Rabbit Anti-GRIN2A Recombinant Antibody (CBLG1-239) (CBMAB-G0788-LY)

Name: Rabbit Anti-GRIN2A Recombinant Antibody (CBLG1-239)
SKU: CBMAB-G0788-LY
Rating: 5 (1 reviews)

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Datasheet

SDS

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Basic Information

Host Animal

Rabbit

Clone

CBLG1-239

Application

Specificity

Human

Antibody Isotype

IgG

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Purity

> 95% Purity determined by SDS-PAGE.

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

Glutamate Ionotropic Receptor NMDA Type Subunit 2A

Introduction

This gene encodes a member of the glutamate-gated ion channel protein family. The encoded protein is an N-methyl-D-aspartate (NMDA) receptor subunit. NMDA receptors are both ligand-gated and voltage-dependent, and are involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. These receptors are permeable to calcium ions, and activation results in a calcium influx into post-synaptic cells, which results in the activation of several signaling cascades. Disruption of this gene is associated with focal epilepsy and speech disorder with or without cognitive disability. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2014]

Entrez Gene ID

2903

UniProt ID

Q12879

Alternative Names

Glutamate Ionotropic Receptor NMDA Type Subunit 2A; Glutamate Receptor; Ionotropic; N-Methyl D-Aspartate 2A; N-Methyl D-Aspartate Receptor Subtype 2A; NMDAR2A; GluN2A; NR2A; N-Methyl-D-Aspartate Receptor Channel; Subunit Epsilon-1; Glutamate [NMDA] Receptor Subunit Epsilon-1;

Function

Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg2+ (PubMed:8768735, PubMed:26919761, PubMed:26875626, PubMed:28105280).

Sensitivity to glutamate and channel kinetics depend on the subunit composition; channels containing GRIN1 and GRIN2A have lower sensitivity to glutamate and faster deactivation kinetics than channels formed by GRIN1 and GRIN2B (PubMed:26919761, PubMed:26875626).

Contributes to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity).

Biological Process

Activation of cysteine-type endopeptidase activity Source: ARUK-UCL
Brain development Source: ARUK-UCL
Calcium ion transmembrane import into cytosol Source: UniProtKB
Chemical synaptic transmission Source: ProtInc
Directional locomotion Source: Ensembl
Dopamine metabolic process Source: Ensembl
Excitatory chemical synaptic transmission Source: ARUK-UCL
Excitatory postsynaptic potential Source: GO_Central
Glutamate receptor signaling pathway Source: ProtInc
Learning or memory Source: ProtInc
Long-term synaptic potentiation Source: GO_Central
Memory Source: Ensembl
Negative regulation of protein catabolic process Source: Ensembl
Neurogenesis Source: Ensembl
Positive regulation of apoptotic process Source: Ensembl
Protein localization to postsynaptic membrane Source: Ensembl
Regulation of synaptic plasticity Source: ARUK-UCL
Response to amphetamine Source: Ensembl
Response to drug Source: Ensembl
Response to ethanol Source: UniProtKB
Response to wounding Source: Ensembl
Sensory perception of pain Source: Ensembl
Serotonin metabolic process Source: Ensembl
Sleep Source: Ensembl
Startle response Source: Ensembl
Visual learning Source: Ensembl

Cellular Location

Cell membrane; Postsynaptic cell membrane; Dendritic spine; Synapse; Cytoplasmic vesicle membrane. Expression at the dendrite cell membrane and at synapses is regulated by SORCS2 and the retromer complex.

