Technical Data
Bacillus anthracis PA (Protective Antigen) (Anthrax)
Anthrax toxins are composed of three distinct proteins, a protective antigen (PA), a lethal factor (LF) and an edema factor (EF). None of these proteins are toxic by themselves and several studies indicate that the anthrax toxin has the familiar A-B enzymatic binding structure, with PA acting as the binding domain and EF and/or LF acting as the active fragments.

Suitable for use in ELISA. Other applications not tested.

Recommended Dilutions:
ELISA: 1ug/ml detects 10ng of free peptide
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ug-20CBlue IceRabbit
Synthetic peptide corresponding to 16aa near the middle of the Anthrax protective antigen protein (AAF86457).
Purified by Immunoaffinity chromatography
Supplied as a liquid in PBS, 0.02% sodium azide.
Recognizes Bacillus anthracis Protective Antigen, 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.