|Other Accession||P15917, 50402185|
|Calculated MW||93770 Da|
|Application Notes||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.|
|Other Names||Anthrax Lethal Factor Antibody: Lethal factor, Anthrax lethal toxin endopeptidase component, LF, Lethal factor|
|Reconstitution & Storage||Anthrax Lethal Factor antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||Anthrax Lethal Factor Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates. Also cleaves mouse Nlrp1b allele 1, leading to NLRP1 inflammasome activation, IL1B release and eventually host inflammatory response (PubMed:19651869).|
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Provided below are standard protocols that you may find useful for product applications.
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.
Schwartz MN. Recognition and management of anthrax - an update. New Engl. J. Med. 2001; 345:1621-6.
Moayeri M and Leppla SH. The roles of anthrax toxin in pathogenesis. Curr. Opin. Microbiol. 2004; 7:19-24.
Bradley KA, Mogridge J, Mourez M, et al. Identification of the cellular receptor for anthrax toxin. Nature 2001; 414:225-9.
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.
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