GeneBio Systems
Anti-PDF Antibody Picoband®
Anti-PDF Antibody Picoband®
SKU:A00304-1
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Size: 100 μg
Storage: At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.
Form: Lyophilized
Reactivity: Human,Mouse,Rat
Applications: WB,IHC,IF,Flow Cytometry,ELISA
Application Details: Western blot, 0.25-0.5 μg/ml, Human, Mouse, Rat
Immunohistochemistry (Paraffin-embedded Section), 2-5 μg/ml, Human
Immunofluorescence, 5 μg/ml, Human
Flow Cytometry (Fixed), 1-3 μg/1x106 cells, Human
ELISA, 0.1-0.5 μg/ml, -
Gene Name: PDF
Specificity:
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.
Immunogen: E.coli-derived human PDF recombinant protein (Position: H51-Q199). Human PDF shares 82.4% amino acid (aa) sequence identity with mouse PDF.
Clonality: Polyclonal
Contents: Each vial contains 4 mg Trehalose, 0.9 mg NaCl, 0.2 mg Na2HPO4.
Purification: Immunogen affinity purified.
Reconstitution: Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.
Reference: 1. Escobar-Alvarez, S., Goldgur, Y., Yang, G., Ouerfelli, O., Li, Y., Scheinberg, D. A. Structure and activity of human mitochondrial peptide deformylase, a novel cancer target. J. Molec. Biol. 387: 1211-1228, 2009. 2. Giglione, C., Serero, A., Pierre, M., Boisson, B., Meinnel, T. Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J. 19: 5916-5929, 2000. 3. Lee, M. D., Antczak, C., Li, Y., Sirotnak, F. M., Bornmann, W. G., Scheinberg, D. A. A new human peptide deformylase inhibitable by actinonin. Biochem. Biophys. Res. Commun. 312: 309-315, 2003.
Uniprot ID: Q9HBH1
Host: Rabbit
Concentration: Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.
Conjugate:
Cross Reactivity: No cross reactivity with other proteins.
Isotype: IgG
Phospho_site:
Clone Number:
Observed Molecular Weight: 25 kDa
Calculated Molecular Weight: 52588 MW
Gene ID: 64146
Protein Name: Peptide deformylase, mitochondrial
Gene Full Name: peptide deformylase, mitochondrial
Synonyms: PDF; PDF1A; Polypeptide deformylase
