Analytical Data
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Gene name
SCN10A
- Application
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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
Q9Y5Y9
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Expression Region
M1-P1956, del R934-P1094
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Protein Length
Full Length
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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
SCN10A encodes the sodium channel protein NaV1.8, which is predominantly expressed in sensory neurons and plays a crucial role in pain perception and nociception. Research into SCN10A and its recombinant protein has gained significant attention due to its implications in understanding chronic pain mechanisms and developing novel analgesic therapies. Mutations in this gene have been associated with various pain phenotypes, suggesting that SCN10A is not only vital for normal pain transmission but also a potential target for therapeutic interventions. The functional characterization of SCN10A recombinant proteins allows researchers to elucidate the channel's biophysical properties, pharmacological profiles, and its role in pain pathways. Advances in molecular biology techniques have facilitated the expression and purification of SCN10A in heterologous systems, enabling detailed studies on how specific mutations affect channel function. This research is crucial for identifying molecular targets for drug development aimed at alleviating pain conditions without the side effects associated with current analgesics. As SCN10A continues to be a focal point in pain research, its recombinant protein serves as a valuable tool for understanding the nuances of pain signaling and exploring new therapeutic avenues.
