Product Pathways - Neuroscience
AMPA Receptor (GluR 2) (D39F2) Rabbit mAb #5306
|W||H M R||Endogenous||100||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
AMPA Receptor (GluR 2) (D39F2) Rabbit mAb detects endogenous levels of total GluR 2 protein. The antibody is not predicted to recognize other AMPA receptor subunits (e.g. GluR 1, GluR 3 or GluR 4) based on sequence homology of the antigen.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human GluR 2 protein.
AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainite-, 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 CNS. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). AMPARs that lack GluR 2 are permeable to calcium, in contrast to GluR 2-containing AMPARs (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).
- Palmer, C.L. et al. (2005) Pharmacol Rev 57, 253-77.
- Cull-Candy, S. et al. (2006) Curr Opin Neurobiol 16, 288-97.
- Hayashi, T. and Huganir, R.L. (2004) J Neurosci 24, 6152-60.
- Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
- Ballif, B.A. et al. (2008) J Proteome Res 7, 311-8.
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For Research Use Only. Not For Use In Diagnostic Procedures.