Analytical Data
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Gene name
Acetylcholinesterase/ACHE
- Application
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Alternative Names
ARAChE; N-AChE; YT
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Species
Bovine
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23795
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Expression Region
Glu31~Leu613
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Molecular Weight
68kDa
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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
Acetylcholinesterase (AChE) is a crucial enzyme that catalyzes the hydrolysis of the neurotransmitter acetylcholine (ACh) in the synaptic cleft, thus playing a vital role in terminating cholinergic signaling and ensuring proper neuromuscular function. Its dysfunction is implicated in various neurological disorders, including Alzheimer’s disease, where the disruption of cholinergic transmission contributes to cognitive decline. The recombinant expression of AChE offers a powerful tool for studying its structure-function relationships, enzyme kinetics, and interactions with inhibitors, which is essential for drug design and therapeutic development. Advances in molecular biology techniques, such as gene cloning and protein expression systems, have enabled the production of highly pure and active recombinant AChE from various sources, including human, rat, and alternative model organisms. These advancements facilitate detailed biochemical and pharmacological studies that enhance the understanding of AChE's role in physiological and pathological processes. Furthermore, recombinant AChE provides a useful platform for screening potential drugs that can modulate its activity, thus contributing to the development of novel treatments for conditions where cholinergic signaling is impaired. Overall, the study of recombinant AChE continues to be a significant area of research with implications for neurobiology and pharmacotherapy.
