Analytical Data
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Gene name
CHRNb2
- Application
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Alternative Names
CHRNb2；Neuronal acetylcholine receptor subunit beta-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
P17787
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Expression Region
26-233aa
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AA Sequence
TDTEERLVEHLLDPSRYNKLIRPATNGSELVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWKPEEFDNMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCTMKFRSWTYDRTEIDLVLKSEVASLDDFTPSGEWDIVALPGRRNENPDDSTYVDITYDFIIRRK
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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
CHRNb2, or the beta-2 subunit of the nicotinic acetylcholine receptor, has garnered significant attention in biomedical research due to its critical role in neurotransmission and neural signaling. As a part of the ligand-gated ion channel family, CHRNb2 is integral to the modulation of synaptic activity in the nervous system. Alterations or dysfunctions in its expression are associated with various neurological disorders, including addiction, anxiety, and neurodegenerative diseases. Understanding the structure and function of CHRNb2 is essential for developing therapeutic strategies that target these pathways. The recombinant protein expression of CHRNb2 provides a valuable tool for studying its biochemical properties and interactions with other receptor subunits and ligands. By producing this protein in a controlled laboratory environment, researchers can investigate its role in receptor assembly, ion conduction, and cellular signaling processes in detail. Additionally, the availability of CHRNb2 in recombinant form facilitates high-throughput screening of small molecules that may modulate its activity, providing potential avenues for drug discovery. Overall, the study of CHRNb2 recombinant protein is a promising area of research that could enhance our understanding of cholinergic signaling and its implications for treating various neurological conditions.
