Nicotinic Acetylcholine Receptor Alpha2 (extracellular) Antibody
Affinity purified polyclonal antibody
|Application ||WB, LCI|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||58611 Da|
|Homology||Mouse - identical; human - 12/13 amino acid residues identical.|
|Other Names||Neuronal acetylcholine receptor subunit alpha-2, Chrna2, Acra2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)DLEQMERTVDLKD, corresponding to amino acid residues 189-201 of rat nAChR־±2 (Accession P12389). 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. Resuspended 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.
Nicotinic Acetylcholine Receptors (nAChRs) mediate the physiological effects of exogenous nicotine. They also play critical physiological roles throughout the brain and body by mediating cholinergic excitatory neurotransmission, modulating the release of neurotransmitters, and have longer-term effects on gene expression and cellular connections1. nAChRs are pentameric complexes made up of combinations of a number of different nAChR subunits, which can be classified as α subunits, containing two cysteine residues at positions analogous to Cys192 and Cys193, and non-alpha subunits (‘structural’ subunits), which can be defined as β subunits when they are expressed in the vertebrate nervous system2. There are nine α subunits (α2–α10) and three β subunits (β2, β3, and β4) in the CNS3. Nicotinic receptors are assembled as combinations of α (2-6) and and β (2-4) subunits. All α subunits are expressed in neuronal cells except for the α1 subunit which is specifically expressed in skeletal muscle. They are also expressed in non-neuronal cells such as bronchial epithelial cells4, as well lymphocytes5. In humans, a mutant α2 subunit has been identified, which forms nAChRs with increased agonist sensitivity and causes a form of familial epilepsy6. Further, an α2 subunit null mouse model has been used to demonstrate a role for α2 nAChR in nicotine-induced modulation of long-term potentiation in the mouse hippocampal CA1 region, which may underlie some of the cognitive effects of nicotine7.
References 1. Jensen, A.A. et al. (2005) J. Med. Chem. 48, 4705. 2. Millar, N.S. and Harkness, P.C. (2008) Mol. Membr. Biol. 25, 279. 3. Hogg, R.C. et al. (2003) Rev. Physiol. Biochem. Pharmacol. 147,1. 4. Fu, X.W. et al. (2009) Am. J. Respir. Cell. Mol. Biol. 41, 93. 5. De Rosa, M.J. et al. (2009) Life Sci. 85, 449. 6. Aridon, P. et al. (2006) Am. J. Human Genetics 79, 342. 7. Nakauchi, S. et al. (2007) Eur. J. Neurosci. 25, 2666.
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