NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death By similarity.Lasky L.A., J. Biol. Chem. 275:21477-21485(2000).Mandich P., Neurosci. Lett. 239:49-53(1997).Ajmar F., Genomics 22:216-218(1994).
Host
Rabbit
Immunogen
Synthesized non-phosphopeptide derived from Human GRIN2B around the phosphorylation site of serine 1303 (Q-H-S(p)-Y-D).
Involvement In Disease
Mental retardation, autosomal dominant 6, with or without seizures (MRD6); Epileptic encephalopathy, early infantile, 27 (EIEE27)
Raised In
Rabbit
Reactivity
Human, Mouse
Regulatory
RUO
Relevance
NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death By similarity.
Lasky L.A., J. Biol. Chem. 275:21477-21485(2000). Mandich P., Neurosci. Lett. 239:49-53(1997). Ajmar F., Genomics 22:216-218(1994).
Species
Homo Sapiens (Human)
Specificity
The antibody detects endogenous levels of total GRIN2B protein.
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+)