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MABN827

Sigma-Aldrich

抗-Tau抗体(克隆T49,非人类)

clone T49, from mouse

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别名:
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau
UNSPSC代码:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物来源

mouse

质量水平

抗体形式

purified antibody

抗体产品类型

primary antibodies

克隆

T49, monoclonal

种属反应性

mouse, rat, bovine

请勿与下列物质发生反应

human

技术

immunohistochemistry: suitable
western blot: suitable

同位素/亚型

IgG1κ

NCBI登记号

UniProt登记号

运输

wet ice

靶向翻译后修饰

unmodified

基因信息

一般描述

Tau,或称微管相关蛋白Tau(MAPT),也称为神经原纤维缠结蛋白、双股螺旋细丝tau(PHF-tau),是一种细胞质蛋白,促进微管的组装和稳定,并可能涉及神经元中轴突极性(axonal polarity )的形成和维持。Tau 结合轴突微管,并被认为是轴突微管和神经细胞质膜成分的连接蛋白(linker protein)。该蛋白有多种亚型,短的亚型赋予细胞骨架可塑性,而较长的亚型可能在其稳定中起一定作用。PAD 是磷酸酶激活结构域(phosphatase activating domain),研究表明,其通过激活轴突蛋白磷酸酶1(PP1)和糖原合成酶激酶3(GSK3),以独立于微管结合的形式,参与基于驱动蛋白的、顺行性快速轴突运输(fast axonal transport,FAT)。Tau的缺陷被认为是许多神经退行性疾病的原因,包括额颞叶痴呆(FTD)、pallido-ponto-nigral degeneration(PPND)、皮克脑病(PIDB)、皮质基底节变性(CB)、核上性麻痹1型(PSNP1)、阿尔茨海默病和帕金森病。 克隆T49对于牛、大鼠和鼠类Tau有免疫反应性,但是对人Tau(分别为UniProt P29172、P19332、P10637、P10636)没有免疫反应性。

免疫原

纯化态对应于牛 Tau。

应用

免疫组化分析:一个代表性批次以的1:1,000 稀释液在小鼠大脑皮层、小鼠肾脏和小鼠小肠组织组织中检测到Tau。
蛋白质印迹分析:一个代表性批次在PBS处理的或FL a-syn pffs A株系或B株系转染的PS19神经元中检测到Tau(Guo, J.L., et al. (2013).Cell. 154:103-117)。
抗-Tau 抗体(克隆T49)(非人类)是针对Tau 的抗体,用于蛋白质印迹和免疫组织化学。

质量

通过蛋白质印迹在人 脑组织裂解物中进行了评估。

蛋白质印迹分析:0.5 µg/mL的该抗体在10 µg小鼠和人脑组织裂解物中检测到Tau。

目标描述

观测值〜53 kDa。该抗体具有45-76 kDa的多种亚型。

外形

形式:纯化

其他说明

浓度:请参考特定批次的数据表。

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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Parissa Fereydouni-Forouzandeh et al.
Methods in molecular biology (Clifton, N.J.), 2754, 309-321 (2024-03-21)
Tau is a microtubule-associated protein enriched in the axonal compartment. Its most well-known function is to bind and stabilize microtubules. In Alzheimer's disease and other neurodegenerative diseases known as tauopathies, tau undergoes several abnormal post-translational modifications including hyperphosphorylation, conformational changes
Sarah Helena Nies et al.
The Journal of biological chemistry, 297(4), 101159-101159 (2021-09-05)
In Alzheimer's disease (AD), deposition of pathological tau and amyloid-β (Aβ) drive synaptic loss and cognitive decline. The injection of misfolded tau aggregates extracted from human AD brains drives templated spreading of tau pathology within WT mouse brain. Here, we
Michael Fassler et al.
Cells, 12(11) (2023-06-10)
TREM2 is a membrane receptor expressed on microglia that plays a pivotal role in the organization and function of these innate immune cell components within the neurodegenerated brain. Whereas TREM2 deletion has been studied extensively in experimental beta-amyloid and Tau-based
Elena Ficulle et al.
Scientific reports, 12(1), 2673-2673 (2022-02-19)
Cellular models recapitulating features of tauopathies are useful tools to investigate the causes and consequences of tau aggregation and the identification of novel treatments. We seeded rat primary cortical neurons with tau isolated from Alzheimer's disease brains to induce a
Antigoni Katsikoudi et al.
The Journal of biological chemistry, 295(37), 13079-13093 (2020-07-24)
Tau aggregation and hyperphosphorylation is a key neuropathological hallmark of Alzheimer's disease (AD), and the temporospatial spread of Tau observed during clinical manifestation suggests that Tau pathology may spread along the axonal network and propagate between synaptically connected neurons. Here

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