Overview
- Peptide RTSDSRDHTRVDWKR(C), corresponding to amino acid residues 271-285 of rat GluR1 (Accession P19490). Extracellular, N-terminus.
Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain lysates:1,2. Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGC-004-GP), (1:200).
3,4. Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody, preincubated with GluR1/GluA1 (extracellular) Blocking Peptide (#BLP-GC004).
Expression of GluR1 in rat hippocampusImmunohistochemical staining of perfusion-fixed frozen rat brain sections using Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGC-004-GP), (1:400), followed by goat anti-guinea pig-Cy2 antibody (green). GluR1 staining appears in neuronal outlines (horizontal arrows) and in the inner molecular layer of the dentate gyrus (vertical arrow). Nuclei are stained with DAPI (blue).
Multiplex staining of GluR1 and PICK1 in rat hippocampus.Immunohistochemical staining of perfusion-fixed frozen rat brain sections with Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGC-004-GP), (1:400), followed by goat anti-guinea pig-AlexaFluor-488 and Anti-PICK1 Antibody (#APZ-014), (1:400), followed by donkey anti-rabbit-Cy3. A. GluR1 immunoreactivity (green) appears in several interneurons (arrows). B. PICK1 immunoreactivity (red) appears also in interneurons (arrows). C. Merge of the two images reveals co-localization in several interneurons (arrows) in the dentate gyrus (DG). Cell nuclei are stained with DAPI (blue).
Multiplex staining of GluR1 and Vesicular GABA Transporter in human U-87 MG cellsCell surface detection of GluR1 and Vesicular GABA Transporter in human glioblastoma U-87 MG. Extracellular staining of live intact cells with Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGC-004-GP), (1:25), followed by goat anti-guinea pig-AlexaFluor-488 secondary antibody (green). Cells were subsequently fixed, permeabilized and labeled with Anti-Vesicular GABA Transporter (VGAT) Antibody (#AGT-005), (1:200), followed by goat anti-rabbit-AlexaFluor-594 secondary antibody (red). Representative merged images of the double labeled cells are shown in A and B.
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AMPA receptors are members of the glutamate receptor family of ion channels that also include the NMDA and Kainate receptors. The three subfamilies are named after the original synthetic agonists that were identified as selective ligands of each family.
The α-amino-3-hydroxy-5-methyl-4-isoazolepropionic acid (AMPA) receptor subfamily includes four members AMPA1-AMPA4 that are also known as GluR1-GluR4 respectively.
The functional AMPA channel is believed to be a tetramer, with most neuronal AMPA receptors being actually heterotetramers composed of AMPA1 plus AMPA2 or AMPA2 plus AMPA3, although homotetramers can also be found.
AMPA receptors are permeable to cations Na+, K+ and Ca2+. The Ca2+ permeability is dependent on the presence of AMPA2: whenever this subunit is present, the channel will be impermeable to Ca2+. The Ca2+ permeability of the AMPA2 subunit is determined by the presence of an arginine (R) at a critical site in the pore loop instead of a glutamine (Q) present in the same site in the other AMPA subunits. A post-transcriptional process known as RNA editing determines the presence of this R. Since most AMPA2 subunits in the adult brain have undergone RNA editing and most AMPA receptors contain the AMPA2 subunit, most native AMPA receptors will be impermeable to Ca2+.
Gating of AMPA receptors by glutamate is extremely fast and therefore the AMPA receptors mediate most excitatory (depolarizing) currents in the brain during basal neuronal activity. The depolarization caused by the activation of post-synaptic AMPA receptors is necessary for the activation of NMDA receptors that will open only in the presence of both glutamate and a depolarized membrane.
Synaptic strength, defined as the level of post-synaptic depolarization, can be long term (hence the term long term potentiation, LTP) and therefore induce changes in signaling and protein synthesis in the activated neuron. These changes are associated with memory formation and learning.
Changes in synaptic strength are thought to involve rapid movement of the AMPA receptors in and out of the synapses and a great deal of effort has focused in understanding the mechanisms that govern AMPA receptor trafficking.
Alomone Labs is pleased to offer an antibody against an extracellular epitope the rat ionotropic glutamate receptor 1. Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGC-004-GP, formerly AGP-009) raised in guinea pig can be used in western blot, immunohistochemistry and immunocytochemistry applications. It has been designed to recognize GluR1 from human, mouse and rat samples. The antigen used to immunize guinea pigs is the same as Anti-GluR1 (GluA1) (extracellular) Antibody (#AGC-004) raised in rabbit. Our line of guinea pig antibodies enables more flexibility with our products such as multiplex staining studies, immunoprecipitation, etc.
Expression of GluR1 in mouse olfactory bulb.Immunohistochemical staining of mouse olfactory bulb sections using Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGC-004-GP). GluR1 staining (green) is detected in the glomerular and external plexiform layers (EPL), (right panel). GluR1 co-localizes with GFAP in periglomerular astrocytes and their processes in the neuropil (merged panel).Adapted from Droste, D. et al. (2017) Sci. Rep. 7, 44817. with permission of Nature Publishing Group.
Applications
Citations
Powered by Bioz- Mouse brain sections.
Beiersdorfer, A. and Lohr, C. (2019) Front. Cell. Neurosci. 13, 451. - Mouse cerebellum and olfactory bulb sections (1:200).
Droste, D. et al. (2017) Sci. Rep. 7, 44817.
- Mouse brain sections.
Beiersdorfer, A. and Lohr, C. (2019) Front. Cell. Neurosci. 13, 451.
