Nicotinic Acetylcholine Receptor alpha 4 (extracellular Antibody
Affinity purified polyclonal antibody
|Reactivity||Human, Mouse, Rat|
|Calculated MW||69957 Da|
|Homology||Rat, mouse - 12/13 amino acid residues identical.|
|Other Names||Neuronal acetylcholine receptor subunit alpha-4, CHRNA4, NACRA4|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)DLVNMHSRVDQLD, corresponding to amino acid residues 190-202 of human nAChR־±4 (Accession P43681). Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.|
|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 water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
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. These channel receptors are usually non-selective cation channels activated upon ligand binding which ultimately leads to the depolarization of postsynaptic cell membranes. To date, 17 different but related subunits of nAChRs have been identified and cloned. They consist of a 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. They are also expressed in non-neuronal cells such as bronchial epithelial cells4, as well lymphocytes5. The diversity of these receptors and their functional organization gives rise to unique properties and functions. The α4β2 receptor composition makes up a high affinity nicotinic receptor. In fact, its upregulation (mainly expressed by the increase of functional receptors at the membrane and not expression per se) is responsible for the increased appearance of binding sites following nicotine administration1,3. Animal studies have shown that nAChR-related mechanisms are involved in attention function6. Indeed α4β2 nAChR seems to also be involved in attention-deficit hyperactivity disorder (ADHD), a disease distinguished by a lack of attention, distractibility and hyperactivity3. The α4β2 and α7 nAChRs appear to be critical in rats for attention and working memory. Also, a α4β2 specific agonist was shown to reduce impulsivity, hyperactivity and attention deficits in adults with ADHD7. This same receptor subtype may also be involved in Parkinson’s disease (PD) as smoking and α4β2 nAChR agonists show beneficial effects in PD8,9. Abgent is pleased to offer a highly specific antibody directed against an epitope located at the extracellular N-terminal domain of human Nicotinic Acetylcholine Receptor α4 (nAChRα4). Anti-Nicotinic Acetylcholine Receptor α4 (extracellular) antibody (#AG1200) can be used in western blot, immunohistochemical and indirect flow cytometry applications. It has been designed to recognize nAChRα4 from mouse, rat and human samples.
References 1. Albuquerque, E.X. et al (2009) Physiol. Rev. 89, 73. 2. Karlin, A. et al. (1986) Ann. NY. Acad. Sci. 463, 53. 3. Kalamida, D. et al. (2007) FEBS J. 274, 3799. 4. Fu, X.W. et al. (2009) Am. J. Respir. Mol. Biol. 41, 93. 5. De Rosa, M.J. et al. (2009) Life Sci. 85, 449. 6. Blonde, A. et al. (2000) Psychopharmacology (Berlin) 149, 293. 7. Wilens, T.E. et al. (1999) Am. J. Psychiatry 156, 1931. 8. Tanner, C.M. et al. (2002) Neurology 58, 581. 9. Schneider, J.S. et al. (1998) Ann. Neurol. 43, 311.
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