产品名称
抗-Tau抗体(克隆T49,非人类), clone T49, from mouse
biological source
mouse
antibody form
purified antibody
antibody product type
primary antibodies
clone
T49, monoclonal
species reactivity
mouse, rat, bovine
should not react with
human
technique(s)
immunohistochemistry: suitable
western blot: suitable
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MAPT(4137)
mouse ... Mapt(17762), Mapt(281296)
rat ... Mapt(29477)
Analysis Note
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。
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。
Application
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)。
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。
General description
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。
观测值〜53 kDa。该抗体具有45-76 kDa的多种亚型。
Immunogen
纯化态对应于牛 Tau。
Other Notes
浓度:请参考特定批次的数据表。
Physical form
形式:纯化
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Sheng Chen et al.
Nature communications, 15(1), 2436-2436 (2024-03-19)
Parkinson's disease (PD) is closely linked to α-synuclein (α-syn) misfolding and accumulation in Lewy bodies. The PDZ serine protease HTRA1 degrades fibrillar tau, which is associated with Alzheimer's disease, and inactivating mutations to mitochondrial HTRA2 are implicated in PD. Here
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
Alberto Carpinteiro Soares et al.
The Journal of biological chemistry, 296, 100636-100636 (2021-04-09)
Tauopathies, such as Alzheimer's disease (AD), are neurodegenerative disorders characterized by the deposition of hyperphosphorylated tau aggregates. Proteopathic tau seeds spread through the brain in a temporospatial pattern, indicative of transsynaptic propagation. It is hypothesized that reducing the uptake of
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
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