D-Cycloserine, NMDA glycine site agonist
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(3 Publications)
MW 102.09 Da, Purity >99%. Partial agonist at the NMDA receptor glycine recognition site. Enhances learning and memory in vivo. Perfomance enhancer in a variety of cognitive models.
Also available in simple stock solutions (ab146677) - add 1 ml of water to get an exact, ready-to-use concentration.
View Alternative Names
AMPA 1, AMPA-selective glutamate receptor 1, ARNT-interacting protein, Basic-helix-loop-helix-PAS protein MOP1, Class E basic helix-loop-helix protein 78, GLUH1, GRIA1_HUMAN, GluA1, GluR-1, GluR-A, GluR-K1, Glutamate receptor 1, Glutamate receptor ionotropic, Glutamate receptor ionotropic AMPA 1, HBGR1, HIF-1, HIF-1-alpha, HIF-alpha, HIF1A_HUMAN, Hypoxia inducible factor 1 alpha isoform I.3, Hypoxia inducible factor 1 alpha subunit, Hypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor, Hypoxia inducible factor 1, alpha subunit (basic helix loop helix transcription factor), Hypoxia-inducible factor 1-alpha, MGC133252, MOP 1, Member of PAS protein 1, Member of PAS superfamily 1, Member of the PAS Superfamily 1, OTTHUMP00000160643, OTTHUMP00000165781, OTTHUMP00000224241, OTTHUMP00000224242, OTTHUMP00000224243, PAS domain-containing protein 8, PASD 8, bHLHe78, hifla
- Chemical Structure
Lab
Chemical Structure - D-Cycloserine, NMDA glycine site agonist (AB120121)
2D chemical structure image of ab120121, D-Cycloserine, NMDA glycine site agonist
Properties and storage information
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Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Glutamate receptors like the GRIA1 play an important role in synaptic plasticity and memory formation through involvement in excitatory neurotransmission. This receptor functions as part of a tetrameric complex where it interacts with other AMPA receptor subunits. Through its ion channel GRIA1 allows the flow of sodium and potassium ions which are essential for depolarizing the postsynaptic neuron and transmitting the nerve signal.
Pathways
The GRIA1 receptor is a significant component of the glutamatergic synapse pathway. This pathway is essential for learning and memory mechanisms in the brain and involves NMDA and AMPA receptors. GRIA1 interacts with proteins such as D-cycloserine an NMDA agonist affecting synaptic responses and plasticity. Its function in this pathway connects it to long-term potentiation a cellular process underlying memory and learning.
Publications (3)
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Biological psychiatry 92:815-826 PubMed34247782
2021
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Cell reports 31:107700 PubMed32492416
2020
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Unspecified reactive species
Cell reports 29:34-48.e4 PubMed31577954
2019
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Unspecified reactive species
Product promise
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