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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|Name:||Furin site, aa 164-176, RKKR, is changed to PGG|
|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|
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