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The GluR1 (lonotropic Glutamate Receptor1) Antibody was raised against a C-terminal synthetic peptide sequence corresponding to amino acids 894-907 of rat GluR1 coupled to bovine thyroglobulin with gluraraldehyde. The antibody produces strong labeling of GluR1 at dilutions of 1/4,000 - 1/6,000 using biotin-streptavidin peroxidase technique in rat cortex and hippocampus. Western blot analysis of GluR1 transfected cells and rat brain homogenates the antibody specifically labels a single band at Uapproximately 102 kD. Western blot analysis of GluR2, 3, 4, 4C, 5, 6, and 7 transfected cells revealed no immunolabeling. Immunolabeling of the above non-NMDA transfected cells demonstrates specificity for GluR1. Additionally, immunolabeling for GluR1 is completely abolished by pre-adsorption with synthetic rat GluR1 (894-907) at 5 µg per mL of diluted antibody.