Recombinant C. tetani TeNT Light Chain antigen, was expressed in E. coli. Pro2-Gly430. with an N-terminal Met and 6-His tag (Accession # P04958)
> 85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie. Blue stain at 5 μg per lane.
2-8°C short term, -20°C long term
Clostridium tetani is a rod-shaped, anaerobic bacterium of the genus Clostridium. Like other Clostridium species, it is Gram-positive, and its appearance on a gram stain resembles tennis rackets or drumsticks. C. tetani is found as spores in soil or in the gastrointestinal tract of animals. C. tetani produces a potent biological toxin, tetanospasmin, and is the causative agent of tetanus, a disease characterized by painful muscular spasms that can lead to respiratory failure and, in up to 40% of cases, death
Tetanus toxin (TeNT) is a potent neurotoxin produced by Clostridium tetani. TeNT is similar in structure and function to the botulinum toxins produced by other Clostridium species. TeNT is among the most toxic protein toxins known for humans. TeNT is synthesized as an inactive single chain precursor that undergoes proteolytic cleavage to create light and heavy chains that are linked by a disulfide bond. The 50 kDa light chain contains a metalloprotease domain whereas the 100 kDa heavy chain contains a receptor binding domain and a domain required for translocation across the cell membrane. Once inside a neuronal cell the zinc metalloprotease domain is able to cleave synaptobrevin to cause motor neuron disinhibition, resulting in the spastic paralysis characteristic of tetanus).
Clostridium tetani; C. tetani; Clostridium; C. tetani TeNT protein; Clostridium tetani Tetanus toxin protein; TeNT; Tetanus toxin