Involvement in disease

Epilepsy, focal, with speech disorder and with or without mental retardation (FESD):
A highly variable neurologic disorder with features ranging from severe early-onset seizures associated with delayed psychomotor development, persistent speech difficulties, and mental retardation to a more benign entity characterized by childhood onset of mild or asymptomatic seizures associated with transient speech difficulties followed by remission of seizures in adolescence and normal psychomotor development. The disorder encompasses several clinical entities, including Landau-Kleffner syndrome, epileptic encephalopathy with continuous spike and wave during slow-wave sleep, autosomal dominant rolandic epilepsy, mental retardation and speech dyspraxia, and benign epilepsy with centrotemporal spikes.
A chromosomal aberration involving GRIN2A has been found in a family with epilepsy and neurodevelopmental defects. Translocation t(16;17)(p13.2;q11.2).
GRIN2A somatic mutations have been frequently found in cutaneous malignant melanoma, suggesting that the glutamate signaling pathway may play a role in the pathogenesis of melanoma.

Topology

Extracellular: 23-555
Helical: 556-576
Cytoplasmic: 577-600
Discontinuously helical: 601-620
Cytoplasmic: 621-625
Helical: 626-645
Extracellular: 646-816
Helical: 817-837
Cytoplasmic: 838-1464

Herzog, L. E., Wang, L., Yu, E., Choi, S., Farsi, Z., Song, B. J., ... & Sheng, M. (2023). Mouse mutants in schizophrenia risk genes GRIN2A and AKAP11 show EEG abnormalities in common with schizophrenia patients. Translational Psychiatry, 13(1), 92.

Mangano, G. D., Riva, A., Fontana, A., Salpietro, V., Mangano, G. R., Nobile, G., ... & Nardello, R. (2022). De novo GRIN2A variants associated with epilepsy and autism and literature review. Epilepsy & Behavior, 129, 108604.

Du, Z., Song, Y., Chen, X., Zhang, W., Zhang, G., Li, H., ... & Wu, Y. (2021). Knockdown of astrocytic Grin2a aggravates β‐amyloid‐induced memory and cognitive deficits through regulating nerve growth factor. Aging Cell, 20(8), e13437.

Poltavskaya, E. G., Fedorenko, O. Y., Kornetova, E. G., Loonen, A. J., Kornetov, A. N., Bokhan, N. A., & Ivanova, S. A. (2021). Study of early onset schizophrenia: Associations of GRIN2A and GRIN2B polymorphisms. Life, 11(10), 997.

Vieira, M. M., Nguyen, T. A., Wu, K., Badger, J. D., Collins, B. M., Anggono, V., ... & Roche, K. W. (2020). An epilepsy-associated GRIN2A rare variant disrupts CaMKIIα phosphorylation of GluN2A and NMDA receptor trafficking. Cell reports, 32(9).

Amador, A., Bostick, C. D., Olson, H., Peters, J., Camp, C. R., Krizay, D., ... & Frankel, W. N. (2020). Modelling and treating GRIN2A developmental and epileptic encephalopathy in mice. Brain, 143(7), 2039-2057.

Myers, S. J., Yuan, H., Kang, J. Q., Tan, F. C. K., Traynelis, S. F., & Low, C. M. (2019). Distinct roles of GRIN2A and GRIN2B variants in neurological conditions. F1000Research, 8.

Lesca, G., M⊘ ller, R. S., Rudolf, G., Hirsch, E., Hjalgrim, H., & Szepetowski, P. (2019). Update on the genetics of the epilepsy‐aphasia spectrum and role of GRIN2A mutations. Epileptic Disorders, 21, S41-S47.

Strehlow, V., Heyne, H. O., Vlaskamp, D. R., Marwick, K. F., Rudolf, G., De Bellescize, J., ... & Lemke, J. R. (2019). GRIN2A-related disorders: genotype and functional consequence predict phenotype. Brain, 142(1), 80-92.

Salmi, M., Bolbos, R., Bauer, S., Minlebaev, M., Burnashev, N., & Szepetowski, P. (2018). Transient microstructural brain anomalies and epileptiform discharges in mice defective for epilepsy and language‐related NMDA receptor subunit gene Grin2a. Epilepsia, 59(10), 1919-1930.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
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For research use only. Not intended for any clinical use.

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