Analytical Data
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基因名
Tau-D/0N4R
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简介
Microtubule-associated protein tau is a microtubule-associated protein found in large numbers in neurons of the central nervous system (CNS). MAPT promotes microtubule assembly and stability and may be involved in the establishment and maintenance of neuronal polarity. Overexpression of MAPT is associated with a poor prognosis of prostate cancer. MAPT has been linked to neurological disorders such as Alzheimer's and Parkinson's disease. Tau-D/0N4R Protein, Human (133a.a, His) is the recombinant human-derived Tau-D/0N4R protein, expressed by E. coli , with C-6*His labeled tag.
- Application
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别名
Microtubule-Associated Protein Tau; Neurofibrillary Tangle Protein; Paired Helical Filament-Tau; PHF-Tau; MAPT; MAPTL; MTBT1; TAU
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种属
Human
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表达系统
E. coli
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标签
C-6*His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P10636-6
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表达区间
Q249-Q381
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蛋白长度
Partial
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分子量
16-18 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Tau-D/0N4R recombinant protein is a significant focus in neurodegenerative research, particularly in the study of tauopathies, which are disorders associated with the hyperphosphorylation and aggregation of tau protein. Tau proteins are crucial for microtubule stabilization in neurons, and their misfolding and aggregation can lead to neurodegenerative diseases like Alzheimer's disease. The specific variant Tau-D/0N4R is characterized by having four Repeat (R) domains, which play a crucial role in tau's aggregation propensity and interaction with microtubules. Understanding the structure, function, and aggregation mechanisms of Tau-D/0N4R can provide insights into the pathophysiology of tauopathies. Research on recombinant Tau proteins facilitates the examination of these molecular processes in a controlled environment, allowing scientists to explore the effects of post-translational modifications, such as phosphorylation, on tau's behavior. Additionally, Tau-D/0N4R serves as a valuable tool for developing therapeutic strategies aimed at preventing tau aggregation or enhancing its clearance from the brain. By producing and characterizing this recombinant protein, researchers aim to unravel the complex dynamics of tau pathology and its implications for cognitive decline in affected individuals, ultimately contributing to the search for targeted treatments and diagnostic markers for tau-related disorders.
