research use only

NMDA Receptor 2B/GluN2B Antibody [K20B17]

Cat.No.: F0550

    Application: Reactivity:
    • F0550-wb
      Lane 1: Mouse brain, Lane 2: Neonatal mouse brain

    Usage Information

    Dilution
    1:1000
    Application
    WB
    Reactivity
    Human, Mouse, Rat
    Source
    Rabbit Monoclonal Antibody
    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
    Predicted MW
    190 kDa

    Datasheet & SDS

    Biological Description

    Specificity
    NMDA Receptor 2B/GluN2B Antibody [K20B17] detects endogenous levels of total NMDA Receptor 2B/GluN2B protein.
    Clone
    K20B17
    Synonym(s)
    Glutamate receptor ionotropic, NMDA 2B; GluN2B; Glutamate [NMDA] receptor subunit epsilon-2; N-methyl D-aspartate receptor subtype 2B (NMDAR2B; NR2B); N-methyl-D-aspartate receptor subunit 3 (NR3; hNR3); GRIN2B; NMDAR2B
    Background
    NMDA Receptor 2B (GluN2B) is the glutamate-binding subunit critical for assembling functional NMDA receptors, which are heterotetrameric ligand-gated cation channels typically composed of two GluN1 and two GluN2 subunits. Each subunit features an extracellular amino-terminal domain (NTD) and ligand-binding domain (LBD), a membrane-spanning domain (TMD) forming the ion-conducting pore, and an intracellular C-terminal domain (CTD) subject to regulatory phosphorylation. NMDA receptor activation requires concurrent binding of glutamate to GluN2B’s LBD and glycine or D-serine to GluN1, along with membrane depolarization to relieve the Mg²⁺ block. This ligand binding induces LBD clamshell closure, transmitting conformational changes through the TMD to open the channel and permit Na⁺, K⁺, and especially Ca²⁺ influx. GluN2B-containing receptors are especially prominent during early neurodevelopment and at extrasynaptic sites, where they enable synaptic plasticity processes such as long-term potentiation (LTP). Phosphorylation of GluN2B at Tyr1472 by Src family kinases enhances Ca²⁺ permeability and couples receptor activation to CaMKII-mediated spine remodeling and memory formation. While GluN2B-driven signaling is essential for neurodevelopment and learning, its overactivation is implicated in excitotoxic neurodegeneration, such as in Alzheimer’s, Parkinson’s, stroke, and chronic pain, where excessive Ca²⁺ entry triggers cell death pathways.
    References
    • https://pubmed.ncbi.nlm.nih.gov/37324591/
    • https://pubmed.ncbi.nlm.nih.gov/30037851/

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