Analytical Data
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Gene name
INa
- Application
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Alternative Names
INa；FXNA；KIAA1815；Endoplasmic reticulum metallopeptidase 1
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Species
Human
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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
Q16352
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Expression Region
1-499aa
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AA Sequence
MSFGSEHYLCSSSSYRKVFGDGSRLSARLSGAGGAGGFRSQSLSRSNVASSAACSSASSLGLGLAYRRPPASDGLDLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRDLRAQLEEASSARSQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDVTVAKPDLTSALREIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVAGYQDSIGQLENDLRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTSGLSISGLNPLPNPSYLLPPRILSATTSKVSSTGLSLKKEEEEEEASKVASKKTSQIGESFEEILEETVISTKKTEKSNIEETTISSQKI
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Molecular Weight
55.3 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
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Protein Description
INa recombinant proteins have garnered significant interest in scientific research due to their critical role in understanding ion channel physiology and pathophysiology. In particular, the voltage-gated sodium channels (NaV), encoded by the SCN genes, are essential for the initiation and propagation of action potentials in neurons and muscle cells. Abnormalities in these channels can lead to various neurological disorders, cardiac arrhythmias, and other health issues. The expression and purification of INa recombinant proteins allow researchers to study the structural and functional properties of these channels in detail. By utilizing advanced techniques such as cryo-electron microscopy and electrophysiological assays, scientists can elucidate the mechanisms of ion conductance, gating kinetics, and the effects of pharmacological agents on channel activity. Moreover, INa recombinant proteins serve as valuable tools in drug discovery and development, facilitating the screening of compounds that can modulate channel function, potentially leading to novel therapeutic strategies for diseases linked to sodium channel dysfunction. Understanding INa channels through recombinant protein studies is therefore pivotal for advancing both basic science and clinical applications in neurology and cardiology.
