|Other Accession||AAF86457, 9280533|
|Calculated MW||85811 Da|
|Application Notes||Anthrax PA antibody can be used for the detection of Anthrax PA protein in ELISA. It will detect 10 ng of free peptide at 1 µg/mL.|
|Other Names||Anthrax PA Antibody : pag, pXO1-110, BXA0164, GBAA_pXO1_0164, Protective antigen, Anthrax toxins translocating protein, PA, Protective antigen|
|Reconstitution & Storage||Anthrax PA 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 PA 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. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax.|
|Cellular Location||Secreted, extracellular space. Note=Secreted through the Sec-dependent secretion pathway. Therefore, PA is translocated across the membrane in an unfolded state and then it is folded into its native configuration on the trans side of the membrane, prior to its release to the environment. PA requires the extracellular chaperone PrsA for efficient folding|
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Provided below are standard protocols that you may find useful for product applications.
Anthrax PA 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. These toxins are usually sufficient to cause rapid cell death, and often the death of the organism.
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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