Anthrax antibody | C3
|Mouse anti Anthrax Protective Antigen antibody, clone C3 recognizes the Protective Antigen of the anthrax toxin. Bacillus anthracis produces a toxin composed of three proteins, the Protective Antigen (PA), the Edema Factor (EF) and the Lethal Factor (LF). The three proteins depend on each other for their toxic effect. Both EF and LF functions intracellularly but are too large to enter the cell through existing channels. The PA is responsible for transporting the EF and LF into cells. The 83kDa PA (PA83) binds to the cell surface where a 20 kDa N-terminal fragment (PA20) is cleaved off, exposing binding sites for LF and EF. The remaining 63 kDa portion (PA63) oligomerizes to form a heptamer pre-pore, which then associates with up to three molecules of EF and/or LF. The receptor complex is internalized within endocytotic vessels that are subsequently acidified, transforming the PA heptamer into a pore that releases the active enzymes EF (an adenylate cyclase) and LF (a protease targeting MAPKKs) into the cytosol.
Mouse anti Anthrax Protective Antigen antibody, clone C3 does not cross-react with the Lethal Factor of Bacillus anthracis, Yersinia pestis, Francisella tularensis or Toxoplasma gondii. The antibody recognizes both the 83kDa and 63kDa truncated form of PA.
- Target Species
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- <0.1% Sodium Azide (NaN3)
- Highly purified protective antigen of Bacillus anthracis.
- Approx. Protein Concentrations
- IgG concentration 1.0mg/ml
- Fusion Partners
- Spleen cells from immunised Balb/c mice were fused with cells of the Sp2/0 myeloma cell line.
- For research purposes only
- 12 months from date of despatch
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
|Application Name||Verified||Min Dilution||Max Dilution|
References for Anthrax antibody
Barth H, et al (2004) Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins.
Microbiol Mol Biol Rev. 68:373-402
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