EF K313R (Anthrax Edema Factor Mutant (EF-A K313R))

This is an inactive, catalytic site mutant of edema factor (EF). The K313 residue is within the sequence VATKG. Others have described this residue as K346 because they numbered residues starting with the signal sequence. Our numbering is for the mature protein. This version of EF has the N-terminal A residue, which would make it the most active EF if the catalytic site were not mutated.

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.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
EF K313R (Anthrax Edema Factor Mutant (EF-A K313R))
100ug (1.24mg/mL) In stock
Regular Price:$355.00
On Sale:

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Product Type: Protein
Name: K313R
Alternative Name(s): EF-A K313R
Source: Expressed in avirulent engineered B. anthracisstrain BH480
Format: Purified protein (liquid)
Purity: Hydroxyapatite Chromatography
Buffer: 5 mM Hepes pH 7.5, 0.50 mM EDTA
Concentration: 1.24mg/mL
Storage: -80C
Shipped: Dry ice

From the laboratory of Stephen H. Leppla, PhD, National Institute of Allergy and Infectious Diseases/NIH.
  1. Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.
  2. Labruyere, E., Mock, M., Surewicz, W. K., Mantsch, H. H., Rose, T., Munier, H., Sarfati, R. S., and Barzu, O. (1991) Structural and ligand-binding properties of a truncated form of Bacillus anthracis adenylate cyclase and of a catalytically inactive variant in which glutamine substitutes for lysine-346. Biochemistry 30, 2619-2624
  3. Leysath, C. E., Phillips, D. D., Crown, D., Fattah, R. J., Moayeri, M., and Leppla, S. H. (2013) Anthrax edema factor toxicity is strongly mediated by the N-end rule. PLoS ONE 8, e74474

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