PA F427A (Anthrax Protective Mutant Antigen (PA F427A))

Dominant negative F427A protective antigen (PA) mutant that fails to translocate LF and EF. The F427 residue is in the lumen of the channel, where the ring of 7 or 8 F residues constitutes the “Psi clamp”, which is necessary for translocation of LF and EF polypeptides.

Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis, the causative agent of anthrax. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). Anthrax is caused by B. anthracis, a spore-forming, Gram positive, rod-shaped bacterium. The lethality of the disease is caused by the bacterium's two principal virulence factors: the polyglutamic acid capsule, which is anti-phagocytic, and the tripartite protein toxin, called anthrax toxin.

From the laboratory of Stephen H. Leppla, PhD, National Institute of Allergy and Infectious Diseases/NIH.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
PA F427A (Anthrax Protective Mutant Antigen (PA F427A))
100ug (2.23mg/mL) In stock
Regular Price:$336.00
On Sale:

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Product Type: Protein
Name: F427A
Alternative Name(s): PA F427A
Accession ID: P13423
Strain: Expressed in avirulent engineered B. anthracisstrain BH480
Format: Purified protein (liquid)
Purity: Hydroxyapatite Chromatography
Buffer: 10 mM HEPES pH 7.5, 0.50 mM EDTA
Concentration: 2.23mg/mL
Storage: -80C
Shipped: Dry ice

From the laboratory of Stephen H. Leppla, PhD, National Institute of Allergy and Infectious Diseases/NIH.
  1. Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.
  2. Krantz, B. A., Melnyk, R. A., Zhang, S., Juris, S. J., Lacy, D. B., Wu, Z., Finkelstein, A., and Collier, R. J. (2005) A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science 309, 777-781
  3. Sun, J., Lang, A. E., Aktories, K., and Collier, R. J. (2008) Phenylalanine-427 of anthrax protective antigen functions in both pore formation and protein translocation. Proc.Natl.Acad.Sci.U.S.A. 105, 4346-4351
  4. Bezrukov, S. M., Liu, X., Karginov, V. A., Wein, A. N., Leppla, S. H., Popoff, M. R., Barth, H., and Nestorovich, E. M. (2012) Interactions of high-affinity cationic blockers with the translocation pores of B. anthracis, C. botulinum, and C. perfringens binary toxins. Biophys.J. 103, 1208-1217

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