Lyophilized Powder This product is freeze dried. All water molecules have been removed.
Antigen Incl. This antibody is shipped with its antigen FREE of charge!
- Peptide RTSDSRDHTRVDWKR(C), corresponding to amino acid residues 271-285 of rat GluR1 (Accession P19490). Extracellular, N-terminus.
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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 (#AGP-009), (1:200).
3,4. Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody, preincubated with the negative control antigen.
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Expression of GluR1 in rat hippocampusImmunohistochemical staining of perfusion-fixed frozen rat brain sections using Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGP-009), (1:400), followed by anti-rabbit-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).
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Immuno-colocalization 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 (#AGP-009), (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.
- 1. Dingledine, R. et al. (1999) Pharmacol. Rev. 51, 7.
- 2. Sheng, M. et al. (2001) Cell. 105, 825.
- 3. Song, I. et al. (2002) Trends. Neurosci. 25, 578.
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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.
Expression of GluR1 in mouse olfactory bulb.Immunohistochemical staining of mouse olfactory bulb sections using Guinea pig Anti-GluR1 (GluA1) (extracellular) Antibody (#AGP-009). 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.
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 (#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 immuno-colocalization studies, immunoprecipitation, etc.
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不知道能不能直接买到大鼠抗豚鼠血管IgG的ELISA试剂盒。
如果买不到这种试剂盒，用空白板的话（就是反应孔中没有抗原或者抗体包被），把自制的豚鼠血管抗原加到反应孔中进行孵育，能不能使抗原附着在孔壁上？这样的话就可以按照elisa的操作步骤进行大鼠血清检测了。
目前的设想是自制抗原，粉碎豚鼠的血管，制成悬液，通过反复多次的冻融，离心后收集上清液作为抗原（即豚鼠血管抗原）。
然后将抗原加入到elisa的反应孔中（这种是特制的空白板，就是反应孔中没有抗原或抗体包被）进行孵育，使豚鼠血管抗原附着在孔壁上，就是让反应孔充当固相载体，形成固相抗原。倒掉多余的抗原。
再加入待检测的大鼠血清，这样血清中的特异性抗豚鼠血管IgG就可以跟固相的抗原结合，形成固相抗原抗体复合物。
加入酶标的兔抗鼠或者羊抗鼠IgG,形成酶标的抗原抗体复合物。
然后就是一些显色步骤。
现在关键的问题就是抗原加入空白板，能不能形成固相抗原，如果不能跟孔壁附着的话，在后面洗涤的过程中就被洗掉了，那就没办法完成检测了。
请各位大侠给指条明路啊！！！小弟在此多谢了！！！
多谢！
