Analytical Data
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Gene name
Tau
- Application
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Alternative Names
Tau；MAPTL；MTBT1；TAU；Microtubule-associated Protein tau
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10636
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Expression Region
558-697aa
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AA Sequence
SRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSK CGSKDNIKHVLGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVK SEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRE
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Molecular Weight
15 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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 proteins are microtubule-associated proteins predominantly expressed in neurons, where they play a crucial role in stabilizing microtubules and maintaining neuronal structure and function. The research surrounding Tau has gained significant traction due to its central involvement in various neurodegenerative disorders, most notably Alzheimer’s disease and other tauopathies, characterized by the abnormal hyperphosphorylation and aggregation of Tau, forming neurofibrillary tangles that disrupt cellular function. Understanding the molecular mechanisms that govern Tau's function and its pathological aggregation is essential for developing therapeutic strategies aimed at halting or reversing neuronal damage. Recent studies have focused on the potential of Tau as a target for drug development, exploring Tau-targeting antibodies, small molecules, and gene therapies to modulate its activity or inhibit its aggregation. Additionally, advances in molecular biology techniques, including recombinant DNA technology, have enabled the production of Tau recombinants for in-depth biochemical characterization and the examination of its interactions with other cellular components. As researchers unravel the complexities of Tau biology, this knowledge holds promise for elucidating the pathogenesis of tauopathies and paving the way for innovative treatment options that could improve the lives of individuals affected by these debilitating diseases.
