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AB73014

Anti-NMDAR2B (phospho S1480) antibody

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(5 Publications)

Rabbit Polyclonal NMDAR2B phospho S1480 antibody. Suitable for WB and reacts with Rat samples. Cited in 5 publications. Immunogen corresponding to Synthetic Peptide within Rat Grin2b phospho S1480.

View Alternative Names

GluN2B, Glutamate [NMDA] receptor subunit epsilon-2, N-methyl D-aspartate receptor subtype 2B, NMDAR2B, NR2B

1 Images
Western blot - Anti-NMDAR2B (phospho S1480) antibody (AB73014)
  • WB

Unknown

Western blot - Anti-NMDAR2B (phospho S1480) antibody (AB73014)

The phosphospecificity of the labeling is shown in the second lane (lambda-phosphatase). The immunolabeling is completely eliminated by treatment with lambda-phosphatase.

All lanes:

Western blot - Anti-NMDAR2B (phospho S1480) antibody (ab73014) at 1/1000 dilution

Lane 1:

Rat hippocampal lysate

Lane 2:

Rat hippocampal lysate incubated in lambda-phosphatase (1200 units for 30 min)

Predicted band size: 166 kDa

Observed band size: 180 kDa,85 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Rat

Applications

WB

applications

Immunogen

Synthetic Peptide within Rat Grin2b phospho S1480. The exact immunogen used to generate this antibody is proprietary information.

Q00960

Specificity

ab73014 is specific for ~180k NMDAR2B protein phosphorylated at Ser1480. Immunolabeling of the NMDAR2B band is blocked by the phosphopeptide used as the antigen but not by the corresponding dephosphopeptide. Immunolabeling is also blocked by lambda-phosphatase treatment.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab73014 is prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.
Storage buffer
pH: 7.5 Constituents: 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.238% HEPES, 0.01% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

NMDAR2B also known as NR2B or GluN2B functions as a subunit of the NMDA receptor complex. It plays a role in synaptic transmission and plasticity in the central nervous system. The target weighs approximately 166 kDa. It is highly expressed in the cerebral cortex hippocampus and striatum. NMDAR2B interacts with other subunits in the NMDA receptor which assemble to form a functional ion channel that allows for calcium ion influx when activated by glutamate and glycine.
Biological function summary

The NMDAR2B subunit contributes to the regulation of synaptic strength and is essential for processes involved in learning and memory. As part of the NMDA receptor complex it mediates excitatory neurotransmission and is involved in synaptic plasticity processes such as long-term potentiation (LTP). These functions are significant for cognitive function and neural development. The receptor's role in signal transduction is aided by the unique properties conferred by the NMDAR2B subunit such as its high affinity for glycine and slower deactivation kinetics.

Pathways

NMDAR2B is involved in the glutamatergic signaling pathway which is important for neural communication. It also participates in the calcium signaling pathway affecting cellular responses to external stimuli. The protein interacts with CaMKII and PSD-95 which are proteins that influence synaptic strength and architecture through these pathways. Its involvement links it to a variety of signaling events important for brain function.

Alterations in NMDAR2B have been associated with neurodegenerative conditions such as Alzheimer's disease and neurodevelopmental disorders like schizophrenia. The protein's malfunction can lead to abnormal synaptic connectivity and excitotoxicity. It is linked to other proteins associated with these diseases such as beta-amyloid in Alzheimer's and dopamine receptor dysregulation in schizophrenia indicating its role in disease progression and symptom manifestation.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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 : 11929923, PubMed : 19910922, PubMed : 21677647, PubMed : 24607230, PubMed : 24876489, PubMed : 27135925, PubMed : 7524561). Participates in synaptic plasticity for learning and memory formation by contributing to the long-term depression (LTD) of hippocampus membrane currents (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 : 11929923, PubMed : 19910922, PubMed : 21677647, PubMed : 24607230, PubMed : 24876489, PubMed : 27135925, PubMed : 7524561). NMDARs mediate simultaneously the potassium 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 : 10436042, PubMed : 11929923, PubMed : 24607230, PubMed : 9463421). In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage (By similarity). Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).
See full target information Grin2b phospho S1480

Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Frontiers in cellular neuroscience 16:911973 PubMed35928572

2022

Casein kinase 2 attenuates brain injury induced by intracerebral hemorrhage via regulation of NR2B phosphorylation.

Applications

Unspecified application

Species

Unspecified reactive species

Zhimin Sun,Qiyao Li,Xiaopeng Li,Yunpeng Shi,Chengrui Nan,Qianxu Jin,Xiaoyan Wang,Yayu Zhuo,Zongmao Zhao

Communications biology 4:1138 PubMed34588597

2021

SALM4 negatively regulates NMDA receptor function and fear memory consolidation.

Applications

Unspecified application

Species

Unspecified reactive species

Eunkyung Lie,Yeji Yeo,Eun-Jae Lee,Wangyong Shin,Kyungdeok Kim,Kyung Ah Han,Esther Yang,Tae-Yong Choi,Mihyun Bae,Suho Lee,Seung Min Um,Se-Young Choi,Hyun Kim,Jaewon Ko,Eunjoon Kim

Scientific reports 10:8078 PubMed32415270

2020

Protopanaxadiol ginsenoside Rd protects against NMDA receptor-mediated excitotoxicity by attenuating calcineurin-regulated DAPK1 activity.

Applications

Unspecified application

Species

Unspecified reactive species

Chen Zhang,Xuedong Liu,Hui Xu,Gengyao Hu,Xiao Zhang,Zhen Xie,Dongyun Feng,Rui Wu,Gang Zhao,Ming Shi

Cell reports 25:841-851.e4 PubMed30355491

2018

The Developmental Shift of NMDA Receptor Composition Proceeds Independently of GluN2 Subunit-Specific GluN2 C-Terminal Sequences.

Applications

Unspecified application

Species

Unspecified reactive species

Sean McKay,Tomás J Ryan,Jamie McQueen,Tim Indersmitten,Katie F M Marwick,Philip Hasel,Maksym V Kopanitsa,Paul S Baxter,Marc-André Martel,Peter C Kind,David J A Wyllie,Thomas J O'Dell,Seth G N Grant,Giles E Hardingham,Noboru H Komiyama

EBioMedicine 7:191-204 PubMed27322472

2016

Exogenous Alpha-Synuclein Alters Pre- and Post-Synaptic Activity by Fragmenting Lipid Rafts.

Applications

Unspecified application

Species

Unspecified reactive species

Marco Emanuele,Alessandro Esposito,Serena Camerini,Flavia Antonucci,Silvia Ferrara,Silvia Seghezza,Tiziano Catelani,Marco Crescenzi,Roberto Marotta,Claudio Canale,Michela Matteoli,Elisabetta Menna,Evelina Chieregatti
View all publications

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