- {{heading}}
- Ab02808-23.0 Anti-Cholera enterotoxin B subunit [TE33]
- Vibrio cholerae
- Rabbit IgG
- Purified
- Ships in 5-6 weeks
- Ab02808-1.1 Anti-Cholera enterotoxin B subunit [TE33]
- Vibrio cholerae
- Mouse IgG1
- Purified
- Ships in 5-6 weeks
Recombinant monoclonal antibody to Cholera enterotoxin B subunit. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma TE33.
UniProt Accession Number of Target Protein: P01556
Alternative Name(s) of Target: ctxB; toxB; VC_1456; Cholera enterotoxin subunit B; Cholera enterotoxin B chain; Cholera enterotoxin gamma chain; Choleragenoid
Immunogen: The original antibody was generated by immunizing mice with CTP3 which is a conserved loop comprising amino acid residues 50-64 on the surface of the B subunit. CTP3 is involved in saccharide binding to the receptor on epithelial cells.
Specificity: This antibody binds the CTP3 loop of the B subunit of the cholera toxin. This antibody is not capable of binding cholera toxin in its native form or its wild type form. TE33 specifically recognizes a loop comprising the sequence 'VPGSQHID' and a beta-turn formed by the sequence 'VPGS'. The CTP3 peptide is involved in saccharide binding to the receptor on the epithelial cells.
Application Notes: The original IgG1 antibody which was raised against the CTP3 peptide also cross reacts with cholera toxin in a solid phase ELISA. The binding of the original IgG1 antibody to cholera toxin and H-LT, a heat-labile toxin produced by enterotoxigenic strains of E. coli was done using solid-phase RIA and western blot (PMID: 2450576). In solution, the original antibody has a thousandfold lower affinity for the cholera toxin as compared to that for CTP3 (PMID: 1379072). The binding of the original antibody to both CTP3 peptide and cholera toxin was assayed by ELISA, solid-phase radioimmunoassay and immunoblot assay. The antibody was incapable of binding cholera toxin in its native form when tested in a solution-phase assay system (PMID: 1993848).
Antibody first published in:
Anglister et al. NMR study of the complexes between a synthetic peptide derived from the B subunit of cholera toxin and three monoclonal antibodies against it. Biochemistry. 1988 Jan 26;27(2):717-24. PMID:2450576
Note on publication:
The contact interaction between a synthetic peptide CTP3 (residues 50-64 of the B subunit of cholera toxin) suggested as a possible epitope for synthetic vaccine against cholera and three different anti-peptide monoclonal antibodies were studied by nuclear magnetic resonance (NMR).