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The expression region of this recombinant Human CHRNE covers amino acids 21-239. This CHRNE protein is theoretically predicted to have a molecular weight of 32.5 kDa. This protein is generated in a e.coli-based system. The CHRNE coding gene included the N-terminal 10xHis tag and C-terminal Myc tag, which simplifies the detection and purification processes of the recombinant CHRNE protein in following stages of expression and purification.The human acetylcholine receptor subunit epsilon (CHRNE) is a key component of the nicotinic acetylcholine receptor (nAChR), which is a ligand-gated ion channel found at neuromuscular junctions. CHRNE is predominantly expressed in skeletal muscle and plays a crucial role in neurotransmission by responding to acetylcholine released from nerve terminals. Upon acetylcholine binding, the nAChR undergoes conformational changes, leading to the influx of cations and muscle cell depolarization, ultimately initiating muscle contraction. Mutations in CHRNE can lead to congenital myasthenic syndromes (CMS), a group of genetic neuromuscular disorders characterized by muscle weakness and fatigue. Studying CHRNE helps unravel the mechanisms of neuromuscular communication and aids in understanding and treating related disorders.
The expression region of this recombinant Human CHRNE covers amino acids 21-239. This CHRNE protein is theoretically predicted to have a molecular weight of 32.5 kDa. This protein is generated in a e.coli-based system. The CHRNE coding gene included the N-terminal 10xHis tag and C-terminal Myc tag, which simplifies the detection and purification processes of the recombinant CHRNE protein in following stages of expression and purification.The human acetylcholine receptor subunit epsilon (CHRNE) is a key component of the nicotinic acetylcholine receptor (nAChR), which is a ligand-gated ion channel found at neuromuscular junctions. CHRNE is predominantly expressed in skeletal muscle and plays a crucial role in neurotransmission by responding to acetylcholine released from nerve terminals. Upon acetylcholine binding, the nAChR undergoes conformational changes, leading to the influx of cations and muscle cell depolarization, ultimately initiating muscle contraction. Mutations in CHRNE can lead to congenital myasthenic syndromes (CMS), a group of genetic neuromuscular disorders characterized by muscle weakness and fatigue. Studying CHRNE helps unravel the mechanisms of neuromuscular communication and aids in understanding and treating related disorders.
| Cat.No | ACP01167 | Target Name | CHRNE |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 21-239aa | Mol Weight | 32.5 kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q04844 |
|---|
Uniprot Id
Q04844
Target Species
Human
Target Name
CHRNE
Target Full Name
Acetylcholine receptor subunit epsilon
Target Function
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Target Involvement
Myasthenic syndrome, congenital, 4A, slow-channel (CMS4A); Myasthenic syndrome, congenital, 4B, fast-channel (CMS4B); Myasthenic syndrome, congenital, 4C, associated with acetylcholine receptor deficiency (CMS4C)
Target Subcellular Location
Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Target Protein Families
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Epsilon/CHRNE sub-subfamily
Target Research Area
Others
Target Synonyms
CHRNE; ACHRE; Acetylcholine receptor subunit epsilon
Target Background
Acetylcholine receptors at mature mammalian neuromuscular junctions are pentameric protein complexes composed of four subunits in the ratio of two alpha subunits to one beta, one epsilon, and one delta subunit. The acetylcholine receptor changes subunit composition shortly after birth when the epsilon subunit replaces the gamma subunit seen in embryonic receptors. Mutations in the epsilon subunit are associated with congenital myasthenic syndrome.
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