Analytical Data
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Gene name
CfTX
- Application
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Alternative Names
Toxin CfTX-1; Toxin 1
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Species
Chironex fleckeri
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A7L035
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Expression Region
21-456aa
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Molecular Weight
65.1 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
Related Products
Protein Description
CfTX (Cyclosporine F, a toxin derived from the venom of Conus species) has garnered significant interest in the field of biochemistry and pharmacology due to its unique structural properties and potential therapeutic applications. Research into CfTX-recombinant proteins aims to harness the specific interactions that these toxins exhibit with ion channels, particularly voltage-gated sodium channels, which play a crucial role in neuronal signaling and muscle contraction. The ability to manipulate and produce recombinant versions of CfTX not only enables detailed studies of its mechanism of action but also opens avenues for developing novel analgesics, as these toxins are known to possess potent pain-relieving properties. The production of recombinantly expressed CfTX allows for the investigation of structure-activity relationships and the optimization of its pharmacological properties. Given the increasing prevalence of chronic pain conditions and the limitations of current analgesic therapies, understanding CfTX's biological effects through recombinant technology could lead to innovative treatments. Furthermore, studying its interactions at the molecular level may shed light on the evolutionary adaptations of cone snail venoms, contributing to our knowledge of neurotoxicology and proteins’ evolutionary biology. Thus, ongoing research on CfTX-recombinant proteins holds promise for both advancing fundamental science and addressing pressing medical needs.
