Rat Acetylcholinesterase (AChE) Protein

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Proteins and Peptides

Acetylcholinesterase (AChE)

E. coli

Activity: Not tested
Sequence Fragment: Gly157-Pro332
Tag: N-terminal His tag

Rat

Unconjugated

Calculated MW: 20.2 kDa

Recombinant

> 95%

10 µg

50 µg

100 µg

200 µg

500 µg

Lyophilized

WB, SDS-PAGE

Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.

Shipped within 5-7 working days.

Store lyophilized form at 2-8°C for up to 1 month. For longer periods, store lyophilized or liquid at -80°C. Avoid repeated freeze–thaw cycles.

No

P37136

YT,ACEE,ARACHE,N-ACHE

Protein AChE

RUO

THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.
To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Concentration: Prior to lyophilization: 200 µg/ml

Background

Acetylcholinesterase (AChE) is an enzyme that plays a critical role in the nervous system by breaking down the neurotransmitter acetylcholine. AChE is a globular protein, typically found as a tetramer composed of four subunits. Each subunit contains a catalytic site responsible for the enzymatic breakdown of acetylcholine. Acetylcholine is involved in transmitting signals across synapses, which are the gaps between nerve cells. After acetylcholine has transmitted its signal, AChE rapidly breaks it down into its constituent parts: choline and acetate. This breakdown process is crucial for terminating the signal transmission and allowing the nerve cell to return to its resting state . AChE is found primarily at cholinergic synapses, where acetylcholine is released as a neurotransmitter. These synapses are abundant in the central nervous system (CNS) and the peripheral nervous system (PNS). At neuromuscular junctions, AChE is particularly important for allowing muscles to relax after contraction. When a motor neuron releases acetylcholine to signal muscle contraction, AChE quickly degrades the acetylcholine, allowing the muscle to relax. AChE activity can be regulated through various mechanisms, including gene expression, post-translational modifications, and interactions with other proteins. Dysregulation of AChE activity has been implicated in various neurological disorders, including Alzheimer's disease and myasthenia gravis.

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