Analytical Data
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Gene name
VSD4-NaV1.7-NaVPas
- Application
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Alternative Names
NENA
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Species
Human
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Source
HEK293
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Tag
Strep;Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15858-1
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Expression Region
M1-G1505
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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
The research on the recombinant protein VSD4-NaV1.7-NaVPas is primarily rooted in the investigation of voltage-gated sodium channels, particularly NaV1.7, which plays a crucial role in the initiation and propagation of action potentials in neurons. NaV1.7 has garnered significant attention due to its involvement in pain signaling; mutations in the SCN9A gene, which encodes NaV1.7, are associated with various pain disorders, ranging from congenital insensitivity to pain to extreme pain sensitivity. Understanding the structure and function of this channel is essential for developing targeted analgesic therapies. The VSD4 region of NaV1.7, which is critical for voltage sensing, and its interaction with NaVPas (a peptide derived from the venom of the spider species, Loxosceles laeta) provide a unique insight into the modulation of sodium channels. This recombinant protein allows researchers to explore the intricate mechanisms of sodium channel gating and pharmacology, enhancing the prospective development of novel pain management strategies and channel blockers. By employing advanced genetic engineering techniques, the VSD4-NaV1.7-NaVPas recombinant construct enables the detailed study of channel behavior in response to voltage changes and pharmacological agents, contributing to a deeper understanding of pain mechanisms and the potential for innovative therapeutic approaches.
