Cholera Toxin B Subunit-low salt
Catalog Number
ATG-131
Description
Cholera toxin B subunit in low salt buffer, recombinant
Synonyms
CTX, Ctx, CT, CT-B, CT subunit B, CTB
Product Background
Cholera toxin is an oligomeric protein complex secreted by the bacterium Vibrio cholerae and is the pathogenic agent responsible for the symptoms of cholera. The holotoxin consists of a single A subunit surrounded by five B subunits, similar in structure to heat-labile enterotoxin from Escherichia coli. The B subunit is responsible for the binding of the heterohexamer to GM1 ganglioside receptors on mammalian cell surfaces and facilitates entrance of the A subunit into the cell. The A subunit bears the ADP-ribosyl-transferase activity, which deregulates the G protein causing activation of adenylate cyclase. The B subunit alone is considered nontoxic. In vitro, cholera toxin B subunit (CTB) is an efficient mucosal adjuvant and carrier molecule for the generation of mucosal antibody responses and/or induction of systemic T-cell tolerance to linked antigens. Due to the ubiquitous occurrence of the GM1 ganglioside receptor on eukaryotic cell membranes, CTB can be used in a wide variety of model systems. CTB is also used for tract tracing in neurological research, taking advantage of its high affinity to GM1 gangliosides and retrograde transport.
Not available outside of the United States
Not available outside of the United States
Category
Vaccine Components
Source
Pseudomonas fluorescens
Species
Vibrio cholerae
Formulation
Lyophilized in phosphate buffer, pH 7.5
Product Molecular Mass: 11.5 kDa, as monomer, 57.4 kDa as pentamer
Product Molecular Mass: 11.5 kDa, as monomer, 57.4 kDa as pentamer
Reconstitution
Reconstitute aseptically with sterile deionized water to a CTB concentration of 1-5 mg/mL. Store reconstituted CTB at -20 °C (not in a frost-free freezer).
Storage
Avoid repeated freeze-thaw.
Purity
> 95%, by SDS-CGE under reducing conditions
Activity
Measured in a hemagglutination assay using sheep red blood cells coated with GM1 ganglioside, and exhibits comparable binding activity as reported in reference.


