Our Anti-Nicotinic Acetylcholine Receptor (nAChR) β4 primary antibody from PhosphoSolutions is rabbit polyclonal. It detects mouse and rat Nicotinic Acetylcholine Receptor (nAChR) β4 and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of mouse habenula lysate showing specific immunolabeling of the ~52 kDa nAChRβ4 protein.
Nicotinic acetylcholine receptors (nAChRs) are ionotropic, cholinergic receptors that are divided into 2 types; muscle type and neuronal type. Neuronal nAChRs are pentameric ion channels consisting of 5 identical (homopentamers) or different (heteropentamers) subunits. Heteropentameric neuronal nAChRs mediate fast synaptic transmission in the autonomic nervous system. The predominant hetero-oligomeric nAChR in the CNS contain the subunits α4β2, whereas α3β4 prevail in the PNS. However, the expression of these subunits varies not only by region but also during development (Scholze et al 2011). In the brain, β2-containing receptors greatly outnumber receptors that contain β4 (McGehee & Role, 1995; Albuquerque, et al., 2009), and in most brain regions, targeted deletion of the β2 subunit virtually abolishes [3H]-epibatidine binding and receptor autoradiography (Zoli, et al., 1998) due to the absence of a β subunit required to form functional nAChRs (Champtiaux & Changeux, 2004).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
ELISA, WB
Rabbit
Chrnb4
52 kDa
Fusion protein from the cytoplasmic loop of the β4 subunit of mouse nAChR.
Mouse
Mouse, Rat
AB_2619714
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from pooled rabbit serum by affinity purification using a column to which the fusion protein antigen was coupled.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
WB Brain: 1:1000
Unconjugated
Specific for endogenous levels of the ~52 kDa nAChRβ4 protein.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Q8R493
UniProt Summary: Component of neuronal acetylcholine receptors (nAChRs) that function as pentameric, ligand-gated cation channels with high calcium permeability among other activities. nAChRs are excitatory neurotrasnmitter receptors formed by a collection of nAChR subunits known to mediate synaptic transmission in the nervous system and the neuromuscular junction. Each nAchR subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, cation permeability, and binding to allosteric modulators (PubMed:20881005, PubMed:31488329, PubMed:8663494, PubMed:8906617, PubMed:9203638). CHRNB4 forms heteropentameric neuronal acetylcholine receptors with CHRNA2, CHRNA3 and CHRNA4, as well as CHRNA5 and CHRNB3 as accesory subunits (PubMed:11118490, PubMed:20881005, PubMed:8663494). CHRNA3:CHRNB4 being predominant in neurons of the autonomic ganglia, it is known as ganglionic nicotinic receptor (PubMed:31488329). CHRNA3:CHRNB4 or CHRNA3:CHRNA5:CHRNB4 play also an important role in the habenulo-interpeduncular tract, modulating the mesolimbic dopamine system and affecting reward circuits and addiction (By similarity). Hypothalamic CHRNA3:CHRNB4 nAChR activation by nicotine leads to activation of POMC neurons and a decrease in food intake (By similarity). {ECO:0000250|UniProtKB:P12392, ECO:0000250|UniProtKB:Q8R493, ECO:0000269|PubMed:11118490, ECO:0000269|PubMed:20881005, ECO:0000269|PubMed:31488329, ECO:0000269|PubMed:8663494, ECO:0000269|PubMed:8906617, ECO:0000269|PubMed:9203638}.
Scholze, P., Ciuraszkiewicz, A., Groessl, F., Orr‐Urtreger, A., McIntosh, J.M. and Huck, S., 2011. α4β2 nicotinic acetylcholine receptors in the early postnatal mouse superior cervical ganglion. Developmental Neurobiology, 71(5), pp.390-399. PMID: 10814726
McGehee, D.S. and Role, L.W., 1995. Physiological diversity of nicotinic acetylcholine receptors expressed by vertebrate neurons. Annual Review of Physiology, 57(1), pp.521-546. PMID: 10814726
Albuquerque, E.X., Pereira, E.F., Alkondon, M. and Rogers, S.W., 2009. Mammalian nicotinic acetylcholine receptors: from structure to function. Physiological Reviews, 89(1), pp.73-120. PMID: 10814726
Zoli, M., Léna, C., Picciotto, M.R. and Changeux, J.P., 1998. Identification of four classes of brain nicotinic receptors using β2 mutant mice. Journal of Neuroscience, 18(12), pp.4461-4472. PMID: 10814726
Champtiaux, N. and Changeux, J.P., 2004. Knockout and knockin mice to investigate the role of nicotinic receptors in the central nervous system. Progress in Brain Research, 145, pp.233-251. PMID: 10814726
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