|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Mouse ACHE ORF mammalian expression plasmid, C-GFPSpark tag||MG50543-ACG|
|Mouse ACHE ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50543-ACR|
|Mouse ACHE ORF mammalian expression plasmid, C-Flag tag||MG50543-CF|
|Mouse ACHE ORF mammalian expression plasmid, C-His tag||MG50543-CH|
|Mouse ACHE ORF mammalian expression plasmid, C-Myc tag||MG50543-CM|
|Mouse ACHE ORF mammalian expression plasmid, C-HA tag||MG50543-CY|
|Mouse ACHE Gene cDNA clone plasmid||MG50543-M|
|Mouse ACHE ORF mammalian expression plasmid, N-Flag tag||MG50543-NF|
|Mouse ACHE ORF mammalian expression plasmid, N-His tag||MG50543-NH|
|Mouse ACHE ORF mammalian expression plasmid, N-Myc tag||MG50543-NM|
|Mouse ACHE ORF mammalian expression plasmid, N-HA tag||MG50543-NY|
|Mouse ACHE natural ORF mammalian expression plasmid||MG50543-UT|
|Learn more about expression Vectors|
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.