PA-U7 (Anthrax Protective Mutant Antigen (PA-U7))
Protective antigen (PA) mutant in which the furin site, aa 164-167, RKKR, is changed to PGG. This PA cannot be proteolytically activated, so it cannot make an oligomer, is not internalized rapidly into cells, and cannot internalize LF and EF. This provides a useful negative control in many studies. This protein can still bind to the toxin receptors, and therefore acts as a competitive toxin inhibitor. This allows its use in Schild plot analyses to measure PA affinity for receptors.
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.
Protective antigen (PA) mutant in which the furin site, aa 164-167, RKKR, is changed to PGG. This PA cannot be proteolytically activated, so it cannot make an oligomer, is not internalized rapidly into cells, and cannot internalize LF and EF. This provides a useful negative control in many studies. This protein can still bind to the toxin receptors, and therefore acts as a competitive toxin inhibitor. This allows its use in Schild plot analyses to measure PA affinity for receptors.
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.
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| Product Type: | Protein |
| Name: | Furin site, aa 164-176, RKKR, is changed to PGG |
| Alternative Name(s): | PA-U7 |
| Accession ID: | P13423 |
| Strain: | Expressed in avirulent engineered B. anthracisstrain BH450 |
| Format: | Purified protein (liquid) |
| Purity: | S200 Size Exclusion Chromatography |
| Buffer: | 10 mM Tris-HCl pH 8 and 100 mM NaCl , 0.5 mM EDTA |
| Concentration: | 7.47mg/mL |
| Storage: | -80C |
| Shipped: | Dry ice |
- Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.
- Liu, S., Bugge, T. H., and Leppla, S. H. (2001) Targeting of tumor cells by cell surface urokinase plasminogen activator-dependent anthrax toxin. J.Biol.Chem. 276, 17976-17984
- Chen, K. H., Liu, S., Bankston, L. A., Liddington, R. C., and Leppla, S. H. (2007) Selection of anthrax toxin protective antigen variants that discriminate between the cellular receptors TEM8 and CMG2 and achieve targeting of tumor cells. J.Biol.Chem. 282, 9834-9846
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