Anti-C. diphtheriae Toxin Monoclonal antibody, Clone 4C7

Name: Anti-C. diphtheriae Toxin Monoclonal antibody, Clone 4C7
SKU: CABT-WN1035
Rating: 5 (1 reviews)

Mouse Anti-C. diphtheriae Toxin Monoclonal antibody for EIA

Write a review

COA

SDS

Datasheet

Summary

Specifications

Antibody Isotype

IgG1

Clone

4C7

Species Reactivity

C. diphtheriae

Immunogen

Diphtheria toxoid.

Conjugate

Unconjugated

Product Background

Antigen Description

Diphtheria toxin is a 58 kDa protein secreted by lysogenic strains of Corynebacterium diphtheriae. The toxin causes the disease diphtheria in humans by gaining entry into the cell cytoplasm and inhibiting protein synthesis. The mechanism of inhibition involves transfer of the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive. The catalysed reaction is as follows: NAD + + peptide diphthamide = nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide The crystal structure of the diphtheria toxin homodimer has been determined to 2.5A resolution. The structure reveals a Y-shaped molecule of 3 domains, a catalytic domain (fragment A), whose fold is of the alpha + beta type; a transmembrane (TM) domain, which consists of 9 alpha-helices, 2 pairs of which may participate in pH-triggered membrane insertion and translocation; and a receptor-binding domain, which forms a flattened beta-barrel with a jelly-roll-like topology. The TM- and receptor binding-domains together constitute fragment B.

Citations

Have you cited CABT-WN1035 in a publication? Let us know and earn a reward for your research.

Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Backbone and side chain H-1, C-13 and N-15 resonance assignments of the catalytic domain of diphtheria toxin

BIOMOLECULAR NMR ASSIGNMENTS

Authors: Sauve, Simon; Gingras, Genevieve; Aubin, Yves

Abstract

Diphtheria is a serious upper respiratory tract disease caused by the diphtheria toxin (DT) secreted from the bacteria Corynebacterium diphtheriae. Vaccination is the best way to protect against this infectious disease. Diphtheria vaccines are prepared by isolating, purifying and chemically deactivating DT. Although toxoids have been used for decades in immunization, there is still little understanding at the molecular level of the process of toxoid preparation, and how chemical treatment enhances their immunogenicity. We have undertaken an NMR study of the catalytic domain as a first step in understanding the molecular details involved in vaccine antigen preparation. Here we report a near complete assignment for the backbone and side chain resonances of the diphtheria toxin catalytic domain.

Characterization of production processes for tetanus and diphtheria anatoxins

BIOLOGICALS

Authors: Guilhen, Fabiana Belasco; Trezena, Aryene Goes; Affonso Prado, Sally Muller; Higashi, Hisako Gondo; Sonobe, Martha Harumi

Abstract

Tetanus and diphtheria are diseases that still cause significant morbidity and mortality. Clostridium tetani produces the tetanus toxin, a 150-kDa protein. The diphtheria toxin is synthesized by Corynebacterium diphtheriae as a protein of 58 kDa. The objective of this study was to carry out a chemical characterization of the tetanus and diphtheria toxin forms in the several production process stages, and thus to establish an affordable alternative in vitro quality control to aggregate to the classical tests. The 150 kDa band of the tetanus toxin and approximately 58 kDa band of the diphtheria toxin were observed by electrophoresis similar as that described in the literature. The same band of 58 KDa was detected in Western blotting reactions. The results obtained for diphtheria toxin showed very similar protein profiles between distinct lots. For the tetanus toxin, the profiles of the initial stage showed some variability, but the ones of the following stages were similar. The similarity of the electrophoresis results indicated reproduction and consistency of the production processes in Butantan Institute and correlated with the yield and antigenic purity classical data. The establishment of alternative in vitro quality control tests can significantly contribute to achieve the consistency approach supported by WHO. (C) 2013 The International Alliance for Biological Standardization. Published by Elsevier Ltd. All rights reserved.