|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|Human ACHE ORF mammalian expression plasmid, C-GFPSpark tag||HG15847-ACG|
|Human ACHE ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG15847-ACR|
|Human ACHE ORF mammalian expression plasmid, C-Flag tag||HG15847-CF|
|Human ACHE ORF mammalian expression plasmid, C-His tag||HG15847-CH|
|Human ACHE ORF mammalian expression plasmid, C-Myc tag||HG15847-CM|
|Human ACHE ORF mammalian expression plasmid, C-HA tag||HG15847-CY|
|Human ACHE Gene cDNA clone plasmid||HG15847-G|
|Human ACHE ORF mammalian expression plasmid, N-Flag tag||HG15847-NF|
|Human ACHE ORF mammalian expression plasmid, N-His tag||HG15847-NH|
|Human ACHE ORF mammalian expression plasmid, N-Myc tag||HG15847-NM|
|Human ACHE ORF mammalian expression plasmid, N-HA tag||HG15847-NY|
|Human ACHE natural ORF mammalian expression plasmid||HG15847-UT|
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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.