Acetylcholinesterase Protein (AChE) (His tag)

Catalog No. ABIN7320239

Recombinant Acetylcholinesterase protein expressed in HEK-293 Cells.

Quick Overview for Acetylcholinesterase Protein (AChE) (His tag) (ABIN7320239)

Target: Acetylcholinesterase (AChE)

Protein Type: Recombinant

Biological Activity: Active

Origin: Mouse

Source: HEK-293 Cells

Purity: > 97 % as determined by SDS-PAGE

Product Details

Purification tag / Conjugate: This Acetylcholinesterase protein is labelled with His tag.

Purpose: Recombinant Mouse Acetylcholinesterase/ACHE Protein (His Tag)(Active)

Sequence: Met 1-Leu 614

Characteristics: A DNA sequence encoding the mouse ACHE (NP_033729.1) (Met 1-Leu 614) was expressed, with a polyhistidine tag at the C-terminus.

Endotoxin Level: < 1.0 EU per μg of the protein as determined by the LAL method.

Biological Activity Comment: Measured by its ability to cleave Acetylthiocholine.The specific activity is > 250 nmols/min/μg.

Application Details

Restrictions: For Research Use only

Handling

Format: Lyophilized

Reconstitution: Please refer to the printed manual for detailed information.

Buffer: Lyophilized from sterile PBS, pH 7.4

Storage: 4 °C,-20 °C,-80 °C

Storage Comment: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Target Details

Target: Acetylcholinesterase (AChE)

Alternative Name: Acetylcholinesterase/ACHE

Background:

Background: Acetylcholinesterase, also known as ACHE, is an enzyme that degrades (through its hydrolytic activity) the neurotransmitter acetylcholine, producing choline and an acetate group. Acetylcholinesterase plays a crucial role in nerve impulse transmission at cholinergic synapses by rapid hydrolysis of the neurotransmitter acetylcholine (ACh). ACHE appears to be a potential therapeutic target at muscle injuries including organophosphate myopathy. It is an externally oriented membrane-bound enzyme and its main physiological role is termination of chemical transmission at cholinergic synapses and secretory organs by rapid hydrolysis of the neurotransmitter acetylcholine (ACh). ACHE plays important roles in the cholinergic system, and its dysregulation is involved in a variety of human diseases. ACHE was significantly down-regulated in the cancerous tissues of 69.2 % of hepatocellular carcinoma (HCC) patients, and the low ACHE expression in HCC was correlated with tumor aggressiveness, an elevated risk of postoperative recurrence, and a low survival rate. Both the recombinant ACHE protein and the enhanced expression of ACHE significantly inhibited HCC cell growth in vitro and tumorigenicity in vivo. ACHE as a tumor growth suppressor in regulating cell proliferation, the relevant signaling pathways, and the drug sensitivity of HCC cells. Thus, ACHE is a promising independent prognostic predictor for HCC recurrence and the survival of HCC patients. ACHE is responsible for the hydrolysis of acetylcholine in the nervous system. It is inhibited by organophosphate and carbamate pesticides. However, this enzyme is only slightly inhibited by organophosphorothionates.

Synonym: mE1a, mE1b, mE1c, mE1c-long, mE1d, mE1d', mE1e

Molecular Weight: 66.2 kDa

NCBI Accession: NP_033729

Pathways: Skeletal Muscle Fiber Development