GRIN2D Polyclonal Antibody
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Application ![]()
| WB |
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Primary Accession | O15399 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 143752 Da |
Gene ID | 2906 |
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Other Names | Glutamate [NMDA] receptor subunit epsilon-4 (EB11) (N-methyl D-aspartate receptor subtype 2D) (NMDAR2D) (NR2D) |
Dilution | WB~~WB 1:500-2000, ELISA 1:10000-20000 |
Format | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% (W/V) sodium azide. |
Storage Conditions | -20℃ |
Name | GRIN2D {ECO:0000303|PubMed:27616483, ECO:0000312|HGNC:HGNC:4588} |
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Function | 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 Mg(2+) (PubMed:26875626, PubMed:27616483, PubMed:28126851, PubMed:9489750). Participates in synaptic plasticity for learning and memory formation (By similarity). 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 Mg(2+) (PubMed:26875626, PubMed:27616483, PubMed:28126851, PubMed:9489750). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 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:28095420, PubMed:28126851, PubMed:9489750). |
Cellular Location | Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
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:9489750, PubMed:27616483, PubMed:26875626, PubMed:28126851). Sensitivity to glutamate and channel kinetics depend on the subunit composition (PubMed:9489750).

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