Product Pathways - Neuroscience
Phospho-AMPA Receptor (GluR 2) (Tyr876) Antibody #4027
|4027S||100 µl (10 western blots)||---||In Stock||---|
|4027||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Human, Mouse.
Specificity / Sensitivity
Phospho-AMPA Receptor (GluR 2) (Tyr876) Antibody detects endogenous levels of GluR 2 only when phosphorylated at Tyr876. It may also detect GluR 3 when phosphorylated at the conserved Tyr887. This residue is 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 Tyr876 of human GluR 2. Antibodies are purified by protein A and peptide affinity chromatography.
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 site at Tyr876 was also independently identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's MS/MS platform for phosphorylation site discovery. Phosphorylation of GluR at Tyr876 was observed in extracts isolated from ischemic rat brain.
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