Botulinum Toxin
From CAD $150 CAD $167
Contents: Botulinum Toxin Type A (Neurotoxin Complex)
Form: Powder
Purity: 99.3%
TESTED FOR:
- PURITY
- STERILITY
- WEIGHT
- ENDOTOXINS(LPS)
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Botulinum Toxin Type A – 100 IU
Botulinum Toxin Type A is a neurotoxic protein complex produced by Clostridium botulinum. It exerts its biological activity by cleaving SNAP-25, a synaptosomal-associated protein required for acetylcholine vesicle fusion at the neuromuscular junction. This results in a reversible blockade of cholinergic neurotransmission, leading to temporary muscle relaxation.
In research settings, Botulinum Toxin Type A is used to study synaptic vesicle cycling, neurotransmitter release mechanisms, and neuromuscular physiology, as well as for modeling neuroparalytic disorders and axon terminal regeneration.
Overview
Botulinum neurotoxins are zinc-dependent endopeptidases composed of a heavy (100 kDa) and light (50 kDa) chain connected via a disulfide bond. The heavy chain mediates binding and internalization into cholinergic neurons, while the light chain enzymatically cleaves SNARE complex proteins, preventing neurotransmitter release.
Type A, the most extensively studied serotype, exhibits high potency and prolonged duration of effect compared to other isoforms. Its mechanism provides a reproducible model system for investigating vesicle exocytosis and synaptic recovery following toxin exposure.
Chemical Makeup
- Active Component: Botulinum neurotoxin type A (150 kDa neurotoxin complex)
- Source Organism: Clostridium botulinum
- Molecular Weight: ~900 kDa (complex with accessory proteins)
- Unit Potency: 100 IU per vial (per COA)
- Mechanism: Zinc-endopeptidase cleavage of SNAP-25
- Form: Lyophilized powder for reconstitution
- Purity: ≥99% (per COA)
- Storage: ≤ –20 °C (protected from light and moisture)
Research and Experimental Applications
Neurotransmitter Release and Synaptic Function
Botulinum Toxin Type A is a reference inhibitor for synaptic vesicle exocytosis. It is utilized to dissect presynaptic membrane dynamics, SNARE complex assembly, and calcium-dependent neurotransmitter release.
Neuromuscular Transmission Studies
Through its highly specific inhibition of acetylcholine release, Botulinum Toxin A provides a controlled model to investigate muscle contraction, denervation, and subsequent axonal sprouting or reinnervation.
Neuroregeneration and Axon Plasticity
The reversible nature of the blockade allows study of neuronal repair and synaptic remodeling following chemical denervation, offering insights into regenerative processes and motor end-plate recovery.
Autonomic and Sensory Pathways
Research also explores non-motor effects of the toxin, including modulation of pain signaling, sensory neurotransmission, and autonomic neurotransmitter release, helping elucidate broader neuronal control mechanisms.
Pharmacokinetics and Duration
The biological effect begins within hours of exposure, peaks between 2–7 days, and gradually declines as new SNARE proteins are synthesized. The functional blockade typically persists for 3–4 months in animal models.
Botulinum Toxin A is available for research and laboratory purposes only. Not for human or veterinary use.
References
- Montecucco C, et al. Mechanism of action of botulinum neurotoxins. Microbiol Mol Biol Rev. 2004;68(3):373–402. https://pubmed.ncbi.nlm.nih.gov/15353562/
- Rossetto O, Pirazzini M, Montecucco C. Botulinum neurotoxins: structure, function and therapeutic use. Pharmacol Rev. 2014;66(1):80–120. https://pubmed.ncbi.nlm.nih.gov/24381391/
- Binz T, Rummel A. Cell entry strategy of clostridial neurotoxins. Toxicon. 2009;54(5):557–562. https://pubmed.ncbi.nlm.nih.gov/19166869/
- Dolly JO, et al. Molecular basis for the inhibition of neurotransmitter release by clostridial neurotoxins. Prog Brain Res. 2004;146:525–537. https://pubmed.ncbi.nlm.nih.gov/14699988/
- Foran PG, et al. Inhibition of exocytosis by botulinum neurotoxins: effects on synaptic proteins. J Biol Chem. 1996;271(23):16008–16011. https://pubmed.ncbi.nlm.nih.gov/8663041/
- Meunier FA, et al. Molecular interactions of botulinum toxin with nerve terminals. Curr Opin Pharmacol. 2003;3(3):308–314. https://pubmed.ncbi.nlm.nih.gov/12810165/
- Keller JE. Recovery from botulinum intoxication in neurons. Neuroscience. 2006;139(2):629–637. https://pubmed.ncbi.nlm.nih.gov/16469380/
- Mazzocchio R, Caleo M. Plastic changes following botulinum toxin type A in motor systems. Neuroscientist. 2015;21(5):594–604. https://pubmed.ncbi.nlm.nih.gov/25505190/
- Dressler D. Pharmacology of botulinum toxin. Drugs R D. 2012;12(1):5–16. https://pubmed.ncbi.nlm.nih.gov/22376018/
- Pirazzini M, et al. Uptake and trafficking of botulinum neurotoxins. Cell Microbiol. 2011;13(1):1–14. https://pubmed.ncbi.nlm.nih.gov/21029261/
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