D-AP5 (mM/ml), NMDA glutamate site antagonist
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(102 Publications)
MW 197.13 Da, Purity >99%. Competitive NMDA receptor glutamate site antagonist. More active form of DL-AP5. Achieve your results faster with highly validated, pure and trusted compounds.
View Alternative Names
AMPA 1, AMPA-selective glutamate receptor 1, AW490526, Chi-1, EB11, EIEE27, EPND, FESD, GLUH1, GRIA1_HUMAN, GRIN 2A, GRIN 2B, GRIN3A, GRIN3B, GluA1, GluN1, GluN2A, GluN2C, GluN2D, GluN3B, GluR-1, GluR-A, GluR-K1, Glutamate Receptor Ionotropic N Methyl D Aspartate 2B, Glutamate Receptor Ionotropic N Methyl D Aspartate 2C, Glutamate Receptor Ionotropic N Methyl D Aspartate subunit 2B, Glutamate [NMDA] receptor subunit 3A, Glutamate [NMDA] receptor subunit 3B, Glutamate [NMDA] receptor subunit epsilon-1, Glutamate [NMDA] receptor subunit epsilon-2, Glutamate [NMDA] receptor subunit epsilon-3, Glutamate [NMDA] receptor subunit epsilon-4, Glutamate [NMDA] receptor subunit zeta-1, Glutamate receptor, Glutamate receptor 1, Glutamate receptor ionotropic, Glutamate receptor ionotropic AMPA 1, Glutamate receptor ionotropic N methyl D aspartate 1, Glutamate receptor ionotropic N methyl D aspartate 2A, Glutamate receptor ionotropic N methyl D aspartate 3B, Glutamate receptor ionotropic NMDA 3B, Glutamate receptor ionotropic NMDA2B, Glutamate receptor ionotropic, N-methyl-D aspartate, subunit 1, Glutamate receptor ionotropic, NMDA 2C, Glutamate receptor subunit epsilon 2, Glutamate receptor, ionotropic, N-methyl D-aspartate 2D, Glutamate receptor, ionotropic, NMDA2B (epsilon 2), Grin2c, Grin2d, HBGR1, LKS, MGC133252, MGC142178, MGC142180, MRD6, MRD8, N Methly D Aspartate Receptor Channel Subunit Epsilon 3, N methyl D asparate receptor channel subunit epsilon 2, N methyl D aspartate receptor channel subunit zeta 1, N methyl D aspartate receptor channel, subunit epsilon 1, N methyl D aspartate receptor subunit 2A, N methyl D aspartate receptor subunit 2B, N methyl D aspartate receptor subunit 2C, N methyl d aspartate receptor subunit 2D, N-methyl D-aspartate receptor subtype 2A, N-methyl D-aspartate receptor subtype 2B, N-methyl D-aspartate receptor subtype 2C, N-methyl D-aspartate receptor subtype 2D, N-methyl-D-aspartate receptor, N-methyl-D-aspartate receptor subtype 3A, N-methyl-D-aspartate receptor subtype 3B, N-methyl-D-aspartate receptor subunit 3, N-methyl-D-aspartate receptor subunit NR1, NMD-R1, NMD3A_HUMAN, NMD3B_HUMAN, NMDA 1, NMDA 2D, NMDA NR2B, NMDA receptor 1, NMDA receptor subtype 2A, NMDA receptor subunit 3B, NMDA type glutamate receptor subunit NR3B, NMDAR, NMDAR-L, NMDAR-L1, NMDAR2C, NMDAR2D, NMDAR3A, NMDAR3B, NMDE1_HUMAN, NMDE2_HUMAN, NMDE3_HUMAN, NMDE4_HUMAN, NMDZ1_HUMAN, NR1, NR2A, NR2B, NR2C, NR2D, NR3, OTTHUMP00000041930, OTTHUMP00000160135, OTTHUMP00000160643, OTTHUMP00000165781, OTTHUMP00000174531, OTTHUMP00000224241, OTTHUMP00000224242, OTTHUMP00000224243, estrogen receptor binding CpG island, glutamate receptor ionotropic NMDA 2D, glutamate receptor ionotropic, NMDA 1, hNR 3, hNR2A
- FuncS
PubMed
Functional Studies - D-AP5 (mM/ml), NMDA glutamate site antagonist (AB144482)
Fractional current mediated by AMPARs increases between birth and hearing onset.
A : Representative mixed glutamatergic responses from P1, P5 and P9 neurons (average of 10 recordings), scaled to peak AMPA current; distinct AMPA and NMDA components visible in each trace. B : Same traces as in A, showing the mixed glutamatergic current, the pharmacologically isolated NMDAR component, and the response after application of AMPAR and NMDAR antagonists, D-APV and CNQX, which abolishes the glutamatergic response. All recordings in Mg++-free ACSF. Note change in scalebars for P9 recordings. C : Ratios of peak AMPA/NMDA current in 39 cells from slices P1-P12. During this period, AMPA/NMDA ratio increases as a function of age (p = 0.012, Kruskal-Wallis; P1/2 vs P9/10, p = 0.048; P7/8 vs P9/10, p = 0.30; P9/10 vs P11/12 p = 0.010; linear regression slope 0.14/day, r2 = 0.32; exponential fit r2 = 0.36). Filled black circles represent means ± SEMs at two-day intervals. Filled gray circles represent cells shown in A,B. D : Increase in AMPA/NMDA ratio with age is accompanied by small increases in average AMPA current (open circles, regressed to gray line) and decreases in average NMDAR current (filled circles, regressed to black line).
Case et al PLoS One. 2011;6(6):e20756. doi: 10.1371/journal.pone.0020756. Epub 2011 Jun 9. Fig 3. Reproduced under the Creative Commons license http://creativecommons.org/licenses/by/4.0/
- Chemical Structure
Lab
Chemical Structure - D-AP5 (mM/ml), NMDA glutamate site antagonist (AB144482)
2D chemical structure image of ab144482, D-AP5 (mM/ml), NMDA glutamate site antagonist
Properties and storage information
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
These subunits work together to form a tetrameric channel allowing calcium influx when activated. This movement of ions plays a critical role in synaptic transmission and plasticity which underlies learning and memory processes. NMDAR requires co-agonists such as glycine for activation and participates in magnesium block removal when neurons are depolarized. Each subunit confers specific properties to the receptor like modulating its ion channel properties and desensitization kinetics.
Pathways
The NMDA receptor complex functions prominently within the glutamatergic signaling pathway and synaptic plasticity pathways. It is connected to calcium/calmodulin-dependent protein kinase II (CaMKII) which links NMDA receptor activity to downstream signaling cascades such as the mitogen-activated protein kinase (MAPK) pathway. These pathways are important for gene expression synaptic strength and neuronal survival highlighting the significance of NMDAR in neurophysiological processes.
Publications (102)
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Heliyon 9:e20620 PubMed37876454
2023
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Cell reports 37:109978 PubMed34758316
2021
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Nature neuroscience 16:632-8 PubMed23542690
2013
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The Journal of neuroscience : the official journal of the Society for Neuroscience 33:5486-98 PubMed23536064
2013
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The Journal of neuroscience : the official journal of the Society for Neuroscience 33:4768-81 PubMed23486948
2013
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The Journal of physiology 591:2541-61 PubMed23478133
2013
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Journal of neurochemistry 125:205-13 PubMed23350646
2013
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The Journal of biological chemistry 288:8952-65 PubMed23400781
2013
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The Journal of physiology 591:219-39 PubMed23070699
2012
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Molecular pharmacology 83:106-21 PubMed23066089
2012
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