Detection of Phospho-GluR1 (S831) by Western Blot.
Western blot of rat hippocampal lysate showing specific immunolabeling of the ~100 kDa GluR1 protein phosphorylated at S831 (Control). The phosphospecificity of this labeling is demonstrated by treatment with 1200 U of lambda Phosphatase ( lambda -PPase) for 30 minutes before being exposed to the Anti-Phospho-GluR1 (S831). The immunolabeling is completely eliminated by treatment with lambda -PPase.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
For long-term storage, ≤ -20° C is recommended. Product is stable at ≤ -20° C for at least 1 year.
Rat GluR1 is a 907 amino acid, 4-transmembrane protein that belongs to the glutamate-gated ion channel family. It is one of four AMPA receptor subunits that form a functional heterotetrameric glutamate receptor. GluR1 only interacts with GluR2. GluR1 has two key serine residues in the C-terminal extracellular region. Serine 831 is constitutively unphosphorylated. Upon exposure to a neurotransmitter, it is phosphorylated by CaMKII leading to a potentiation of glutamate-mediated current. Serine 845 is constitutively phosphorylated by Protein Kinase A (PKA). The presence of the phosphate insures membrane localization of the subunit. Following NMDA receptor activation, S845 is dephosphorylated with subsequent subunit internalization.
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