
Target Protein Families
Polypeptide deformylase family
Target Tissue Specificity
Ubiquitous.
Target Synonyms
PDF; PDF1A; Peptide deformylase; mitochondrial; EC 3.5.1.88; Polypeptide deformylase
Target 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.
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