Analytical Data
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Gene name
SCNN1g
- Application
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Alternative Names
ENaCg; ENaCgamma; PHA1; SCNEG; Sodium Channel,Nonvoltage-Gated 1,Alpha; Epithelial Na(+) channel subunit gamma; Nonvoltage-gated sodium channel 1 subunit gamma
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P51170
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Expression Region
Thr80~Thr401
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Molecular Weight
41kDa
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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
SCNN1G, a member of the epithelial sodium channel (ENaC) family, plays a crucial role in sodium absorption and fluid homeostasis in epithelial tissues. It is predominantly expressed in the kidney and airway epithelia, where it contributes to the regulation of electrolyte balance and blood pressure. Mutations in the SCNN1G gene have been linked to several disorders, including Liddle syndrome, characterized by hypertension resulting from increased sodium retention. The study of SCNN1G recombinant proteins has gained significant attention in recent years, as it offers insights into the structure-function relationships of ion channels and their regulatory mechanisms. Researchers are focusing on the purification and characterization of SCNN1G to better understand its physiological role and the impact of genetic variations on its function. The recombinant forms of SCNN1G can be utilized to elucidate its interaction with various channel regulators and pharmacological agents, thereby paving the way for novel therapeutic approaches to manage conditions associated with dysfunctional sodium transport. Advances in recombinant protein technology have made it feasible to produce SCNN1G in heterologous expression systems, facilitating the development of high-throughput assays that can screen for potential drug candidates targeting ENaC-related pathologies. Overall, understanding SCNN1G at the molecular level not only deepens our comprehension of epithelial transport mechanisms but also holds promise for targeted interventions in sodium-related diseases.
