Datasheet

Biological Description

Specificity	NMDA Receptor 1 (GluN1) Antibody [D10D12] detects endogenous levels of total NMDA Receptor 1 (GluN1) protein.
Background	NMDA Receptor 1 (GluN1) (N-Methyl-D-aspartate receptor subunit 1) is the obligatory glycine/D-serine-binding subunit present in all functional NMDA receptors, making it essential for receptor assembly and function in virtually all central neurons. Structurally, GluN1 consists of an extracellular amino-terminal domain (ATD) that regulates allosteric modulation, a bilobed agonist-binding domain (ABD) that binds glycine or D-serine, a transmembrane domain forming part of the ion channel pore, and an intracellular carboxyl-terminal domain (CTD) that interacts with scaffolding and signaling proteins such as PSD-95, calmodulin, and NF-L; alternative splicing of exons 5, 21, and 22 generates eight isoforms with distinct regulatory properties. Widely expressed across the CNS, GluN1 pairs with GluN2 (A–D) and sometimes GluN3 subunits to form heterotetrameric receptors whose properties depend on subunit composition. Functionally, GluN1-containing receptors act as ligand-gated ion channels that require both glutamate (binding to GluN2) and glycine/D-serine (binding to GluN1) for activation, and their voltage-dependent Mg²⁺ block and high Ca²⁺ permeability make them central to synaptic transmission, long-term potentiation, excitatory postsynaptic current duration, and activity-dependent synaptic plasticity underlying learning and memory.

Specificity

NMDA Receptor 1 (GluN1) Antibody [D10D12] detects endogenous levels of total NMDA Receptor 1 (GluN1) protein.

Background

NMDA Receptor 1 (GluN1) (N-Methyl-D-aspartate receptor subunit 1) is the obligatory glycine/D-serine-binding subunit present in all functional NMDA receptors, making it essential for receptor assembly and function in virtually all central neurons. Structurally, GluN1 consists of an extracellular amino-terminal domain (ATD) that regulates allosteric modulation, a bilobed agonist-binding domain (ABD) that binds glycine or D-serine, a transmembrane domain forming part of the ion channel pore, and an intracellular carboxyl-terminal domain (CTD) that interacts with scaffolding and signaling proteins such as PSD-95, calmodulin, and NF-L; alternative splicing of exons 5, 21, and 22 generates eight isoforms with distinct regulatory properties. Widely expressed across the CNS, GluN1 pairs with GluN2 (A–D) and sometimes GluN3 subunits to form heterotetrameric receptors whose properties depend on subunit composition. Functionally, GluN1-containing receptors act as ligand-gated ion channels that require both glutamate (binding to GluN2) and glycine/D-serine (binding to GluN1) for activation, and their voltage-dependent Mg²⁺ block and high Ca²⁺ permeability make them central to synaptic transmission, long-term potentiation, excitatory postsynaptic current duration, and activity-dependent synaptic plasticity underlying learning and memory.

Usage Information

Application

WB, IP

Dilution

WB	IP
1:1000	1:50

Reactivity

Human, Mouse, Rat

Source

Rabbit Monoclonal Antibody

MW

120 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/30037851/

NMDA Receptor 1 (GluN1) Antibody [D10D12]

Biological Description

Usage Information

References

Application Data