ctxB
Escherichia Coli.
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
Sterile filtered colorless solution.
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
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.
Product Specs
Cholera Toxin B subunit (ctxB), produced by the bacterium Vibrio cholerae, is the protein complex responsible for the severe watery diarrhea associated with cholera infection. This toxin comprises six protein subunits: one A subunit and five B subunits, forming an AB5 structure. The B subunit binds to target cells, while the A subunit activates a G protein, which in turn activates adenylate cyclase. Five B subunits arrange themselves in a ring, with the A subunit's A1 portion (CTA1) acting as an enzyme that modifies G proteins and the A2 chain (CTA2) forming a helix nestled within the B subunit ring's central pore.
Recombinant Cholera Toxin B subunit, produced in E. coli, is a single, non-glycosylated polypeptide chain with 103 amino acids and a molecular weight of 11.6 kDa. This ctxB product is purified using proprietary chromatographic techniques.
A sterile, colorless solution.
ctxB is provided in a 0.2 µm filtered solution containing 5mM PB (pH 7.0), 75mM NaCl, and 50% glycerol.
For short-term storage (up to 2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity exceeds 98.0%, as determined by: (a) RP-HPLC analysis and (b) SDS-PAGE analysis.
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
Escherichia Coli.
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Product Science Overview
Cholera toxin (CT) is a protein complex secreted by the bacterium Vibrio cholerae, the causative agent of cholera. The toxin is composed of two subunits: A and B. The B subunit (CTB) is responsible for binding to the host cell surface, facilitating the entry of the A subunit, which then exerts the toxic effects. Recombinant Cholera Toxin B subunit (rCTB) is a genetically engineered version of the CTB, produced without the toxic A subunit, making it a valuable tool in research and therapeutic applications.
The CTB subunit is a pentameric protein, meaning it forms a complex of five identical subunits. Each subunit binds to the GM1 ganglioside, a glycolipid found on the surface of mammalian cells. This binding is crucial for the toxin’s entry into the cells. The recombinant version of CTB retains this binding ability, allowing it to be used in various applications without the associated toxicity of the A subunit .
Recombinant CTB is typically produced in bacterial or mammalian expression systems. One common method involves expressing the protein in Escherichia coli or HEK 293 cells. The recombinant protein is then purified using affinity chromatography techniques, ensuring high purity and the absence of the toxic A subunit .
- Vaccine Development: rCTB is used as an adjuvant in vaccines to enhance the immune response. Its ability to bind to GM1 ganglioside makes it an effective carrier for delivering antigens to the immune system.
- Research Tool: In neuroscience, rCTB is used for retrograde labeling of neurons. By binding to GM1 ganglioside, it can trace neuronal pathways, aiding in the study of neural connections and functions .
- Therapeutic Potential: rCTB has been explored for its potential in treating autoimmune diseases and inflammatory conditions. For example, recombinant fusion proteins of CTB with functional peptides have been used to deliver therapeutic peptides to intestinal epithelial cells, demonstrating anti-inflammatory effects .
