Acetylcholinesterase: Acetylcholinesterase Protein | Acetylcholinesterase Antibody

Acetylcholinesterase Gene family

Acetylcholinesterase 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.

Reference for Acetylcholinesterase

  • Zhao Y, et al. (2011) Acetylcholinesterase, a key prognostic predictor for hepatocellular carcinoma, suppresses cell growth and induces chemosensitization. Hepatology. 53(2): 493-503.
  • Roepcke CB, et al. (2010) Analysis of phosphorothionate pesticides using a chloroperoxidase pretreatment and acetylcholinesterase biosensor detection. J Agric Food Chem. 58(15): 8748-56.
  • Zaheer-ul-Haq, et al. (2010) Benchmarking docking and scoring protocol for the identification of potential acetylcholinesterase inhibitors. J Mol Graph Model. 28(8): 870-82.
  • Pegan K, et al. (2010) Acetylcholinesterase is involved in apoptosis in the precursors of human muscle regeneration. Chem Biol Interact. 187(1-3): 96-100.

Acetylcholinesterase Protein

Acetylcholinesterase protein function

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis. {ECO:0000269|PubMed:11985878, ECO:0000269|PubMed:1517212, ECO:0000269|PubMed:1748670, ECO:0000269|PubMed:2714437}.

Acetylcholinesterase protein expression

Tissue specificity

Isoform H is highly expressed in erythrocytes.

Acetylcholinesterase protein sequence

This sequence information is just for reference only.From Uniport

  • Length
  • Mass (Da)

Acetylcholinesterase Antibody

There are 2 Acetylcholinesterase antibodies which are validated in multiple tissues with various applications, including ELISA, IHC-P. There are 2 Acetylcholinesterase antibody for ELISA, 1 Acetylcholinesterase antibody for IHC-P. Among all these Acetylcholinesterase antibodies, there are 2 anti-Acetylcholinesterase rabbit polyclonal antibodies . All the Acetylcholinesterase anbodies are produced in house and all are in stock. Acetylcholinesterase antibody customerized service is available.

Acetylcholinesterase Gene

ACHE gene / cDNA is a protein-coding gene which located on 7q22.1. The ACHE gene is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, mosquito, C.elegans, M.oryzae, and frog.174 organisms have orthologs with human gene ACHE.