Acetylcholinesterase / ACHE Recombinant Protein | ACHE recombinant protein

Recombinant Mouse Acetylcholinesterase / ACHE Protein (His tag)

Cat. Num. AAA2546923

• Purity: > 97 % as determined by SDS-PAGE
• Synonyms: Acetylcholinesterase / ACHE; Recombinant Mouse Acetylcholinesterase / ACHE Protein (His tag); mE1a; mE1b; mE1c; mE1c-long; mE1d; mE1d'; mE1e; ACHE recombinant protein

• Host: Human Cells
• Purity/Purification: > 97 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 614

• Application Notes: The recombinant mouse ACHE consists of 594 amino acids and has a predicted molecular mass of 66.2 kDa as estimated in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Glu 32
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for ACHE recombinant protein

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.

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

NCBI and Uniprot Product Information

• NCBI GI #: 13928664
• NCBI GeneID: 11423
• NCBI Accession #: NP_033729.1
• NCBI GenBank Nucleotide #: NM_009599.4
• UniProt Accession #: P21836
• Molecular Weight: – Da
• NCBI Official Full Name: acetylcholinesterase
• NCBI Official Synonym Full Names: acetylcholinesterase
• NCBI Official Symbol: Ache
• NCBI Protein Information: acetylcholinesterase
• UniProt Protein Name: Acetylcholinesterase
• UniProt Gene Name: Ache
• UniProt Synonym Gene Names: AChE

Uniprot Description

AChE: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis. Belongs to the type-B carboxylesterase/lipase family. 4 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.1.1.7; Hydrolase; Lipid Metabolism - glycerophospholipid; Membrane protein, GPI anchor

Chromosomal Location of Human Ortholog: 5 G2|5 76.32 cM

Cellular Component: axon; basal lamina; cell soma; cell surface; cytoplasm; dendrite; endoplasmic reticulum lumen; extracellular region; extracellular space; Golgi apparatus; membrane; neuromuscular junction; neuron projection; nuclear envelope; perinuclear region of cytoplasm; plasma membrane; postsynaptic membrane; presynaptic membrane; rough endoplasmic reticulum; synapse

Molecular Function: acetylcholine binding; acetylcholinesterase activity; choline binding; cholinesterase activity; collagen binding; hydrolase activity; laminin binding; protein binding; protein homodimerization activity; protein self-association; serine hydrolase activity

Biological Process: acetylcholine catabolic process; acetylcholine metabolic process; cell adhesion; choline metabolic process; neurotransmitter receptor biosynthetic process; positive regulation of axonogenesis; positive regulation of dendrite morphogenesis; protein tetramerization; receptor internalization; regulation of receptor recycling; retina development in camera-type eye; synaptogenesis