Analytical Data
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Gene name
scn
- Application
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Alternative Names
scn；KIAA1356；NAC3；Sodium channel Protein type 3 subunit alpha
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A7X482
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Expression Region
32-116aa
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AA Sequence
STSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYKRTIKISGQKAMYALKSKDFKKMSEAKYQLQKIYNEIDEALKSKY
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Molecular Weight
17.2 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
SCN (sodium channel) recombinant proteins are increasingly significant in the field of electrophysiology and pharmacology due to their role in understanding ion channel function and drug interactions. Sodium channels are crucial for the generation and propagation of action potentials in excitable cells, such as neurons and muscle fibers. Alterations in their function are implicated in various diseases, including epilepsy, cardiac arrhythmias, and chronic pain syndromes. The study of SCN recombinant proteins allows researchers to investigate the structure-function relationships of these channels, enabling insights into their gating mechanics and permeability properties. Moreover, the ability to produce these proteins in a recombinant form facilitates a range of experimental approaches, from patch-clamp electrophysiology to high-throughput screening of potential therapeutic compounds. As more sodium channel isoforms are identified, recombinant techniques play a pivotal role in characterizing their distinct biophysical properties and pharmacological profiles, contributing to the development of targeted therapies and a better understanding of channelopathies. Overall, the research on SCN recombinant proteins not only enhances the fundamental knowledge of ionic conductance but also paves the way for innovative treatments for various sodium channel-related disorders.
