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Merck
CN

MAB5416

抗-谷氨酸受体3抗体,克隆3B3

clone 3B3, Chemicon®, from mouse

别名:

AMPA-selective glutamate receptor 3, Glutamate receptor ionotropic, AMPA 3, glutamate receptor 3, glutamate receptor C, glutamate receptor subunit 3, glutamate receptor, ionotrophic, AMPA 3

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
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产品名称

抗-谷氨酸受体3抗体,克隆3B3, clone 3B3, Chemicon®, from mouse

Quality Level

biological source

mouse

conjugate

unconjugated

antibody form

purified antibody

antibody product type

primary antibodies

clone

3B3, monoclonal

species reactivity

monkey, mouse, human

species reactivity (predicted by homology)

rat

manufacturer/tradename

Chemicon®

technique(s)

immunocytochemistry: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... GRIA3(2892)

Analysis Note

对照


海马组织
蛋白质印迹分析: 该抗体的一个先前批次被用于WB。

Application

免疫组织化学: 一个先前批次的该抗体被用于IH。

最佳工作稀释度必须由最终用户确定。
抗谷氨酸受体3抗体,克隆3B3是用于WB、IC、IH、IH(P)的抗谷氨酸受体3的抗体。

Biochem/physiol Actions

与谷氨酸受体3(GluR3)反应。与GluR2无交叉反应。

General description

AMPA受体介导大多数兴奋性突触的快速突触电流,化学计量以亚型组成为特征。AMPA选择性GluR亚基有四种类型(GluR1、GluR2、GluR3和GluR4)。不同亚基的四聚体或五聚体组合有助于AMPA受体的功能多样性。 从突触后膜插入或去除GluR1/GluR4寡聚通道似乎是LTP/LTD活性依赖性的,而GluR2/GluR3寡聚体不断循环。 Millipore’s抗GluR2/3抗体可用于定位PSD中GluR2/GluR3受体装配体的表达。
约110 kDa

Immunogen

融合蛋白,GluR3的N末端

Physical form

形式:纯化
溶于PBS中的液体。不含防腐剂。

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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存储类别

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


分析证书(COA)

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David Bartolomé-Martín et al.
Journal of cell science, 125(Pt 2), 422-434 (2012-02-15)
Following the exocytosis of neurotransmitter-containing synaptic vesicles, endocytosis is fundamental to re-establishing conditions for synaptic transmission. As there are distinct endocytotic pathways that each differ in their efficiency to generate releasable synaptic vesicles, we used the dye FM1-43 to track
Janusz Tucholski et al.
Schizophrenia research, 146(1-3), 177-183 (2013-03-07)
Numerous studies have demonstrated brain region- and subunit-specific abnormalities in the expression of subunits of the AMPA subtype of glutamate receptors in schizophrenia. In addition, abnormalities in the expression of proteins that regulate the forward trafficking of AMPA receptors through
Evolutionarily conserved pattern of AMPA receptor subunit glycosylation in Mammalian frontal cortex.
Tucholski, J; Pinner, AL; Simmons, MS; Meador-Woodruff, JH
Testing null
Xiu Sun et al.
The European journal of neuroscience, 30(4), 539-550 (2009-08-14)
Synaptic scaling has been proposed as a form of plasticity that may contribute to drug addiction but it has not been previously demonstrated in the nucleus accumbens (NAc), a critical region for addiction. Here we demonstrate bidirectional synaptic scaling in
B Borroni et al.
Scientific reports, 7(1), 6723-6723 (2017-07-29)
Frontotemporal Dementia (FTD) is a neurodegenerative disorder mainly characterised by Tau or TDP43 inclusions. A co-autoimmune aetiology has been hypothesised. In this study, we aimed at defining the pathogenetic role of anti-AMPA GluA3 antibodies in FTD. Serum and cerebrospinal fluid

相关内容

Glutamate is an excitatory neurotransmitter found in the synaptic vesicles of glutamatergic synapses. The post-synaptic neurons in these synapses contain ionotropic and metabotropic glutamate receptors. Glutamate binds to AMPA (α-amino-3-hydroxy-5- methylisoxazole-4-propionic acid) subtype glutamate receptors, leading to sodium influx into the post-synaptic cell and resulting in neuronal excitability and synaptic transmission. The NMDA (N-methyl-d-aspartate) subtype glutamate receptors, on the other hand, regulate synaptic plasticity, and can influence learning and memory. The metabotropic g-protein coupled mGluRs modulate downstream calcium signaling pathways and indirectly influence the synapse’s excitability. The synaptic architecture includes intracellular scaffolding proteins (PSD-95, GRIP), intercellular cell adhesion molecules (NCAMs, N-Cadherins), and a variety of signaling proteins (CaMKII/PKA, PP1/PP2B). Processes critical for synaptic transmission and plasticity are influenced by these molecules and their interactions. When the function of these molecules is disrupted, it leads to synaptic dysfunction and degeneration, and can contribute to dementia as seen in Alzheimer’s disease.

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