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Peptide NVGNINNDKKDETYR(C), corresponding to amino acid residues 179-193 of rat GluR2 (Accession P19491). Extracellular, N-terminus.
Western blot analysis of rat brain membranes:1. Guinea pig Anti-GluR2 (GluA2) (extracellular) Antibody (#AGP-073), (1:500).
2. Guinea pig Anti-GluR2 (GluA2) (extracellular) Antibody, preincubated with the control peptide antigen.Western blot analysis of mouse brain lysate:1. Guinea pig Anti-GluR2 (GluA2) (extracellular) Antibody (#AGP-073), (1:600).
2. Guinea pig Anti-GluR2 (GluA2) (extracellular) Antibody, preincubated with the control peptide antigen.
Expression of GluA2 in rat PC12 cellsCell surface detection of GluA2 in live intact rat pheochromocytoma PC12 cells. A. Extracellular staining of cells using Guinea pig Anti-GluR2 (GluA2) (extracellular) Antibody (#AGP-073), (1:50) followed by goat anti-guinea pig-AlexaFluor-594 secondary antibody (red). B. Live image of the cells. C. Merge of A and B.
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 the amino acid arginine (R) at a critical site in the pore loop instead of 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 been focused on understanding the mechanisms that govern AMPA receptor trafficking.
Species reactivity key:
Alomone Labs is pleased to offer an antibody directed against an extracellular epitope of the rat ionotropic glutamate receptor 2. Guinea pig Anti-GluR2 (GluA2) (extracellular) Antibody (#AGP-073) raised in guinea pig can be used in western blot and live cell imaging applications. It has been designed to recognize GluR2 from human, mouse and rat samples. The antigen used to immunize guinea pigs is the same as Anti-GluR2 (GluA2) (extracellular) Antibody (#AGC-005) raised in rabbit. Our line of guinea pig antibodies enables more flexibility with our products such as immuno-colocalization studies, immunoprecipitation, etc.
- Anti-GluR2 (GluA2) (extracellular)-ATTO-488 Antibody (#AGC-005-AG). A fluorescent labeled primary antibody. It can be used in immuno-colocalization studies in conjunction with any of our antibodies raised in rabbit.
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