Analytical Data
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Gene name
SCN1A
- Application
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Alternative Names
Sodium channel protein brain I subunit alpha;Sodium channel protein type I subunit alpha;Voltage-gated sodium channel subunit alpha Nav1.1
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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
P35498
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Expression Region
1-128aa
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Molecular Weight
18.5 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
SCN1A encodes the alpha subunit of the voltage-gated sodium channel NaV1.1, which is crucial for the generation and propagation of action potentials in neurons. Mutations in the SCN1A gene are associated with various neurological disorders, particularly Dravet syndrome, a severe form of epilepsy that manifests in early childhood. Due to its significant role in neuronal excitability and synaptic transmission, SCN1A has garnered considerable attention in both clinical and research settings. Understanding the functional implications of SCN1A mutations requires detailed studies of the recombinant protein, which allows for the investigation of channel dynamics, pharmacological properties, and the effects of specific mutations. Furthermore, the development of SCN1A-recombinant protein not only enhances our understanding of its structure-function relationships but also aids in the identification of potential therapeutic targets for sodium channel dysfunction-related disorders. Insights gained from recombinant SCN1A can pave the way for innovative treatments, including the exploration of small molecules and gene therapies aimed at correcting or mitigating the effects of SCN1A mutations. Consequently, thorough research on SCN1A recombinant proteins is essential for unraveling the complexities of sodium channel biology and for advancing the management of epilepsy and related neurological disorders.
