Diphtheria toxin (DT) is a potent exotoxin that is a member of the family of ADP-ribosylating bacterial toxins. It was first identified in 1888 as the causative agent of an infectious disease in humans known as diphtheria. DT is secreted by strains of the gram-positive bacterium Corynebacterium diphtheria carrying a lysogenic bacteriophage, which contains the toxin gene (Freeman, VJ). The toxin is secreted as a precursor molecule and cleaved to produce a single polypeptide chain of 535aa (Mwt 58.342) containing two major functional domains, known as domains A and B. The N-terminal A domain (aa1-193) carries the catalytic domain for ADP-ribosylation of elongation factor 2 (EF2). The C-terminal B domain (aa194-535) is further divided into receptor (R) binding and transmembrane (T) domains (Choe, S). The B domain promotes binding of DT to cells, the internalization of DT by receptor-mediated endocytosis and the entry of the A polypeptide chain into the cytosolic compartment (Greenfield, L). In humans, DT binds to heparin-binding epidermal growth factor receptor (HB-EGFR) on the surface of cells, and the toxin–receptor complex undergoes receptor-mediated endocytosis. The arginine-rich segment connecting the A and B domains is then cleaved to yield active DT-A and DT-B fragments. The A fragment is translocated across the endocytic membrane into the cytoplasm, a process that is facilitated by DT-B. In the cytoplasm, the catalytic domain A inactivates elongation factor-2, which is an essential component of the protein translation machinery, halting protein synthesis and causing cell death (Collier, RJ).||Applications: |Other applications not tested.||Recommended Dilution:|Optimal dilutions to be determined by the researcher.||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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