Nicotinic Acetylcholine Receptor (nAChR) β4 Antibody

Applications

Reactivity

Mouse
Rat

Overview
Catalog #	bs-70178r-100ul
Product Name	Nicotinic Acetylcholine Receptor (nAChR) β4 Antibody
Applications	WB
Specificity	Specific for endogenous levels of the ~52 kDa nAChRβ4 protein.
Reactivity	Mouse, Rat
Specifications
Conjugation	Unconjugated
Host	Rabbit
Source	Fusion protein from the cytoplasmic loop of the β4 subunit of mouse nAChR.
Clonality	Polyclonal
Isotype	IgG
Concentration	Lot Dependent
Purification	Antigen Affinity purification from Pooled whole antiserum
Storage Buffer	10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
Storage Condition	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.
Target
Gene ID	108015
Swiss Prot	Q8R493
Synonyms	acetylcholine receptor nicotinic beta 4 (neuronal) antibody, ACHB4_HUMAN antibody, AChR antibody, Cholinergic receptor nicotinic beta 4 antibody, Cholinergic receptor nicotinic beta polypeptide 4 antibody, cholinergic receptor nicotinic beta polypeptide 4 antibody, Chrnb4 antibody, Neuronal acetylcholine receptor subunit beta-4 antibody, Neuronal nicotinic receptor beta 4 subunit antibody
Background	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).
Application Dilution
WB	1:300-5000