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Product Usage Information

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 μg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

AMPA Receptor 2 (GluA2) (D39F2) Rabbit mAb detects endogenous levels of total GluA2 protein. The antibody is not predicted to recognize other AMPA receptor subunits (e.g. GluA1, GluA3 or GluA4) based on sequence homology of the antigen.

Species Reactivity:

Human, Mouse, Rat

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human GluA2 protein.

Background

AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

Src family tyrosine kinases phosphorylate the GluR 2 subunit of AMPA receptors at Tyr876, which increases the interaction with GRIP1/2 but not PICK1. In addition, Tyr876 is important for AMPA- and NMDA-induced GluR 2 internalization (3). The phosphorylation sites at Tyr869, Tyr873 and Tyr876 were identified at Cell Signaling Technology (CST) using PhosphoScan^?, CST's MS/MS platform for phosphorylation site discovery (4). Phosphorylation of GluR 2 at Tyr869, Tyr873 and Tyr876 was observed in extracts isolated from ischemic rat brain. These sites were independently found in a large-scale identification of tyrosine phosphorylation sites from murine brain (5).

1. Palmer, C.L. et al. (2005) Pharmacol Rev 57, 253-77.
2. Cull-Candy, S. et al. (2006) Curr Opin Neurobiol 16, 288-97.
3. Hayashi, T. and Huganir, R.L. (2004) J Neurosci 24, 6152-60.
4. Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
5. Ballif, B.A. et al. (2008) J Proteome Res 7, 311-8.