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ABN426

Sigma-Aldrich

Anti-phospho-Neurogranin (Ser36)/Neuromodulin (Ser41) Antibody

serum, from rabbit

别名:

Protein kinase C substrate 7.5 kDa protein RC3

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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

serum

抗体产品类型

primary antibodies

克隆

polyclonal

种属反应性

mouse

种属反应性(根据同源性预测)

rat (based on 100% sequence homology)

技术

western blot: suitable

NCBI登记号

UniProt登记号

运输

wet ice

靶向翻译后修饰

phosphorylation (pSer36)

基因信息

mouse ... Nrgn(64011)
rat ... Nrgn(64356)

一般描述

Neurogranin (Ng) (also named RC3, p17 or BICKS) is a small protein originally identified in rat brain and abundantly expressed in several telencephalic areas, such as the cerebral cortex, hippocampus, amygdala, and striatum. In neurons, it is found concentrated at dendritic spines where it participates in synaptic signaling events through the regulation of calmodulin (CaM). Neurogranin protein is a critical third messenger and substrate of PKC in the molecular cascade necessary for synaptic development and remodeling. Neurogranin (Ng) features an IQ motif that mediates its interaction with CaM and phosphatidic acid (PA). The interaction is controlled by phosphorylation at serine 36 of Neurogranin. Neurogranin is phosphorylated at serine 36 by PKC. Ser36-phosphorylated Neurogranin is unable to bind either CaM or PA. Neurogranin in localized in the cell bodies of neurons in the cortex and in the apical and basal dendrites of pyramidal neurons. Neurogranin is not found in dendrites and its expression is very low as well in Alzheimer’s disease patients.

特异性

Phosphorylated Neurogranin and Neuromodulin

免疫原

Epitope: IQ domain
KLH-conjugated linear peptide corresponding to the IQ domain of Rat phospho-Neurogranin.

应用

Research Category
Neuroscience
Research Sub Category
Neuroregenerative Medicine
This Anti-phospho-Neurogranin (Ser36)/Neuromodulin (Ser41) Antibody is validated for use in Western Blotting for the detection of phospho-Neurogranin (Ser36)/Neuromodulin (Ser41).

质量

Evaluated by Western Blotting in Mouse brain tissue lysate.

Western Blotting Analysis: A 1:1000 dilution of this antibody detected phospho-Neurogranin (Ser36) / Neuromodulin (Ser41) in 10 µg of Mouse brain tissue lysate treate with magnisium (lane1) or PKC (lane2)

目标描述

~43 kDa is phospho-Neuromodulin (GAP-43) and ~17 KD is phospho-Neurogranin. Uncharacterized band(s) may appear in some lysates.

外形

Unpurified
Rabbit Polyclonal serum with 0.05% sodium azide.

储存及稳定性

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

其他说明

Concentration: Please refer to lot specific datasheet.

免责声明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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Sarah E Svirsky et al.
Molecular neurobiology, 61(9), 7256-7268 (2024-02-20)
Extensive effort has been made to study the role of synaptic deficits in cognitive impairment after traumatic brain injury (TBI). Neurogranin (Ng) is a calcium-sensitive calmodulin (CaM)-binding protein essential for Ca2+/CaM-dependent kinase II (CaMKII) autophosphorylation which subsequently modulates synaptic plasticity.
Shu Xu et al.
Frontiers in psychiatry, 12, 763032-763032 (2021-11-16)
Objective: Rapid eye movement sleep deprivation (REM-SD) can cause a decline in learning and memory and lead to changes in behavior. Therefore, REM sleep plays a key role in processes that govern learning and memory. However, the mechanism underlying REM-SD-induced
Nikolaus A Watson et al.
Nature communications, 11(1), 1684-1684 (2020-04-05)
There are thousands of known cellular phosphorylation sites, but the paucity of ways to identify kinases for particular phosphorylation events remains a major roadblock for understanding kinase signaling. To address this, we here develop a generally applicable method that exploits

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