|Detection of C. tetani TeNT Light Chain by Western Blot. Western blot shows recombinant C. tetani TeNT Light Chain. PVDF Membrane was probed with 2 µg/mL of C. tetani TeNT Light Chain Monoclonal Antibody (Catalog # MAB6535) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for TeNT Light Chain at approximately 53 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Tetanus toxin, a member of the peptidase M27 family of proteins, is produced by the anaerobic spore-forming bacteria Clostridium tetani as a single-chain polypeptide that is 1315 amino acids (aa) in length. The protein is subsequently cleaved by an endogenous protease to yield the 52 kDa tetanus toxin light chain (TeNT-LC), which is 457 aa in length, and the 98 kDa tetanus toxin heavy chain that is 858 aa long. The light and heavy chains are linked by a disulfide bridge and are non-toxic after separation. Tetanus toxin acts by inhibiting neurotransmitter release. It binds to peripheral neural synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the ’76-Gln-|-Phe-77’ bond of synaptobrevin-2.
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