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GluR1 is a subunit of the AMPA ionotropic glutamate receptor, which is responsible for fast excitatory synaptic transmission in the CNS.1 AMPA receptors are composed of four subunits, GluR1, GluR2, GluR3, and GluR4, which combine into heterotetramers to form a cation-permeable pore in the plasma membrane. Each subunit has two isoforms with the primary isoform designated as flip and a second isoform generated through alternative splicing designated as flop.2,3 The GluR1 flip and flop isoforms do not affect desensitization or channel opening and closing kinetics.3 GluR1 can be phosphorylated by PKA at serine 845 (Ser845), which increases the peak open probability of the ion channel, and dephosphorylation is required for AMPA receptor endocytosis.1 GluR1 (phospho-Ser845) levels increase in the ventromedial prefrontal cortex (vmPFC) and nucleus accumbens (NAc) following cocaine-cue extinction.4 Levels of GluR1 (phospho-Ser845) are reduced following NMDA receptor activation in rat hippocampal slices and by amyloid-β (Aβ) oligomers in primary mouse neurons.5,6 Cayman’s GluR1 (Phospho-Ser845) Rabbit Monoclonal Antibody (Clone RM296) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Control of GluR1 AMPA receptor function by cAMP-
2. Flip and flop: A cell-
3. Flip and flop: A molecular determinant for AMPA receptor channel opening. Biochemistry 48(17), 3767-3777 (2009).
4. Alterations in expression and phosphorylation of GluA1 receptors following cocaine-
5. Differential regulation of AMPA receptor GluA1 phosphorylation at serine 831 and 845 associated with activation of NMDA receptor subpopulations. Neurosci. Lett. 497(2), 94-98 (2011).
6. Soluble oligomers of amyloid-