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Merck
CN
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主要文件

ABN88

Sigma-Aldrich

Anti-phospho-NR1 (Ser896) Antibody

from rabbit, purified by affinity chromatography

别名:

glutamate receptor, ionotropic, N-methyl D-aspartate 1, glutamate [NMDA] receptor subunit zeta 1, N-methyl-D-aspartate receptor channel, subunit zeta-1, N-methyl-D-aspartate receptor subunit NR1, glutamate [NMDA] receptor subunit zeta-1

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About This Item

UNSPSC代码:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物来源

rabbit

质量水平

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

纯化方式

affinity chromatography

种属反应性

rat

种属反应性(根据同源性预测)

mouse (based on 100% sequence homology), human (based on 100% sequence homology)

技术

immunohistochemistry: suitable (paraffin)
western blot: suitable

NCBI登记号

UniProt登记号

运输

wet ice

靶向翻译后修饰

phosphorylation (pSer896)

基因信息

human ... GRIN1(2902)
mouse ... Grin1(14810)
rat ... Grin1(24408)

一般描述

NR1 (NMDA1or NMDAR1, also known as GRIN1) along with the NR2 subunit forms a heterodimer that make up the NMDA receptor. The NMDA receptor (NMDAR) is characterized as a ionotropic receptor for glutamate. As the name suggests, (NMDA (N-methyl D-aspartate) is an agonist for the receptor. A distinct characteristic of the NMDA receptor is that it is both ligand-gated and voltage-dependent based on its sensitivity to magnesium. Activated NMDA receptors result in the opening of an ion channel that is nonselective to cations. The result is the flow of Na+ and small amounts of Ca2+ ions into the cell and K+ out of the cell. Calcium flux by the NMDARs has been implicated in synaptic plasticity, a mechanism in the cell for learning and memory.

特异性

This antibody recognizes NR1 when phosphorylated at Ser896.

免疫原

Epitope: Phosphorylated Ser896
KLH-conjugated linear peptide corresponding to rat NR1 phosphorylated at Ser896.

应用

Detect phospho-NR1 (Ser896) using this Anti-phospho-NR1 (Ser896) Antibody validated for use in WB, IH(P).
Immunohistochemistry Analysis: 1:25 dilution from a previous lot detected NR1 in normal rat hippocampus tissue.

质量

Evaluated by Western Blot in lambda phosphatase untreated and treated rat microsomal brain tissue lysates.

Western Blot Analysis: 1 µg/mL of this antibody detected NR1 on 10 µg of lambda phosphatase untreated and treated rat microsomal brain tissue lysates.

目标描述

~130kDa observed

联系

Replaces: 06-640

分析说明

Control
Lambda phosphatase untreated and treated rat microsomal brain tissue lysates

其他说明

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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储存分类代码

10-13 - German Storage Class 10 to 13


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Sheu-Ran Choi et al.
Molecular pain, 15, 1744806919843046-1744806919843046 (2019-03-23)
Spinal D-serine plays an important role in nociception via an increase in phosphorylation of the N-Methyl-D-aspartate (NMDA) receptor GluN1 subunit (pGluN1). However, the cellular mechanisms underlying this process have not been elucidated. Here, we investigate the possible role of neuronal
Jing-Dun Xie et al.
The Journal of biological chemistry, 291(37), 19364-19373 (2016-07-28)
Painful peripheral neuropathy is a severe adverse effect of chemotherapeutic drugs such as paclitaxel (Taxol). The glutamate N-methyl-d-aspartate receptors (NMDARs) are critically involved in the synaptic plasticity associated with neuropathic pain. However, paclitaxel treatment does not alter the postsynaptic NMDAR
Milena De Felice et al.
Molecular pain, 12 (2016-04-21)
Bone metastases occur frequently in advanced breast, lung, and prostate cancer, with approximately 70% of patients affected. Pain is a major symptom of bone metastases, and current treatments may be inadequate or have unacceptable side effects. The mechanisms that drive
Sheu-Ran Choi et al.
Experimental neurobiology, 28(4), 516-528 (2019-09-09)
We have previously demonstrated that the neurosteroid dehydroepiandrosterone sulfate (DHEAS) induces functional potentiation of N-methyl-D-aspartate (NMDA) receptors via increases in phosphorylation of NMDA receptor GluN1 subunit (pGluN1). However, the modulatory mechanisms responsible for the expression of the DHEA-synthesizing enzyme, cytochrome
Sheu-Ran Choi et al.
Biological & pharmaceutical bulletin, 39(12), 1922-1931 (2016-09-08)
We recently demonstrated that activation of spinal sigma-1 receptors (Sig-1Rs) induces pain hypersensitivity via the activation of neuronal nitric oxide synthase (nNOS) and nicotinamide adenine dinucleotide phosphate (NADPH) oxidase 2 (Nox2). However, the potential direct interaction between nNOS-derived nitric oxide

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