Botulinum Toxins, List Biological Laboratories

Supplier: List Biological Laboratories
Ratings: (No Reviews)

Total Ratings: 0
Avg. Ratings: 0.0 out of 5

622A 133L 611A 141A 140A 625A 612A 630A 140B 138B 128C 136A 138A 620A 130A 130B 623A 146A 128A 136B 139 613A
102946-396EA 331.65 USD
102946-396 102946-330 102946-340 102946-384 102946-394 102946-312 102946-334 102946-388 102946-322 102946-320 102946-386 102946-392 102946-390 102946-316 102946-338 102946-326 102946-336 102946-314 102946-324 102946-308 102946-318 102946-328
Botulinum Toxins, List Biological Laboratories
Microbiology Test Systems Antigen-Antibody Tests Ag-AK, Seren
Clostridium botulinum neurotoxins (BoNT) are among the most toxic substances known to man

Botulinum neurotoxins are valuable research tools in studies aimed at elucidating the mechanisms involved 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 with the 150 kD holotoxin, recombinant nontoxic heavy chains can be used to evaluate the binding properties of the toxins and the recombinant nontoxic light chains can be used to screen for inhibition of the enzymatic activity of the protease domain.

 Seven immunologically distinct serotypes of neurotoxin, designated types A through G (BoNT/A, BoNT/B, BoNT/C, BoNT/D, BoNT/E, BoNT/F, BoNT/G), have been identified.  These neurotoxins are naturally produced complexed with one or more nontoxic neurotoxin-associated proteins (NAPs).  NAPs are important to toxicity by ingestion in that they protect the neurotoxin from proteases, acidity, heat and they may also play a role in translocation across the mucosal layer.  Synthesized as single 150 kDa polypeptide chains, the actual neurotoxin portion of the complex is subsequently activated by cleavage to produce two chains, a heavy chain and a light chain, which are linked 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, which leads to muscular paralysis.  Each toxin is easily divided 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 cleaved by the enzymatic domain.

Ordering information: List Lab's Letter of Assurance form must be filled out by end-user for every order, unless otherwise specified. Shipping address must match purchase order.
Order Now

Learn more

About VWR

Avantor is a vertically integrated, global supplier of discovery-to-delivery solutions for...

Learn more About VWR