Technical Data
Bacillus anthracis LF (Lethal Factor) (Anthrax)
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. LF is the primary toxin of anthrax and functions as a highly specific protease that cleaves members of the mitogen-activated protein kinase kinase (MAPKK) family near their amino terminus, interfering with MAPK signaling and inducing apoptosis.

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.
PabIgGAffinity Purified
100ug-20°CBlue IceRabbit
As reported
Synthetic peptide corresponding to 16aa near the middle of the Anthrax lethal factor protein (P15917).
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, 0.02% sodium azide.
Recognizes Bacillus anthracis Lethal Factor, middle region.
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. Duesbury, N., et al.,(1998), “Poteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor”, Science, 280: 734-736.