Date published: 2025-11-5

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Diphtheria Toxin Antibody (3B6): sc-51868

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  • Diphtheria Toxin Antibody (3B6) is a mouse monoclonal IgG1 Diphtheria Toxin antibody provided at 100 µg/ml
  • raised against Diphtheria toxoid
  • recommended for detection of different determinants of Diphtheria toxin and anatoxin of Corynebacterium diphtheriae origin by ELISA
  • At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for Diphtheria Toxin Antibody (3B6). This work is in progress.

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    Diphtheria Toxin Antibody (3B6) is a mouse monoclonal IgG1 antibody that detects Diphtheria Toxin protein of Corynebacterium diphtheriae origin by enzyme-linked immunosorbent assay (ELISA). Anti-Diphtheria Toxin antibody (3B6) is available as the non-conjugated format. Corynebacterium diphtheriae is a Gram-positive, nonmotile aerobic bacterium commonly found in soil and animal feces, which infects the epithelial cells of the upper respiratory tract. The bacteria produce and secrete a potent toxin that is absorbed and disseminated through lymph channels and blood to susceptible tissues, leading to severe health complications. Diphtheria Toxin (3B6) monoclonal antibody recognizes a protein that plays a critical role in pathogenesis by catalyzing the ADP-ribosylation and inactivation of elongation factor 2 (eEF-2), effectively halting protein synthesis in host cells. The structure of Diphtheria Toxin is particularly important, as Diphtheria Toxin consists of a Y-shaped molecule with three distinct domains: a catalytic domain (fragment A) that exhibits an α + β fold, a transmembrane domain composed of nine α-helices that may facilitate pH-triggered membrane insertion and translocation, and a receptor-binding domain that forms a flattened β-barrel with a jelly-roll-like topology. Together, the transmembrane and receptor-binding domains constitute fragment B, which is essential for the toxin′s entry into host cells. This intricate structure not only underscores the toxin′s mechanism of action but also highlights the potential for therapeutic interventions targeting these domains to mitigate the effects of diphtheria.

    For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.

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    Diphtheria Toxin Antibody (3B6) References:

    1. The crystal structure of diphtheria toxin.  |  Choe, S., et al. 1992. Nature. 357: 216-22. PMID: 1589020
    2. Diphtheria toxin: mode of action and structure.  |  Collier, RJ. 1975. Bacteriol Rev. 39: 54-85. PMID: 164179
    3. Studies on Diphtheria Toxin : II. The Rôle of the Amino Acids in the Metabolism of Bacterium diphtheriae.  |  Davis, L. and Ferry, NS. 1919. J Bacteriol. 4: 217-41. PMID: 16558837
    4. Further Studies upon the Effect of Various Carbohydrates on Production of Diphtheria Toxin with Special Reference to its Flocculating Titer and Final pH.  |  Hazen, EL. and Heller, G. 1932. J Bacteriol. 23: 195-209. PMID: 16559546
    5. The Purification and Concentration of Diphtheria Toxin: II. Observations on the Nature of the Toxin.  |  Eaton, MD. 1936. J Bacteriol. 31: 367-83. PMID: 16559895
    6. The Purification and Concentration of Diphtheria Toxin: III. Separation of Toxin from Bacterial Protein.  |  Eaton, MD. 1937. J Bacteriol. 34: 139-51. PMID: 16560042
    7. Studies on Diphtheria Toxin and Its Reaction with Antitoxin.  |  Pappenheimer, AM. 1942. J Bacteriol. 43: 273-89. PMID: 16560498
    8. The effect on solutions of diphtheria toxin and diphtheria antitoxin of contact with certain surfaces.  |  Moloney, PJ. and Taylor, EM. 1932. Biochem J. 26: 1754-61. PMID: 16744999
    9. Diphtheria toxin.  |  Pappenheimer, AM. 1977. Annu Rev Biochem. 46: 69-94. PMID: 20040
    10. Diphtheria toxin forms transmembrane channels in planar lipid bilayers.  |  Donovan, JJ., et al. 1981. Proc Natl Acad Sci U S A. 78: 172-6. PMID: 6264431

    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    Diphtheria Toxin Antibody (3B6)

    sc-51868
    100 µg/ml
    $316.00