Analytical Data
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Gene name
CHRNE
- Application
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Alternative Names
CHRNE；ACHRE；Acetylcholine receptor subunit epsilon
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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
Q04844
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Expression Region
21-239aa
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AA Sequence
KNEELRLYHHLFNNYDPGSRPVREPEDTVTISLKVTLTNLISLNEKEETLTTSVWIGIDWQDYRLNYSKDDFGGIETLRVPSELVWLPEIVLENNIDGQFGVAYDANVLVYEGGSVTWLPPAIYRSVCAVEVTYFPFDWQNCSLIFRSQTYNAEEVEFTFAVDNDGKTINKIDIDTEAYTENGEWAIDFCPGVIRRHHGGATDGPGETDVIYSLIIRRK
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Molecular Weight
31.9 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
CHRNE, or the cholinergic receptor nicotinic epsilon subunit, is a critical component of the nicotinic acetylcholine receptor (nAChR), which plays a significant role in neuromuscular transmission and neurotransmission in the central nervous system. Research on CHRNE is imperative due to its involvement in various physiological processes, and its implications in several neuromuscular disorders, such as congenital myasthenic syndromes and other autoimmune diseases like myasthenia gravis. Given the importance of nAChRs in mediating excitatory neurotransmission, CHRNE’s structural and functional characteristics are crucial for understanding receptor assembly, ion channel function, and receptor pharmacology. The recombinant expression of CHRNE in various systems, including mammalian cells and yeast, facilitates detailed analysis of its biophysical properties, ligand-binding characteristics, and interaction with other receptor subunits. This research not only advances our understanding of the fundamental biology of nicotinic receptors but also lays the groundwork for the development of targeted therapeutic strategies to treat diseases associated with nAChR dysfunction. Moreover, by investigating the structure and function of CHRNE, researchers aim to identify novel drug targets and improve existing treatment modalities for related neurological and muscular disorders, thereby enhancing therapeutic outcomes for affected patients.
