Technical Data
B0003-05P6
Bacillus anthracis (Anthrax) EF (Edema Factor) Protein (CT)
Description:
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). PA binds to two related proteins on the cell surface; these are termed tumor epithelial marker 8 (TEM8)/anthrax toxin receptor (ATR) and capillary morphogenesis protein 2 (CMG2), 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. 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.

Applications:
Suitable for use in ELISA. Other applications not tested.

Recommended Dilution:
ELISA: 1ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
100ug-20°CBlue IceRabbit
Concentration:
~1mg/ml
Immunogen:
Synthetic peptide corresponding to 16aa near the C-terminal of the Anthrax edema factor protein (P40136).
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in PBS, 0.02% sodium azide.
Specificity:
Recognizes Bacillus anthracis Edema Factor, C-terminal.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Schwartz, M.N., (2001), “Recognition and management of anthrax – an update”, New Engl. J. Med., 345: 1621-1626. 2. Moayeri, M., et al., (2004), “The roles of anthrax toxin in pathogenesis”, Curr. Opin. Microbiol., 7: 19-24. 3. Bradley, K.A., et al., (2001), “Identification of the cellular receptor for anthrax toxin”, Nature, 414: 225-229. 4. Scobie, H.M., et al., (2003), “Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor”, Proc. Natl. Acad. Sci. USA, 100: 5170-5174. 5. Singh, Y., et al., (1999), “Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytotic uptake into mammalian cells”, Infect. Immun., 67: 1853-1859. 6. Collier, R.J., et al., (2003), “Anthrax toxin”, Annu. Rev. Cell Dev. Biol., 19: 45-70.