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Mouse Anti-GRIA1 Recombinant Antibody (S355-1) (CBMAB-G0771-LY)

This product is antibody recognizes GRIA1. The antibody S355-1 immunoassay techniques such as: WB.
See all GRIA1 antibodies
Published Data
Fig.1 Plantar incision increases the surface delivery of AMPA receptor subunit GluR1, but not GluR2, in the dorsal horn.
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Fig.2 Colocalization of stargazin and GluR1 in rat dorsal horn.
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Fig.3 Interaction between stargazin and GluR1 subunit in the ipsilateral dorsal horn is enhanced at 3 h after plantar incision.
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Fig.4 Intrathecal pretreatment of rats with small interfering RNA (siRNA)311 inhibits the enhanced surface delivery of GluR1 after plantar incision.
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Summary

Host Animal
Mouse
Specificity
Rat, Mouse
Clone
S355-1
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
Fusion protein amino acids 1-389 (extracellular N-terminus) of rat GluA1/GluR1, accession number P19490
Specificity
Rat, Mouse
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
50% glycerol
Preservative
0.1% sodium azide
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Glutamate Ionotropic Receptor AMPA Type Subunit 1
Introduction
Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. These receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The classification of glutamate receptors is based on their activation by different pharmacologic agonists. This gene belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
Entrez Gene ID
Mouse14799
Rat50592
UniProt ID
MouseP23818
RatP19490
Alternative Names
GluA1; gluR-A
Function
Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.
Biological Process
Cellular response to ammonium ion Source: Ensembl
Chemical synaptic transmission Source: ProtInc
Long-term memory Source: Ensembl
Long-term synaptic depression Source: Ensembl
Receptor internalization Source: Ensembl
Signal transduction Source: ProtInc
Cellular Location
Cell membrane; Postsynaptic cell membrane; Postsynaptic density membrane; Endoplasmic reticulum membrane; Early endosome membrane; Recycling endosome membrane; Dendrite; Dendritic spine. Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. Colocalizes with PDLIM4 in early endosomes. Displays a somatodendritic localization and is excluded from axons in neurons (By similarity). Localized to cone photoreceptor pedicles (By similarity).
Topology
Extracellular: 19-536
Helical: 537-557
Cytoplasmic: 558-584
Helical: 585-600
Extracellular: 601-603
Helical: 604-609
Cytoplasmic: 610-630
Helical: 631-805
Extracellular: 806-826
Helical: 827-906
PTM
Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-603 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).
Phosphorylated at Ser-645. Phosphorylated at Ser-710 by PKC. Phosphorylated at Ser-849 by PKC, PKA and CAMK2. Phosphorylated at Ser-863 by PKC, PKA and PRKG2 (By similarity). Phosphorylation of Ser-863 is reduced by induction of long-term depression and increased by induction of long-term potentiation (By similarity).

Ismail, V., Zachariassen, L. G., Godwin, A., Sahakian, M., Ellard, S., Stals, K. L., ... & Baralle, D. (2022). Identification and functional evaluation of GRIA1 missense and truncation variants in individuals with ID: An emerging neurodevelopmental syndrome. The American Journal of Human Genetics, 109(7), 1217-1241.

Asthana, P., Kumar, G., Milanowski, L. M., Au, N. P. B., Chan, S. C., Huang, J., ... & Ma, C. H. E. (2022). Cerebellar glutamatergic system impacts spontaneous motor recovery by regulating Gria1 expression. npj Regenerative Medicine, 7(1), 45.

Kim, J. E., Lee, D. S., Park, H., Kim, T. H., & Kang, T. C. (2021). AMPA receptor antagonists facilitate NEDD4-2-mediated GRIA1 ubiquitination by regulating PP2B-ERK1/2-SGK1 pathway in chronic epilepsy rats. Biomedicines, 9(8), 1069.

Kim, J. E., Lee, D. S., Park, H., Kim, T. H., & Kang, T. C. (2021). Inhibition of AKT/GSK3β/CREB pathway improves the responsiveness to AMPA receptor antagonists by regulating GRIA1 surface expression in chronic epilepsy rats. Biomedicines, 9(4), 425.

Ang, G., Brown, L. A., Tam, S. K., Davies, K. E., Foster, R. G., Harrison, P. J., ... & Peirson, S. N. (2021). Deletion of AMPA receptor GluA1 subunit gene (Gria1) causes circadian rhythm disruption and aberrant responses to environmental cues. Translational Psychiatry, 11(1), 588.

Kochetova, O. V., Avzaletdinova, D. S., Korytina, G. F., Morugova, T. V., & Mustafina, O. E. (2020). The association between eating behavior and polymorphisms in GRIN2B, GRIK3, GRIA1 and GRIN1 genes in people with type 2 diabetes mellitus. Molecular Biology Reports, 47(3), 2035-2046.

Bygrave, A. M., Jahans-Price, T., Wolff, A. R., Sprengel, R., Kullmann, D. M., Bannerman, D. M., & Kätzel, D. (2019). Hippocampal–prefrontal coherence mediates working memory and selective attention at distinct frequency bands and provides a causal link between schizophrenia and its risk gene GRIA1. Translational psychiatry, 9(1), 142.

Aitta-Aho, T., Maksimovic, M., Dahl, K., Sprengel, R., & Korpi, E. R. (2019). Attenuation of novelty-induced hyperactivity of gria1-/-mice by Cannabidiol and hippocampal inhibitory Chemogenetics. Frontiers in pharmacology, 10, 309.

Parekh, P. K., Becker-Krail, D., Sundaravelu, P., Ishigaki, S., Okado, H., Sobue, G., ... & McClung, C. A. (2018). Altered GluA1 (Gria1) function and accumbal synaptic plasticity in the ClockΔ19 model of bipolar mania. Biological psychiatry, 84(11), 817-826.

Ang, G., McKillop, L. E., Purple, R., Blanco-Duque, C., Peirson, S. N., Foster, R. G., ... & Vyazovskiy, V. V. (2018). Absent sleep EEG spindle activity in GluA1 (Gria1) knockout mice: relevance to neuropsychiatric disorders. Translational Psychiatry, 8(1), 154.

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For research use only. Not intended for any clinical use.

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