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

N° du produit ABIN7875509

Cet anticorps Lapin Polyclonal détecte spécifiquement Peptide Deformylase (Def) dans ELISA, WB, FACS, IF et IHC (p). Il présente une réactivité avec des échantillons de Humain, Souris et Rat.

Aperçu rapide pour Peptide Deformylase (Def) (AA 51-199) anticorps (ABIN7875509)

Antigène: Peptide Deformylase (Def)

Reactivité: Humain, Souris, Rat

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Inconjugué

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

Détail du produit

Épitope: AA 51-199

Fonction: Peptide deformylase Antibody / PDF

Purification: Antigen affinity chromatography

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

Isotype: IgG

Information d'application

Indications d'application: Optimal dilution of the Peptide deformylase antibody should be determined by the researcher.

Restrictions: For Research Use only

Stockage

Format: Lyophilized

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

Stock: 4 °C,-20 °C

Stockage commentaire: 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.

Détail du antigène

Antigène: Peptide Deformylase (Def)

Autre désignation: Peptide deformylase

Sujet: 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