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Cholera toxin consists of a single A subunit surrounded by five B subunits. The B subunits are responsible for the attachment of the native toxin to ganglioside GM1 on mammalian cell surfaces, and facilitate translocation of the A subunit. The A subunit catalyzes the ADP-ribosylation of an arginine residue on the a subunit of G proteins, reducing intrinsic GTPase activity and activating the a subunit. ADP-ribosylation of other proteins such as human red cell Ca-ATPase has also been reported. Cholera toxin must interact with ADP-ribosylation factor (ARF) for maximal activity.
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| Regulatory Status |
RUO – Research Use Only |
|---|
Related Products
| Alternative Name | AC toxin |
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| Purity | ≥80% (SDS-PAGE) |
| Source | Produced in E. coli. |
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| Source | From Bordetella pertussis, strain NCTC 10739. |
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| Purity | ≥98% |
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| Alternative Name | Clostridium difficile toxin A |
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Last modified: May 29, 2024