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

Produktnummer ABIN7875509

Dieser Kaninchen Polyklonal Antikörper detektiert spezifisch Peptide Deformylase (Def) in ELISA, WB, FACS, IF und IHC (p). Es zeigt Reaktivität gegenüber Proben von Human, Maus und Ratte.

Kurzübersicht für Peptide Deformylase (Def) (AA 51-199) Antikörper (ABIN7875509)

Target: Peptide Deformylase (Def)

Reaktivität: Human, Maus, Ratte

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Unkonjugiert

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

Produktdetails

Bindungsspezifität: AA 51-199

Verwendungszweck: Peptide deformylase Antibody / PDF

Aufreinigung: 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.

Isotyp: IgG

Anwendungsinformationen

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

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Lyophilized

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

Lagerung: 4 °C,-20 °C

Informationen zur Lagerung: 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.

Antigendetails

Target: Peptide Deformylase (Def)

Andere Bezeichnung: Peptide deformylase

Hintergrund: 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