Mouse Monoclonal Bacillus anthracis protective antigen antibody. Suitable for IP, ELISA, WB and reacts with Bacillus anthracis samples. Cited in 1 publication. Immunogen corresponding to Full Length Protein corresponding to Bacillus anthracis pagA.
Preservative: 0.01% Sodium azide
Constituents: PBS
| IP | ELISA | WB | |
|---|---|---|---|
| Bacillus anthracis | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Bacillus anthracis | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Bacillus anthracis | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Bacillus anthracis | Dilution info Use at an assay dependent concentration. | Notes - |
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Protective antigen constitutes one of the three proteins composing the anthrax toxin; it mediates attachment to host cells and translocation of edema factor (EF) and lethal factor (LF) into the host cytoplasm (PubMed:11700562, PubMed:14507921, PubMed:15243628, PubMed:15326297). PA associated with LF forms the lethal toxin (LeTx) and causes death when injected; PA associated with EF forms the edema toxin (EdTx) and produces edema (PubMed:1651334). PA induces immunity to infection with anthrax (PubMed:11544370). Protective antigen. Mediates the attachment to host cells by binding host cell receptors ANTXR1 and ANTXR2 (PubMed:11700562, PubMed:14507921, PubMed:15243628, PubMed:15326297). Following host cell surface attachment, PA is cleaved by FURIN to generate the PA-63 (Protective antigen PA-63) form, which constitutes the mature form of the protein that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol (PubMed:11700562, PubMed:15243628, PubMed:15326297). Protective antigen PA-63. Mature form that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol (PubMed:15243628, PubMed:15326297). Following attachment to host cell receptors and cleavage by FURIN, homooligomerizes to form ring-shaped oligomers that are in a pre-pore conformation, and associates with EF and LF (PubMed:10085027, PubMed:12117959, PubMed:15313199). Toxin-leaded complexes are then endocytosed in a clathrin-dependent process, followed by a conformational change of oligomerized PA-63 from the pre-pore to pore state, which is triggered by the low pH in the endosome (PubMed:10085027, PubMed:12551953, PubMed:15326297, PubMed:20221438). Once active, the pore mediates unfolding of EF and LF, which pass through the pore and translocate into the host cytosol (PubMed:16051798, PubMed:21037566, PubMed:32047164, PubMed:32521227, PubMed:32810181).
Bacillus anthracis protective antigen
pag, pXO1-110, BXA0164, GBAA_pXO1_0164, pagA, Protective antigen, PA, Anthrax toxins translocating protein, PA-83, PA83
Mouse Monoclonal Bacillus anthracis protective antigen antibody. Suitable for IP, ELISA, WB and reacts with Bacillus anthracis samples. Cited in 1 publication. Immunogen corresponding to Full Length Protein corresponding to Bacillus anthracis pagA.
Preservative: 0.01% Sodium azide
Constituents: PBS
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Bacillus anthracis protective antigen often referred to as PA plays an important role in the mechanism of anthrax toxin's entry into host cells. PA weighs approximately 83 kDa and is an essential component of B. anthracis the bacterium causing anthrax. It expresses on the surface of the bacteria and exists in the extracellular environment. Within the anthrax toxin complex PA functions mechanically by binding to host cell receptors and facilitating the entry of other anthrax toxin components lethal factor (LF) and edema factor (EF) into the host cells.
Bacillus anthracis protective antigen behaves as a part of a complex specifically the anthrax toxin composed of LF EF and PA itself. PA binds to host cell’s receptors such as ANTXR1 and ANTXR2. Once PA attaches to these receptors it undergoes proteolytic cleavage to heptamer formation allowing the assembly of the toxin complex. This heptamer serves as a platform for LF and EF which subsequently translocate into the host cell's cytosol disrupting cellular processes and immune responses.
Bacillus anthracis protective antigen operates primarily in endocytic and intracellular trafficking pathways. The binding and cleavage of PA on the host cell surface enable endocytosis of the toxin complex through clathrin-mediated pathways. This interaction with cellular components is critical for facilitating the entry of LF and EF which relate to pathways involving cellular signaling and immune response suppression. These processes highlight PA’s role in efficiently hijacking host cellular machinery for pathogenic activity.
Bacillus anthracis protective antigen is chiefly associated with anthrax a severe and sometimes lethal disease. The action of PA in the anthrax toxin contributes to systemic issues such as shock and multi-organ dysfunction. Within this context PA’s interaction with LF and EF directly correlates with the virulence and lethality of the anthrax pathogen. Understanding PA and its interactions provides invaluable insight for developing therapeutic interventions and effective anthrax antibodies aimed at neutralizing the effects of the toxin.
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