Analytical Data
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Gene name
Kcne2
- Application
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Alternative Names
Kcne2;Potassium voltage-gated channel subfamily E member 2
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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
Q9Y6J6
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Expression Region
1-123aa
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AA Sequence
MSTLSNFTQTLEDVFRRIFITYMDNWRQNTTAEQEALQAKVDAENFYYVI LYLMVMIGMFSFIIVAILVSTVKSKRREHSNDPYHQYIVEDWQEKYKSQI LNLEESKATIHENIGAAGFKMSP
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Molecular Weight
17 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
Kcne2, also known as potassium voltage-gated channel subfamily E member 2, is a member of the KCNE family of proteins that modulate potassium channels. The KCNE proteins are critical for the proper functioning of ion channels, particularly the KCNQ family, which is vital for various physiological processes, including cardiac action potentials and neuronal excitability. Research into Kcne2 has gained momentum due to its potential implications in cardiac and neurological disorders, where alterations in ion channel function can lead to arrhythmias and other pathologies. Understanding the structure-function relationship of Kcne2 is essential for elucidating its role in health and disease. The recombinant expression of Kcne2 allows researchers to study its interactions with potassium channels using electrophysiological techniques and other biochemical assays. This line of research not only sheds light on the biophysical properties of Kcne2 but also opens avenues for therapeutic interventions targeting ion channel dysregulation. Thus, studying Kcne2 reconstituted proteins is crucial for advancing our comprehension of ion channel mechanisms and their significance in various physiological and pathological contexts.










