Our Anti-GluR2-subunit (Ser880) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects rat GluR2-subunit (Ser880) and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of rat brain lysate showing specific immunolabeling of the ~100 kDa GluR2 protein phosphorylated at Ser880 in the first lane (-). Phosphospecificity is shown in the second lane (+) where immunolabeling is blocked by preadsorption of the phosphopeptide used as the antigen, but not by the corresponding non-phosphopeptide (not shown).
The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR) while those activated by α-amino-3-hydroxy-5-methyl-4-isoxalone propionic acid (AMPA) are known as AMPA receptors (AMPAR). The AMPAR are comprised of four distinct glutamate receptor subunits designated (GluR1-4) and they play key roles in virtually all excitatory neurotransmission in the brain (Keinänen et al., 1990; Hollmann and Heinemann, 1994). The number of GluR2 subunits in the AMPA receptor complex affects the Ca2+ permeability, rectification and single-channel conductance of AMPA receptors. Ser-880 has been identified as the PKC phosphorylation site within the C-terminal region of GluR2 and has been shown to differentially regulate the interaction of the PDZ domain-containing proteins GRIP1 and PICK 1 (Matsuda et al., 1999)
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
WB
Rabbit
GRIA2
100 kDa
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser880 conjugated to keyhole limpet hemocyanin (KLH).
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from rabbit serum by affinity purification via sequential chromatography on phospho and non-phosphopeptide affinity columns.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
WB Brain: 1:1000
Unconjugated
Specific for endogenous levels of the ~100 kDa GluR2 protein phosphorylated at Ser880. Immunolabeling is blocked by preadsorption with the phosphopeptide used as antigen, but not by the corresponding non-phosphopeptide.
Phosphorylated
Ser880
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
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Mao, M., et al. 2018. Regulation of Phosphorylation of AMPA Glutamate Receptors by Muscarinic M4 Receptors in the Striatum In vivo. Neuroscience, 375, pp.84-93.
Lameth, J., et al. 2017. Acute Neuroinflammation Promotes Cell Responses to 1800 MHz GSM Electromagnetic Fields in the Rat Cerebral Cortex. Neurotoxicity Research, pp.1-16.
Singer, B.F., et al. 2016. Stimuli associated with the presence or absence of amphetamine regulate cytoskeletal signaling and behavior. European Neuropsychopharmacology, 26(11), pp.1836-1842.
O-Leary, H., et al. 2016. Enhanced long term potentiation and decreased AMPA receptor desensitization in the acute period following a single kainate induced early life seizure. Neurobiology of disease, 87, 134-144.
Mao, L.M., et al. 2015. Dynamic increases in AMPA receptor phosphorylation in the rat hippocampus in response to amphetamine. Journal of neurochemistry, 133(6), pp.795-805.
Xue, B., et al. 2015. Rapid and sustained GluA1 S845 phosphorylation in synaptic and extrasynaptic locations in the rat forebrain following amphetamine administration. Neurochemistry international, 64, pp.48-54.