Technical Data
Bacillus anthracis (Anthrax) EF (Edema Factor) Protein
Anthrax infection is initiated by the inhalation, ingestion, or cutaneous contact with Bacillus anthracis endospores. B. anthracis produces three polypeptides that comprise the anthrax toxin: protective antigen (PA), lethal factor (LF), and edema factor (EF) (1,2 for review). PA binds to two related proteins on the cell surface; these are termed tumor epithelial marker 8 (TEM8)/anthrax toxin receptor (ATR) (3) and capillary morphogenesis protein 2 (CMG2) (4), although it is still unclear which is physiologically relevant. Following PA binding to its receptor, PA is cleaved into two fragments by a furin-like protease. The bound fragment binds both LF and EF; the resulting complex is then endocytosed which allows the translocation of LF and EF into the cytoplasm (5). EF is a calmodulin and Ca++-dependent adenylate cyclase responsible for the edema seen in the disease. It is thought to benefit the B. anthracis bacteria by inhibiting cells of the host immune system.

Suitable for use in ELISA. Other applications not tested.

Recommended Dilution:
ELISA: It will detect 10ng of free peptide at 1ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C. For long-term storage, aliquot and store at 4C. Do not freeze. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.
100ug4C Do Not FreezeBlue IceRabbit
Not determined
Rabbit anti-Anthrax EF protein polyclonal antibody was raised against a synthetic peptide corresponding to 16 amino acids near the carboxy terminus of the Anthrax edema factor protein
Supplied as a liquid in PBS, 0.02% sodium azide.
Recognizes Anthrax Edema Factor (EF).
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Schwartz MN. Recognition and management of anthrax an update. New Engl. J. Med. 2001; 345:1621-6. 2. Moayeri M and Leppla SH. The roles of anthrax toxin in pathogenesis. Curr. Opin. Microbiol. 2004; 7:19-24. 3. Bradley KA, Mogridge J, Mourez M, et al. Identification of the cellular receptor for anthrax toxin. Nature 2001; 414:225-9. 4. Scobie HM, Rainey GJ, Bradley KA, et al. Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor. Proc. Natl. Acad. Sci. USA 2003; 100:5170-4. 5. Singh Y, Klimpel KR, Goel S, et al. Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytotic uptake into mammalian cells. Infect. Immun. 1999; 67:1853-9. 6. Collier RJ and Young JA. Anthrax toxin. Annu. Rev. Cell Dev. Biol. 2003; 19:45-70.