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Phospho-Ser831 GluR1 Antibody

Affinity purified rabbit polyclonal antibody

  • WB - Phospho-Ser831 GluR1 Antibody AN1013
    Western blot of rat hippocampal lysate showing specific immunolabeling of the ~100k GluR1 protein phosphorylated at Ser831 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: λ-Ptase). The blot is identical to the control except that it was incubated in λ-Ptase (1200 units for 30 min) before being exposed to the GluR1 Ser831 antibody. The immunolabeling is completely eliminated by treatment with λ-Ptase.
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession P19490
Reactivity Rat
Predicted Chicken, Human, Mouse
Host Rabbit
Clonality polyclonal
Calculated MW 100 KDa
Additional Information
Gene ID 50592
Gene Name GRIA1
Other Names Glutamate receptor 1, GluR-1, AMPA-selective glutamate receptor 1, GluR-A, GluR-K1, Glutamate receptor ionotropic, AMPA 1, GluA1, Gria1, Glur1
Target/Specificity Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser831 conjugated to KLH.
Dilution WB~~ 1:1000
Format Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.
Antibody Specificity Specific for the ~100k GluR1 protein phosphorylated at Ser831. Immunolabeling is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide. Immunolabeling is completely eliminated by λ-phosphatase treatment.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPhospho-Ser831 GluR1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
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Research Areas
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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 GluR1 subunit is widely expressed throughout the nervous system. GluR1 is potentiated by phosphorylation at Ser831 which has been shown to be mediated by either PKC or CaM kinase II (McGlade-McCulloh et al., 1993; Mammen et al., 1999; Roche et al., 1996). In addition, phosphorylation of this site has been linked to synaptic plasticity as well s learning and memory (Soderling and Derkach, 2000).


Hollmann M, Heinemann S (1994) Cloned glutamate receptors. Annu Rev Neurosci 17:31-108.
Keinänen K, Wisden W, Sommer B, Werner P, Herb A, Verdoorn TA, Sakmann B, Seeburg PH (1990) A family of AMPA-selective glutamate receptors. Science 249:556-560.
Mammen AL, Kameyama K, Roche KW, Huganir RL (1999) Phosphorylation of the a-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II. J Biol Chem 272:32528-32533.
McGlade-McCulloh E, Yamamoto H, Tan S-E, Brickey DA, Soderling TR (1993) Phosphorylation and regulation of glutamate receptors by calcium/calmodulin-dependent protein kinase II. Nature (London) 362:640-642.
Roche KW, O'Brien RJ, Mammen AL, Bernhardt J, Huganir RL (1996) Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron 16:1179-1188.
Soderling TR, Derkach VA (2000) Postsynaptic protein phosphorylation and LTP. Trends Neurosci 23:75-80.
Yuxia Jiao, Nidhi Jalan-Sakrikar, A. J. Robison, Anthony J. Baucum, II, Martha A. Bass, and Roger J. Colbran (2011) Characterization of a Central Ca2+/Calmodulin-dependent Protein Kinase IIα/β Binding Domain in Densin That Selectively Modulates Glutamate Receptor Subunit Phosphorylation J. Biol. Chem. 286: 24806 - 24818.
Robert M. Sears, Rong-Jian Liu, Nandakumar S. Narayanan, Ruth Sharf, Mark F. Yeckel, Mark Laubach, George K. Aghajanian, and Ralph J. DiLeone (2010) Regulation of Nucleus Accumbens Activity by the Hypothalamic Neuropeptide Melanin-Concentrating Hormone J. Neurosci., 30: 8263 - 8273.
Steven J. Coultrap, Isabelle Buard, Jaqueline R. Kulbe, Mark L. Dell'Acqua, and K. Ulrich Bayer (2010) CaMKII Autonomy Is Substrate-dependent and Further Stimulated by Ca2+/Calmodulin J. Biol. Chem., 285: 17930 – 1793.
Kurtis D. Davies, Susan M. Goebel-Goody, Steven J. Coultrap, and Michael D. Browning (2008) Long Term Synaptic Depression That Is Associated with GluR1 Dephosphorylation but Not -Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Internalization J. Biol. Chem., 283: 33138 - 33146.
Sergio Leal-Ortiz, Clarissa L. Waites, Ryan Terry-Lorenzo, Pedro Zamorano, Eckart D. Gundelfinger, and Craig C. Garner (2008) Piccolo modulation of Synapsin1a dynamics regulates synaptic vesicle exocytosis. J. Cell Biol., 181: 831 - 846.

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$ 335.00
Cat# AN1013
(40 western blots)
Availability: 7-10 days
Bulk Size
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