Cholera Toxin

Cholera toxin is a member of the AB5-subunit family of toxins. It consists of a single A subunit responsible for ADP-ribosylation and five B subunits arranged as a pentameric ring with cell surface receptor binding and internalization functions. The A subunit catalyzes the ADP-ribosylation of the α-subunit of the stimulatory G protein (Gαs), leading to increased adenylyl cyclase activity and cAMP levels. It also ADP-ribosylates transducing and tubulin.

Cholera toxin and its A subunit are commonly used to study signal transduction mechanisms due to their impact on adenylate cyclase. Additionally, cholera toxin acts as an adjuvant by stimulating B lymphocytes and T helper cell type 2 responses by inhibiting interleukin-12 production. The non-toxic B subunit (CTB) attaches to cells by binding to ganglioside GM1, making it a useful label for microglial cells in neurological research. It has also proved to be an excellent tracer for axonal transport studies using immunohistochemical methods.

Cholera Toxin from Vibrio cholerae has been used as a positive control in cAMP (cyclic AMP) assay for enterotoxins. It has been added as a supplement in cell culture media of primary tumors and epithelial cells.

Cholera Toxin from Vibrio cholerae has been used in toxin neutralization assays to assess the cytotoxicity of cells.

Toxin consisting of an A subunit (27 kDa) surrounded by five B subunits (approximately 12 kDa each), which attach the toxin to ganglioside GM₁ on the cell surface.

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Package size based on protein content.

Lyophilized powder containing Tris buffer salts, sodium chloride, sodium azide and sodium EDTA

When reconstituted at 1 mg/mL in water, solution will contain 0.05 M Tris buffer salts, pH 7.5, 0.2 M NaCl, 0.003 M NaN₃, and 0.001 M sodium EDTA. Store reconstituted solutions in the refrigerator.