A phospho-specific peptide corresponding to residues surrounding Serine 845 of human GluR1 was used as an immunogen. The antibody only detects GluR1 phosphorylated on Serine 845.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Glutamic acid is the major excitatory neurotransmitter in the mammalian central nervous system. Glutamate receptors are classified on the basis of their activation by different agonists (1-3). GluR1, human glutamate receptor type 1, is an integral membrane protein that is widely expressed in the human brain. The postsynaptic actions of glutamic acid are mediated by a variety of receptors that are named according to their selective agonists. GluR1 is known to bind a kainate subtype of agonist. It has been found that malfunctioning of the glutamatergic system may result in certain brain disorders and neurodegeneration (3). Phosphorylation of the GluR1 subunit on serine 845 by PKA is required for PKA-induced increases in ?-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor cell-surface expression because it promotes receptor insertion and decreases receptor endocytosis. Furthermore, dephosphorylation of GluR1 serine 845 triggers NMDA-induced AMPA receptor internalization (4).
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Western blot analysis on rat brain lysates using anti-Phospho-GluR1 (pS845), 1:20,000 dilution. Cells were either (A) untreated (B) treated with Lambda Phosphatase
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