Analytical Data
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Gene name
Cobrotoxin
- Application
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Alternative Names
(CBT)(CBTX)(CTX)(Atratoxin)(Cobratide)(Short neurotoxin 1)
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Species
Naja atra
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Source
E. coli
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Tag
N- His-KSI
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P60770
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Expression Region
22-83aa
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Molecular Weight
22.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Cobrotoxin, a neurotoxic protein derived from the venom of the Taiwanese cobra (Naja naja atra), has garnered significant interest in the field of biomedical research due to its potential therapeutic applications. This 20-kDa polypeptide primarily targets nicotinic acetylcholine receptors (nAChRs), leading to neuromuscular paralysis and respiratory failure. The study of cobrotoxin and its recombinant form, produced through genetic engineering techniques, is pivotal for understanding its mechanism of action and developing novel pharmacological agents. Research has indicated that cobrotoxin can serve as a valuable tool in neuroscience, particularly in the exploration of synaptic transmission and receptor function. Moreover, its unique properties make it a candidate for developing pain management therapies and studying autoimmune diseases. The ability to produce cobrotoxin recombinantly allows for controlled studies, minimizing the ethical concerns associated with snake venom extraction. This progress in recombinant protein technology enhances the potential for cobrotoxin-based drugs, which could provide alternatives to traditional treatments, thereby paving the way for innovative approaches in both pain relief and neurological research. Overall, understanding cobrotoxin at a molecular level not only contributes to basic science but also opens up avenues for clinical applications, emphasizing the importance of this research in the broader context of medical science.
