Nicotinic Acetylcholine Receptor beta1 (extracellular) Antibody
Affinity purified polyclonal antibody
|Reactivity||Human, Mouse, Rat|
|Calculated MW||57027 Da|
|Homology||Mouse, human - identical.|
|Other Names||Acetylcholine receptor subunit beta, Chrnb1, Acrb|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)EKDEEMSTKVYLD, corresponding to amino acid residues 68-80 of rat nAChR־²1 (Accession P25109). Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||25 µl, 50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl DDW.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||2 µg peptide per 1 µg antibody.|
|Formulation||Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
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Provided below are standard protocols that you may find useful for product applications.
Neuronal nicotinic acetylcholine receptors (nAChRs) belong to the superfamily of ligand-gated ion channels and are widely expressed throughout the central and peripheral nervous systems. nAChRs play crucial roles in modulating a wide range of higher cognitive functions by mediating presynaptic, postsynaptic, and extrasynaptic signaling1. nAChRs are formed by the assembly of five transmembrane subunits, selected from a pool of 17 homologous polypeptides (α1-10, β1-4, γ, δ, and ε). There are many nAChR subtypes, each consisting of a specific combination of subunits, which mediate diverse physiological functions. They are widely expressed in the central nervous system, while, in the periphery, they mediate synaptic transmission at the neuromuscular junction and ganglia. nAChRs are also found in non-neuronal/non-muscle cells (keratinocytes, epithelia, macrophages, etc. )2. 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 of these various subunits organized around a central pore3. While most β subunits are neuronal, the β1 subunit forms functional receptors along with other subunits in the muscle2. β1 subunit seems to be involved in myasthenia gravis (MG)4, an acquired autoimmune disease usually characterized by the presence of circulating autoantibodies that bind to and destroy muscle nAChRs5.
References 1. Betz, H. et al. (1990) Neuron 5, 383. 2. Kalamida, D. et al. (2007) FEBS J. 274, 3799. 3. Albuquerque, E.X. et al. (2009) Physiol. Rev. 89, 73. 4. Lindstrom, J. (1997) Mol. Neurobiol. 15, 193. 5. Kostelidou, K. et al. (2006) FEBS J. 273, 3557.
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