FP59 (Anthrax Lethal Factor Fusion to Pseudomonas Exotoxin A Catalytic Domain (FP59-AGG))
A fusion protein of LF residues 1-254 with the catalytic domain III of Pseudomonas exotoxin A. The “AGG” suffix indicates that this protein has the native A-terminal sequence of LF. This protein is delivered like LF and EF into the cell cytosol, where the exotoxin A domain III causes ADP-ribosylation of EF-2 to block protein synthesis and cause cell death. This is a convenient tool for assessing the presence of toxin receptors and the integrity of the uptake process, since cell death (occurring after 24-48 hours) is easily measured. This protein is functionally equivalent to the widely used protein LFn-DTA, which contains the diphtheria toxin catalytic domain.
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.
A fusion protein of LF residues 1-254 with the catalytic domain III of Pseudomonas exotoxin A. The “AGG” suffix indicates that this protein has the native A-terminal sequence of LF. This protein is delivered like LF and EF into the cell cytosol, where the exotoxin A domain III causes ADP-ribosylation of EF-2 to block protein synthesis and cause cell death. This is a convenient tool for assessing the presence of toxin receptors and the integrity of the uptake process, since cell death (occurring after 24-48 hours) is easily measured. This protein is functionally equivalent to the widely used protein LFn-DTA, which contains the diphtheria toxin catalytic domain.
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: | LFn-Pseudomonas exotoxin A domain III |
| Alternative Name(s): | FP59-AGG |
| Accession ID: | P15917 |
| Source: | Expressed in avirulent engineered B. anthracisstrain BH460 |
| Format: | Purified protein (liquid) |
| Purity: | Q-Sepharose Ion Exchange Chromatography |
| Buffer: | 5 mM Hepes pH 7.5, 0.50 mM EDTA |
| Concentration: | 1.68mg/mL |
| Storage: | -80C |
| Shipped: | Dry ice |
- Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.
- Arora, N., Klimpel, K. R., Singh, Y., and Leppla, S. H. (1992) Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells. J.Biol.Chem. 267, 15542-15548
- Milne, J. C., Blanke, S. R., Hanna, P. C., and Collier, R. J. (1995) Protective antigen-binding domain of anthrax lethal factor mediates translocation of a heterologous protein fused to its amino- or carboxy- terminus. Mol.Microbiol. 15, 661-666
- van Rijn JM, Werner L, Aydemir Y, Spronck JMA, Pode-Shakked B, van Hoesel M, Shimshoni E, Polak-Charcon S, Talmi L, Eren M, Weiss B, H J Houwen R, Barshack I, Somech R, Nieuwenhuis EES, Sagi I, Raas-Rothschild A, Middendorp S, Shouval DS. Enhanced Collagen Deposition in the Duodenum of Patients with Hyaline Fibromatosis Syndrome and Protein Losing Enteropathy. Int J Mol Sci. 2020 Nov 2;21(21):8200. View article
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