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PhosphoSolutions/Nicotinic Acetylcholine Receptor (nAChR) β2 Antibody/1470-nACB2/100 µl

Rabbit Polyclonal Antibody

Pooled Serum
Size:
100 µl
Formulation:
Affinity Purified from Pooled Serum
Specificity:
Mouse, Rat
Applications:
WB 1:1000
Species:
Rabbit
Molecular Reference:
~52 kDa
Cite This Antibody:
PhosphoSolutions Cat# 1470-nACB2, RRID:AB_2619712
Antigen/Purification: ExpandCollapse

The antigen is a fusion protein from the cytoplasmic loop of the β2-subunit of rat nAChR.

The antibody is prepared from pooled rabbit serum by affinity purification using a column to which the fusion protein immunogen was coupled.

Biological Significance: ExpandCollapse

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).

Storage

100 µl in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

For long term storage –20° C is recommended. Stable at –20° C for at least 1 year.

General References

Scholze, P., Ciuraszkiewicz, A., Groessl, F., Orr‐Urtreger, A., McIntosh, J. M., & Huck, S. (2011). α4β2 nicotinic acetylcholine receptors in the early postnatal mouse superior cervical ganglion. Developmental neurobiology, 71(5), 390-399.

McGehee, D. S., & Role, L. W. (1995). Physiological diversity of nicotinic acetylcholine receptors expressed by vertebrate neurons. Annual review of physiology, 57(1), 521-546.

Albuquerque, E. X., Pereira, E. F., Alkondon, M., & Rogers, S. W. (2009). Mammalian nicotinic acetylcholine receptors: from structure to function. Physiological reviews, 89(1), 73-120.

Zoli, M., Léna, C., Picciotto, M. R., & Changeux, J. P. (1998). Identification of four classes of brain nicotinic receptors using β2 mutant mice. The Journal of neuroscience, 18(12), 4461-4472.

Champtiaux, N., & 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, 233-251.