| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | Vibriocholerae Toxin B Protein; Toxin B |
| Biological Activity | |
| Expression System | |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Protein Length | |
| Purity | |
| Shipping | |
| Storage | |
| Target |
Background
Toxin B is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: Vibriocholerae Toxin B Protein; Toxin B.
Cholera toxin (CT) is an AB5 enterotoxin produced by Vibrio cholerae and is responsible for the disease manifestations. Several publications indicate that the toxin binds to glycoprotein and that the B-chain binds to GM1 ganglioside pentasaccharide on the cell surface.
Endotoxin: <1 EU per μg of the protein by the LAL method.
Biological significance and function
Toxin B is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as Molecular & Cellular Biology.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Molecular weight: 11.6 kDa
- Protein length: The recombinant Vibriocholerae Toxin B consists of 103 amino acids and predicts a molecular mass of 11.6 kDa.
- Expression region: Amino acid sequence derived from Vibriocholerae Toxin B (Thr22-Asn124)(P01556) was expressed.
- Purity: > 98 % as determined by SDS-PAGE
- Biological activity: Testing in progress
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.
Expression and purification strategy
Expression system: E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: No tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: Liquid in from sterile 50 mM Tris-HCl, 200 mM NaCl, 10% glycerol, pH8.0. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.
