Cholera Toxin B subunit has been used as a tracer to study the ascending projections of the nuclei of the descending trigeminal tract (nTTD) in the zebra finch.
Cholera Toxin B subunit has been used:
- for macrophage stimulation and i.p. injection in a study to determine the endotoxin sensitivity of Caspase-4.
- in transganglionic and retrograde tract-tracing method combined with dual-immunofluorescence histochemistry of adult rat Vmes neuron cells.
The advantage of this product over the native CTXB is that it has no traces of Vibrio cholera, and no contamination of the highly toxic Cholera toxin A subunit. This product is expressed in human HEK 293 cells as a C-terminally his-tagged protein with a calculated molecular mass of 13 kDa (amino acids Thr22-Asn124).
Cholera Toxin B subunit stimulates both systemic and mucosal antibody production in animals and humans. CTB functions as an oral subunit vaccine for cholera, which is associated with acute watery diarrhoea.
Cholera Toxin B subunit Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 103 amino acids and having a molecular mass of 11.6kDa.
ctxB is purified by proprietary chromatographic techniques.
Cholera Toxin B subunit (ctxB) Cholera is a protein complex secreted by the bacterium Vibrio cholerae. ctxB is responsible for the massive, watery diarrhea characteristic of cholera infection. The cholera toxin is an oligomeric complex made up of 6 protein subunits: a single copy of the A subunit and5 copies of the B subunit, denoted as AB5. Subunit B binds while subunit A activates the G protein which activates adenylate cyclase. The five B subunits form a five-membered ring. The A subunit has 2 important segments. The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) forms an extended alpha helix which sits snugly in the central pore of the B subunit ring.
