PA-3M (Anthrax Protective Mutant Antigen (PA-3M))
Contains three mutated residues (D683A, L685E, Y688K), which are involved in the interaction of the protective antigen (PA) with its receptors. This mutated PA is unable to bind to its receptor. It provides a useful negative control in many studies.
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.
Contains three mutated residues (D683A, L685E, Y688K), which are involved in the interaction of the protective antigen (PA) with its receptors. This mutated PA is unable to bind to its receptor. It provides a useful negative control in many studies.
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: | D683A, L685E, Y688K |
| Alternative Name(s): | PA-3M |
| Accession ID: | P13423 |
| Strain: | Expressed in avirulent engineered B. anthracisstrain BH450 |
| Format: | Purified protein (liquid) |
| Purity: | Hydroxyapatite Chromatography |
| Buffer: | 5 mM Hepes pH 7.5, 0.50 mM EDTA |
| Concentration: | 4.86mg/mL |
| Storage: | -80C |
| Shipped: | Dry ice |
- Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.
- Rosovitz, M. J., Schuck, P., Varughese, M., Chopra, A. P., Mehra, V., Singh, Y., McGinnis, L. M., and Leppla, S. H. (2003) Alanine scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody. J.Biol.Chem. 278, 30936-30944
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