Peptide Deformylase (Def) (AA 51-199) antibody

Catalog No. ABIN7875509

This Rabbit Polyclonal antibody specifically detects Peptide Deformylase (Def) in ELISA, WB, FACS, IF and IHC (p). It exhibits reactivity toward Human, Mouse and Rat.

Quick Overview for Peptide Deformylase (Def) (AA 51-199) antibody (ABIN7875509)

Target: Peptide Deformylase (Def)

Reactivity: Human, Mouse, Rat

Host: Rabbit

Clonality: Polyclonal

Conjugate: Un-conjugated

Application: ELISA, Western Blotting (WB), Flow Cytometry (FACS), Immunofluorescence (IF), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))

Product Details

Binding Specificity: AA 51-199

Purpose: Peptide deformylase Antibody / PDF

Purification: Antigen affinity chromatography

Immunogen: An E.coli-derived human recombinant protein (amino acids H51-Q199) was used as the immunogen for the Peptide deformylase antibody.

Isotype: IgG

Application Details

Application Notes: Optimal dilution of the Peptide deformylase antibody should be determined by the researcher.

Restrictions: For Research Use only

Handling

Format: Lyophilized

Buffer: 0.5 mg/mL if reconstituted with 0.2 mL sterile DI water

Storage: 4 °C,-20 °C

Storage Comment: After reconstitution, the Peptide deformylase antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.

Target Details

Target: Peptide Deformylase (Def)

Alternative Name: Peptide deformylase

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.

UniProt: Q9HBH1