Technical Data

B0003-05P
Clone Type
Polyclonal
Host
Rabbit
Isotype
IgG
Grade
Affinity Purified
Applications
E
Shipping Temp
Blue Ice
Storage Temp
-20°C
Rabbit Anti-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 (6).

Applications
Suitable for use in ELISA. Other applications have not been tested.
Recommended Dilution
Optimal dilution determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic peptide corresponding to 16 amino acids near the carboxy terminus of the Anthrax Edema Factor protein.
Form
Supplied as a liquid in PBS, pH 7.4, 0.02% sodium azide.
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes Anthrax EF.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
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.
USBio References
No references available
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