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HYB 123-05-02 detects Cornynebacterium diptheria toxoid and toxin in a neutralizing manner. Neutralization was determined in a VERO cell toxin neutralization assay.
HYB 123-05-02 has been successfully used in ELISA procedures. HYB 123-05-02 reacts strongly with Corynebacterium diphtheriae toxoid. HYB 123-05-02 detects Corynebacterium diphtheriae toxoid in sandwich ELISA in combination with a polyclonal antibody against the toxoid as capture antibody. Strong reaction is also seen in ELISA with Corynebacterium diphtheriae toxoid coated directly onto the microtiter well.
The HYB 123-05-02 immunogen is purified formaldehyde treated diphtheria toxin from a culture of Corynebacterium diptheriae subsp. intermedius Park-Williams no. 8.
NOTE: Concentration is lot-dependent and can vary from 0.85-1.15 mg/mL
Diphtheria toxin (DT) is secreted by certain strains of Corynebacterium diphtheriae and catalyzes the ADP-ribosylation of eukaryotic aminoacyl-transferase II (EF-2) using NAD as a substrate. This reaction forms the basis for its toxicity toward eukaryotic organisms. Diphtheria toxin is synthesized and excreted as a proenzyme, composed of a single polypeptide chain having a molecular weight of approximately 63 kDa. Two covalent alterations in structure are necessary for expression of its enzymatic activity. First, mild proteolysis results in the formation of "nicked toxin," which is enzymatically inactive and consists of two major fragments, A and B, linked by a disulfide bond. Reduction of the nicked toxin with thiols releases the N-terminal A fragment (~24 kDa) which is enzymatically active. The C-terminal B fragment (~39 kDa) has no apparent enzymatic activity, but is required for toxicity. Evidence suggests that the B fragment is responsible for recognizing and binding the toxin to cell surface receptors.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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