- Peptide EHETRLVAKLFKD(C), corresponding to amino acid residues 22-34 of rat nAChRα1 (Accession P25108). Extracellular, N-terminus.
- Western blot analysis of rat skeletal muscle (lanes 1 and 3) and mouse C2C12 myoblasts (lanes 2 and 4):1,2. Anti-Nicotinic Acetylcholine Receptor α1 (CHRNA1) (extracellular) Antibody (#ANC-001), (1:200).
3,4. Anti-Nicotinic Acetylcholine Receptor α1 (CHRNA1) (extracellular) Antibody, preincubated with Nicotinic Acetylcholine Receptor α1/CHRNA1 (extracellular) Blocking Peptide (#BLP-NC001).
- Albuquerque, E.X. et al. (2009) Physiol. Rev. 89, 73.
- Karlin, A. et al. (1986) Ann. NY. Acad. Sci. 463, 53.
- Kalamida, D. et al. (2007) FEBS J. 274, 3799.
- Barkas, T. et al. (1987) Science 235, 77.
- Lindstrom, J.M. (2000) Muscle Nerve 23, 453.
- Neumann, D. et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 3008.
Acetylcholine, released by cholinergic neurons, activates two groups of acetylcholine receptors (AChRs); muscarinic AChRs (mAChRs) which belong to the superfamily of G-protein coupled receptors (GPCRs), and nicotinic AChRs (nAChRs) which belong to the ligand-gated ion channel superfamily. nAChRs also respond to nicotine, hence their name1.
To date, 17 different but related subunits of nAChRs have been identified and cloned. They consist of α subunits (α1-10), which is responsible for the binding of ligands. In fact, this subunit includes a Cys-loop in the first extracellular domain that is required for agonist binding2. The other subunits responsible for making up the active receptor are the β (β1-4), γ, δ and ε subunits3. Structurally, all subunits have the following: a conserved large extracellular N-terminal domain, 3 conserved transmembrane domains, a variable cytoplasmic loop and a fourth transmembrane domain with a short extracellular C-terminal domain. An active nAChR is generally a heteropentamer (homopentamers also exist) of these various subunits organized around a central pore1.
All α subunits are expressed in neuronal cells except for the α1 subunit which is specifically expressed in skeletal muscle. Indeed, two different nAChR structural entities with the following stoichiometry are observed in this tissue: (α1)2β1δγ in fetal muscle cells and (α1)2β1δε at mature neuromuscular synapses3.
The α1 extracellular domain contains the main immunogenic region, a region against which a large fraction of autoantibodies against nAChR is directed in the autoimmune disease myasthenia gravis (MG)4. This autoimmune disease is characterized by the malfunction of neuromuscular transmission as a result of nonfunctional nAChRs, leading to defective signaling at the neuromuscular junction5.
Due to its central role in muscle contraction and autonomic nervous system, nAChRs have evolved to be important targets of toxins secreted by plants, insects and animals. One prominent toxin affecting α1, in addition to other subunits, is α-bungarotoxin, a snake toxin which blocks nAChRs6.
Species reactivity key:
Anti-Nicotinic Acetylcholine Receptor α1 (CHRNA1) (extracellular) Antibody (#ANC-001) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot analysis. The antibody recognizes an extracellular epitope and is thus ideal for detecting the receptor in living cells. It has been designed to recognize nAChRα1 from mouse, rat, and human samples.
- Human HK-2 cells.
Kim, C.S. et al. (2016) PLoS ONE 11, e0152591.
- Anti-Nicotinic Acetylcholine Receptor α2 (CHRNA2) (extracellular) Antibody (#ANC-002)
- Anti-Nicotinic Acetylcholine Receptor α3 (CHRNA3) (extracellular) Antibody (#ANC-003)
- Anti-Nicotinic Acetylcholine Receptor α7 (CHRNA7) (extracellular) Antibody (#ANC-007)
- Anti-Nicotinic Acetylcholine Receptor α10 (CHRNA10) Antibody (#ANC-010)