Application

Anti-Adenylate Cyclase Toxin, B. pertussis, clone 3D1 , Cat. No. MABF2086, is a mouse monoclonal antibody that detects Adenylate cyclase (AC) toxin from Bordetella pertussis and has been tested for use in ELISA, Flow Cytometry, Inhibition Assay, Neutralizing, and Western Blotting.

Inhibition Analysis: A representative lot inhibited AC toxin-induced cAMP accumulation in Jurkat cells and inhibited intoxication of sheep erythrocytes. (Bumba, L., et. al. (2016). Mol Cell. 62(1):47-62; Gray, M.C., et. al. (2001). J Bacteriol. 183(20):5904-10; Holubova, J., et. al. (2012). Infect Immun. 80(3):1181-92; Hewlett, E.L., et. al. (2006). Mol Microbiol. 59(2):447-59).

Flow Cytometry Analysis: A representative lot detected Adenylate Cyclase Toxin, B. pertussis in Flow Cytometry applications (Gray, M.C., et. al. (2001). J Bacteriol. 183(20):5904-10).

Western Blotting Analysis: A representative lot detected Adenylate Cyclase Toxin, B. pertussis in Western Blotting applications (Lee, S.J., et. al. (1999). Infect Immun. 67(5):2090-5).

ELISA Analysis: A representative lot detected Adenylate Cyclase Toxin, B. pertussis in ELISA applications (Weingart, C.L., et. al. (2000). Infect Immun. 68(12):7152-5; Wang, X., et. al. (2015). J Biol Chem. 290(38):23025).

Neutralizing Analysis: A representative lot neutralized Adenylate Cyclase Toxin action. (Holubova, J., et. al. (2012). Infect Immun. 80(3):1181-92.

General description

Adenylate Cyclase Toxin (UniProt: C8C508; also known as ACT or CyaA) is one of several virulence factors produced by the bacterium Bordetella pertussis. Bordetella pertussis, a gram-negative bacterium, is shown to be the causative agent for whooping cough. It produces several virulence factors, including Cya A. The CyaA toxin is a bifunctional protein of 1,706 residues consisting of an NH2-terminal catalytic domain of 400 amino acids and a COOH-terminal part with 1,306 residues. The CyaA polypeptide is synthesized as an inactive protoxin, which is then converted to an active toxin by posttranslational palmitoylation of two internal lysine residues (Lys 856 and 963). Upon interaction of its C-terminal hemolysin moiety with the cell surface receptor alphaM-beta2 integrin ((Cd11b/Cd18), the N-terminal cyclase domain translocates into the host cell cytosol where it generates supraphysiological levels of cAMP concentration, which inhibits host cell anti-bacterial activities and apoptotic death of macrophages. CyaA toxin is also shown to elicit potassium ion efflux from erythrocytes in a process that is thought to be a precursor event to osmotic lysis of erythrocytes.Clone 3D1 is shown to cause both an enhancement of hemolysis and inhibition of intoxication in erythrocytes. It also inhibits toxin-induced cAMP accumulation in Jurkat cells. (Ref.: Guermonprez, P., et al. (2001). J. Exp. Med. 193(9); 1035 1044; Gray, MC., et al. (2001). J. Bacteriol. 183(20); 5904-5910; Holubova, J., et al. (2012). Infect. Immun. 80(3); 1181 1192).

Immunogen

Adenylate cyclase (AC) toxin from Bordetella pertussis.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Format: Purified

Quality

Evaluated by Western Blotting in Adenylate cyclase toxin from Bordetella pertussis.

Western Blotting Analysis: 0.2 µg/mL of this antibody detected Adenylate Cyclase Toxin from Bordetella pertussis.

Specificity

Clone 3D1 is a mouse monoclonal antibody that detects Adenylate cyclase (AC) toxin from Bordetella pertussis.

Target description

~220 kDa observed. Uncharacterized bands may be observed in some lysate(s).