ACHE antibody
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Description
Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | acetylcholinesterase (Yt blood group) (ACHE) |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Recommended Dilution | WB: 1:500 - 1:2000; IHC: 1:50 - 1:100 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 71 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB, IHC |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months (Avoid repeated freeze / thaw cycles.) |
| UniProt ID | P22303 |
| Gene ID | 43 |
| Alias | YT,ACEE,ARACHE,N-ACHE |
| Background | Antibody anti-ACHE |
| Status | RUO |
| Note | Mol. Weight 71 kDa |
Descripción
Acetylcholinesterase (AChE) is an enzyme that plays a critical role in the nervous system by breaking down the neurotransmitter acetylcholine. AChE is a globular protein, typically found as a tetramer composed of four subunits. Each subunit contains a catalytic site responsible for the enzymatic breakdown of acetylcholine. Acetylcholine is involved in transmitting signals across synapses, which are the gaps between nerve cells. After acetylcholine has transmitted its signal, AChE rapidly breaks it down into its constituent parts: choline and acetate. This breakdown process is crucial for terminating the signal transmission and allowing the nerve cell to return to its resting state . AChE is found primarily at cholinergic synapses, where acetylcholine is released as a neurotransmitter. These synapses are abundant in the central nervous system (CNS) and the peripheral nervous system (PNS). At neuromuscular junctions, AChE is particularly important for allowing muscles to relax after contraction. When a motor neuron releases acetylcholine to signal muscle contraction, AChE quickly degrades the acetylcholine, allowing the muscle to relax. AChE activity can be regulated through various mechanisms, including gene expression, post-translational modifications, and interactions with other proteins. Dysregulation of AChE activity has been implicated in various neurological disorders, including Alzheimer's disease and myasthenia gravis.
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ACHE antibody
Acetylcholinesterase hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. Acetylcholinesterase exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. It is encoded by the single ACHE gene, and the structural diversity in the gene products arises from alternative mRNA splicing, and post-translational associations of catalytic and structural subunits. The major form of acetylcholinesterase found in brain, muscle and other tissues is the hydrophilic species, which forms disulfide-linked oligomers with collagenous, or lipid-containing structural subunits. The other, alternatively spliced form, expressed primarily in the erythroid tissues, differs at the C-terminal end, and contains a cleavable hydrophobic peptide with a GPI-anchor site. It associates with the membranes through the phosphoinositide (PI) moieties added post-translationally.
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