PA D512K (Anthrax Protective Mutant Antigen (PA-D512K))
Dominant negative (D512K) protective antigen (PA), inactive mutant. This mutant PA cannot oligomerize. However, it can be complemented by PA GN or PA NS, with which it forms active octamers.
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.
Dominant negative (D512K) protective antigen (PA), inactive mutant. This mutant PA cannot oligomerize. However, it can be complemented by PA GN or PA NS, with which it forms active octamers.
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: | D512K |
| Alternative Name(s): | PA D512K |
| Accession ID: | P13423 |
| Strain: | Expressed in avirulent engineered B. anthracisstrain BH460 |
| Format: | Purified protein (liquid) |
| Purity: | Hydroxyapatite Chromatography |
| Buffer: | 5 mM Hepes pH 7.5, 0.50 mM EDTA |
| Concentration: | 1.84mg/mL |
| Storage: | -80C |
| Shipped: | Dry ice |
- Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.
- Mogridge, J., Mourez, M., and Collier, R. J. (2001) Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin. J.Bacteriol. 183, 2111-2116
- Mogridge, J., Cunningham, K., Lacy, D. B., Mourez, M., and Collier, R. J. (2002) The lethal and edema factors of anthrax toxin bind only to oligomeric forms of the protective antigen. Proc.Natl.Acad.Sci.U.S.A. 99, 7045-7048
- Phillips, D. D., Fattah, R. J., Crown, D., Zhang, Y., Liu, S., Moayeri, M., Fischer, E. R., Hansen, B. T., Ghirlando, R., Nestorovich, E. M., Wein, A. N., Simons, L., Leppla, S. H., and Leysath, C. E. (2013) Engineering anthrax toxin variants that exclusively form octamers, and their application to targeting tumors. J.Biol.Chem. 288, 9058-9065
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