Analytical Data
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Gene name
ACHE
- Application
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Alternative Names
ARAChE; N-AChE; YT
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Species
Mouse
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Source
HEK293
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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
P21836
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Expression Region
Glu32~Leu614
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Molecular Weight
70kDa
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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
Acetylcholinesterase (ACHE) is a crucial enzyme involved in the hydrolysis of the neurotransmitter acetylcholine, playing a vital role in neurotransmission and muscle function. The dysfunction of ACHE has been implicated in various neurological disorders, including Alzheimer’s disease and myasthenia gravis, making it a significant target for therapeutic interventions. The study of recombinant ACHE proteins has gained prominence in recent years due to their potential applications in both basic research and clinical settings. Recombinant technology allows for the production of ACHE in controlled environments, ensuring high yield and purity, which can facilitate detailed studies on enzyme kinetics, substrate specificity, and inhibitor interactions. Moreover, understanding the structural and functional properties of recombinant ACHE can aid in the design of novel pharmacological agents aimed at modulating cholinergic signaling. Advances in molecular biology and protein engineering have enabled modifications in ACHE that enhance its stability and activity, paving the way for innovative treatments for diseases characterized by cholinergic dysfunction. Additionally, recombinant ACHE is also utilized in the development of biosensors for detecting organophosphates and other neurotoxins, showcasing its relevance beyond traditional enzymology. Overall, research on recombinant ACHE proteins is at the forefront of addressing pressing challenges in neuroscience and toxicology, making it a promising area for future investigation and therapeutic development.
