Anthrax Lethal Factor Antibody: 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.
Immunogen
Anthrax lethal factor antibody was raised against a synthetic peptide corresponding to 16 amino acids near the carboxy terminus of the Anthrax lethal factor protein.The immunogen is located within the last 50 amino acids of Anthrax Lethal Factor.
Application
Anthrax lethal factor antibody can be used for the detection of Anthrax LF protein in ELISA. It will detect 10 ng of free peptide at 1 μg/mL.
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