GABA A Receptor alpha 6 Antibody

Gamma-aminobutyric acid (GABA) is the primary inhibitory neurotransmitter in the central nervous system, causing a hyperpolarization of the membrane through the opening of a Cl- channel associated with the GABAA-Receptor (GABAA-R) subtype. GABAA-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 GABAA-R is a multimeric subunit complex. To date six alphas, four betas and four gammas, plus alternative splicing variants of some of these subunits, have been identified. Injection in oocytes or mammalian cell lines of cRNA coding for alpha and beta subunits results in the expression of functional GABAA-Rs sensitive to GABA. However, coexpression of a gamma subunit is required for benzodiazepine modulation. The various effects of the benzodiazepines in brain may also be mediated via different alpha subunits of the receptor. Lastly, phosphorylation of beta subunits of the receptor has been shown to modulate GABAA-R function.

GABAA Receptor a6 (CT) polyclonal antibody was raised against a fusion protein with the amino acid sequence representing the cytosolic loop of rat GABAA-R a6 Subunit.

For long term storage –80˚ C is recommended, but shorter term storage at –20˚ C is also acceptable as aliquots may be taken without freeze/thawing due to the presence of 50% glycerol. Stable for one year.

GABAA Receptor antibody is specific for the 56 to 57k GABAA-R α6-Subunit in rat brain membrane fractions. Rabbit anti-GABAA Receptor α6 (CT) does not recognize any other GABAA-R subunits as reactivity is eliminated in α6 knockout brain. Antibody dilutions and tissue load should be based on tissue type and expected expression level. Initial recommended range of dilutions: 1:1000 to 1:2000. Recognizes bovine, human, mouse and rat GABAA-R-α6-subunit. Applications include Dot Blots (DB) and Western Blot (WB) . Suitability for Immunohistochemistry (IHC) not yet determined. When internally tested under ideal conditions the working dilutions were 1:1000 for DB and WB.

Kittler, J.T., McAinsh, K., Moss, S.J. "Mechanisms of GABA A receptor assembly and trafficking - Implications for the modulation of inhibitory neurotransmission, " Mol. Neurobiol 26 (2002) 2251 - 268.

Bencsits, E., Ebert, V., Tretter, V., and Sieghart, W. "A significant part of native γ-aminobutyric acidA receptors containing α4-subunits do not contain γ- or δ-subunits. J. Biol. Chem. 274 (1999), 19,613-19,616.

Whiting, P.J., McKernan, R.M., Wafford, K.A. "Structure and pharmacology of vertebrate, GABAA receptor subtypes." In: International Review of Neurobiology (Bradley, R.J., Harris R.A., eds.), pp 95. San Diego: Academic Press (1995) .