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.
In order to purchase this product, we require a Letter of Assurance form to be completed. Download form here: Kerafast Letter of Assurance
|Name:||LFn-Pseudomonas exotoxin A domain III|
|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|
If you publish research with this product, please let us know so we can cite your paper.