Acetylcholinesterase Protein, Mouse, Recombinant (His Tag)

• 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.

• Synonyms:

  Acre Protein, Mouse; Chrne Protein, Mouse

• Gene Name:

  Acetylcholinesterase (Yt blood group)

• Expression System:

  HEK293 Cells

• Tag:

  C-His

• Field of Research:

  Neurotransmitter Associated Enzymes Phosphatases and Regulators

• Endotoxin:

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

• Purity:

  > 97 % as determined by SDS-PAGE.

• Activity:

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

• Form:

  Lyophilized

• Buffer:

  Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

• Molecular Weight:

  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.

• Storage Conditions:

  In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.

• Symbol:

  ACHE

• Species:

  Mouse

• Protein ID:

  NP_033729.1

• Overview:

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

• AA Sequence:

  Met1-Leu614

• Protein ID Link:

  https://www.ncbi.nlm.nih.gov/protein/NP_033729.1