Botulinum toxins . Clostridium botulinum neurotoxins (BoNT) are among the most toxic substances to man. the Seven immunologically distinct serotypes of neurotoxin, designate types A through G. (BoNT/A, BoNT/B, BoNT/C, BoNT/D, BoNT/E, BoNT/F, BoNT/G) have been identify. These botulinum neurotoxins are naturally produce complex with one or more nontoxic, neurotoxin-associate proteins (NAPs). NAPs are important to toxicity by ingestion in that they protect the neurotoxin from proteases. and acidity heat and they may also play a role in translocation across the mucosal layer.
certainly Synthesize as single 150 kDa polypeptide chains. the actual neurotoxin portion of the complex is subsequently activate by cleavage to produce two chains, a heavy chain and a light chain, which are link by a single disulfide bond. For each toxin, the 50 kDa light chain is a zinc-dependent protease. which cleaves a single target protein essential for synaptic, vesicle membrane. fusion during neurotransmission.
Neurotoxin types A, C, and E specifically bind to and selectively cleave the synaptosome-associated protein, SNAP-25 while types B, D, F and G. cleave synaptobrevin-2 also known as VAMP-2. Cleavage of the target protein inhibits neurotransmitter release among neurons.
Each toxin is easily divide into three domains that reflect the three functions important for toxicity. Binding translocation, and cleavage of a specific substrate. The heavy chain is responsible for recognizing both a specific ganglioside and a specific protein receptor on the presynaptic membrane. The translocation domain portion of the heavy chain mediates the passage of light chain across the endosomal membrane and finally the target protein is cleave by the enzymatic domain.
Use of Botulinum Neurotoxin in Research
Botulinum neurotoxins are valuable research tools in studies aim at elucidating the mechanisms involve in vesicle trafficking and the extreme toxicity, as well as in gaining an understanding of the underlying events of synaptic transmission. In addition to studies. actually With the 150 kD holotoxin, recombinant nontoxic heavy chains can be use to evaluate the binding properties of the toxins. And the recombinant nontoxic, light chains can be use to screen for inhibition of the enzymatic activity of the protease domain.
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