Species predicted to react based on 100% sequence homology:Human, Mouse
Specificity / Sensitivity
Phospho-AMPA Receptor (GluR 2) (Tyr869/Tyr873/Tyr876) Antibody detects endogenous levels of GluR 2 only when phosphorylated at Tyr869, Tyr873 or Tyr876. It may also detect GluR 3 when phosphorylated at the conserved Tyr880, Tyr884 or Tyr887. These residues are not conserved in GluR 1 or GluR 4.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr869, Tyr873 and Tyr876 of human GluR 2. Antibodies are purified by protein A and peptide affinity chromatography.
Background
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. Activity changes of AMPARs are implicated 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. Phosphorylation of GluR2 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 (4).