Anti-Recombinant-Phospho-GRIA1/GluR-1-Ser845 antibody [RM1W10] (STJA0024588)

SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
STJA0024588
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General Information

Short DescriptionRabbit monoclonal anti-Recombinant-Phospho-Glutamate Receptor 1-Ser845 for use in WB in Human and Rat samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsWB
HostRabbit
ReactivityHuman/Rat
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityMonoclonal
Clone IDRM1W10
IsotypeIgG
ConjugationUnconjugated
PurificationProtein A/G purified from cell culture supernatant
Dilution RangeWB: 1:500-1:1000
Formulation0.01M PBS
Storage InstructionSuitable for storage at +4°C between 1-2 weeks. For longer term store at-20°C for up to 12 months.

Target Information

Gene SymbolGRIA1
Gene ID2890
Uniprot IDGRIA1_HUMAN

Additional Info

Post Translational Modifications Palmitoylated. Depalmitoylated by CPT1C and upon L-glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-603, which 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. 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. Phosphorylation of Ser-863 is reduced by induction of long-term depression and increased by induction of long-term potentiation.
Function Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid. 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 upon entry of monovalent and divalent cations such as sodium and calcium. The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG2 or CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate. Resensitization is blocked by CNIH2 through interaction with CACNG8 in the CACNG8-containing AMPA receptors complex. Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable. Also permeable to other divalents cations such as strontium(2+) and magnesium(2+) and monovalent cations such as potassium(1+) and lithium(1+).
Protein Name Glutamate Receptor 1
Glur-1
Ampa-Selective Glutamate Receptor 1
Glur-A
Glur-K1
Glutamate Receptor Ionotropic - Ampa 1
Database Links Reactome: R-HSA-204005
Reactome: R-HSA-399710
Reactome: R-HSA-399719
Reactome: R-HSA-416993
Reactome: R-HSA-438066
Reactome: R-HSA-5694530
Reactome: R-HSA-8849932
Reactome: R-HSA-9620244
Cellular Localisation Cell Membrane
Multi-Pass Membrane Protein
Endoplasmic Reticulum Membrane
Postsynaptic Cell Membrane
Postsynaptic Density Membrane
Cell Projection
Dendrite
Dendritic Spine
Early Endosome Membrane
Recycling Endosome Membrane
Presynapse
Synapse
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
Localized To Cone Photoreceptor Pedicles
Alternative Antibody Names Anti-Glutamate Receptor 1 antibody
Anti-Glur-1 antibody
Anti-Ampa-Selective Glutamate Receptor 1 antibody
Anti-Glur-A antibody
Anti-Glur-K1 antibody
Anti-Glutamate Receptor Ionotropic - Ampa 1 antibody
Anti-GRIA1 antibody
Anti-GLUA1 antibody
Anti-GLUH1 antibody
Anti-GLUR1 antibody

Information sourced from Uniprot.org

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