Analytical Data
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Gene name
bCTx
- Application
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Alternative Names
bCTx；
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P59891
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Expression Region
1-30aa
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AA Sequence
LKDGYPTNSKGCKISGCLPGENKFCLNECQ
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Molecular Weight
3.2 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
bCTx, or beta-conotoxin, is a type of peptide derived from the venom of marine cone snails, specifically from the Conus species. These toxins are known for their ability to selectively target ion channels and receptors, making them valuable for both pharmacological research and potential therapeutic applications. The unique structure and specificity of bCTx peptides allow them to modulate neuronal excitability and muscle contraction, which has led researchers to explore their roles in understanding pain mechanisms, neurological disorders, and muscle diseases. The study of bCTx recombinant proteins involves the use of genetic engineering techniques to produce these peptides in a controlled laboratory environment, facilitating detailed examination of their interactions with biological targets. This burgeoning field of research not only aids in deciphering the complex functioning of ion channels and receptors but also paves the way for the development of new drugs that can mimic or block the action of these natural toxins. Furthermore, the potential to create modified versions of bCTx may enhance their efficacy and selectivity, making them promising candidates for novel therapeutic interventions. Through the continued investigation of bCTx recombinant proteins, scientists aim to leverage the intricate mechanisms of these natural venoms for advances in medical science, particularly in pain management and neurological health.
