GABAA Receptor γ2 (Ser327) Antibody

Gamma-aminobutyric acid (GABA) is the primary inhibitory neurotransmitter in the central nervous system. There are two major classes of GABA receptors: the GABA-A and the GABA-AB subtype of receptors. GABA-A-Rs are important therapeutic targets for a range of sedative, anxiolytic, and hypnotic agents and are implicated in several diseases including epilepsy, anxiety, depression, and substance abuse. The GABA-A-R is a multimeric subunit complex. To date six αs, four βs and four γs, plus alternative splicing variants of some of these subunits, have been identified (Olsen and Tobin, 1990; Whiting et al., 1999; Ogris et al., 2004) . Injection in oocytes or mammalian cell lines of cRNA coding for α- and β-subunits results in the expression of functional GABA-A-Rs sensitive to GABA. However, coexpression of a γ-subunit is required for benzodiazepine modulation. It has recently been suggested that PKCε regulates the sensitivity of GABA-A α1β2γ2 receptors to ethanol and benzodiazepines through phosphorylation of serine 327 in the large intracellular loop of γ2 (Qi et al., 2007)

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Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser327 of the γ2 subunit of rat GABAA receptor, conjugated to keyhole limpet hemocyanin (KLH) .

Specific for endogenous levels of the ~45 kDa GABAA receptor γ2 subunit phosphorylated at Ser327. Immunolabeling is blocked by preadsorption with the phosphopeptide used as antigen, but not by the corresponding non-phosphopeptide.