无载体,SUMO标签,≥90%(SDS-PAGE),expressed in E. coli; 见COA
生化机理
Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg2+ (PubMed:21376300, PubMed:26875626, PubMed:26919761, PubMed:28126851, PubMed:28228639, PubMed:36959261, PubMed:7679115, PubMed:7681588, PubMed:7685113).
NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the long-term potentiation (LTP) (PubMed:26875626).
Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg2+ (PubMed:21376300, PubMed:26875626, PubMed:26919761, PubMed:27164704, PubMed:28095420, PubMed:28105280, PubMed:28126851, PubMed:28228639, PubMed:36959261, PubMed:38538865, PubMed:7679115, PubMed:7681588, PubMed:7685113).
NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (By similarity).
Each GluN2 or GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2+ permeability, and binding to allosteric modulators (PubMed:26875626, PubMed:26919761, PubMed:36309015, PubMed:38598639).
Post-translational: NMDA is probably regulated by C-terminal phosphorylation of an isoform of GRIN1 by PKC (PubMed:8316301). Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB) (PubMed:8316301). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity (PubMed:8316301).
Recombinant Human NMDAR1 Protein (rp217158) - SDS-PAGE
3 μg/lane of Recombinant Human NMDAR1 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 28.4 kDa.
ZJ26F0434675
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