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Anti-Adenylate Cyclase Toxin Antibody, B. pertussis Antibody, clone 3D1 clone 3D1, from mouse

ITEM#: 3042-MABF2086100UG

MFR#: MABF2086-100UG

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

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).