|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||105373 Da|
|Other Names||Glutamate receptor ionotropic, NMDA 1, GluN1, Glutamate [NMDA] receptor subunit zeta-1, N-methyl-D-aspartate receptor subunit NR1, NMD-R1, GRIN1, NMDAR1|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding serine 889 of human NMDAR1 was used as an immunogen. This antibody detects NMDAR1 phosphorylated at serine 889.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NMDAR1 Antibody Phospho (pS889) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:7685113, PubMed:28126851, PubMed:26919761, PubMed:26875626, PubMed:28105280). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:26919761).|
|Cellular Location||Cell membrane; Multi- pass membrane protein. Cell junction, synapse, postsynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density Note=Enriched in postsynaptic plasma membrane and postsynaptic densities.|
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Provided below are standard protocols that you may find useful for product applications.
The NMDA (N-methyl D-aspartate) receptors in the brain play a critical role in synaptic plasticity, synaptogenesis and excitotoxicity. Molecular cloning has demonstrated that NMDA receptors consist of several homologous subunits (NMDAR1). A variety of studies have suggested that protein phosphorylation of NMDA receptors may regulate their function and play a role in many forms of synaptic plasticity such as long-term potentiation. PKC phosphorylation occurs on several distinct sites on the NR1 subunit. Most of these sites are contained within a single alternatively spliced exon in the C-terminal domain, which has previously been proposed to be on the extracellular side of the membrane (1). A role for NMDAR1 in the molecular pathology underlying Huntington disease (HD) has been proposed on the basis of neurochemical studies in HD and the ability of the NMDAR1 to mediate neuronal cell death (2). Also, studies reveal a unrecognized role of the NMDAR1 in dynamically maintaining the long-term synaptic stability of memory storage circuits in the brain (3).
1. Tingley WG, et al. Nature 364(6432): 70-3, 1993
2. Collins C, et al. Genomics 17(1):237-9, 1993
3. Cui Z, et al. Neuron 41(5):781-93, 2004
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