Description
Product Characteristics:
GAD-65 and GAD-67, glutamate decarboxylases, function to catalyze the production of GABA (g-aminobutyric acid). In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl-conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA) and metabotropic (GABAB) receptors as well as a third class of receptors called GABAC. Both GABAA and GABAC are ligand-gated ion channels, however, they are structurally and functionally distinct. Members of the GABAA receptor family include GABAA R alpha 1-6, GABAA R beta 1-3, GABAA R©1-3, GABAA R∂, GABAA R gamma, GABAA R delta 1 and GABAA R delta 2. The GABAB family is composed of GABAB R1 alpha and GABAB R1 beta. GABA transporters have also been identified and include GABA T-1, GABA T-2 and GABA T-3 (also designated GAT-1, -2 and -3). The GABA transporters function to terminate GABA action.
Subcellular location: Cell membrane
Synonyms: GABA A Receptor beta 1 phospho S434, GARB1 Ser 434, GABAA receptor subunit beta-1, GABA-A receptor, beta-1 polypeptide, Gabrb-1, Gamma Aminobutyric Acid A Receptor Beta 1, Gamma Aminobutyric Acid Receptor, beta-1, Gamma-aminobutyric acid GABA A receptor, subunit beta 1, Gamma-aminobutyric acid receptor subunit beta-1, GARB1, GABRA1, AW061132, B230208N19Rik, GABAA receptor beta 1, GABAA receptor subunit beta-1, GABA-A receptor, beta-1 polypeptide, Gabrb-1, GABRB1, Gamma aminobutyric acid GABA A receptor beta 1, Gamma Aminobutyric Acid A Receptor Beta 1, Gamma Aminobutyric Acid Receptor, beta-1, Gamma-aminobutyric acid GABA A receptor, subunit beta 1, Gamma-aminobutyric acid receptor subunit beta-1, GARB1, GBRB1_HUMAN.
Target Information: Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine (By similarity). Functions as receptor for diazepines and various anesthetics, such as pentobarbital, these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel. {ECO:0000250, ECO:0000269:PubMed:20400944}