Analytical Data
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Gene name
Tau-F/2N4R GSK-3beta-phosphorylated
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10636-8
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Expression Region
M1-L441
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Molecular Weight
45-65 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
Related Products
Protein Description
Tau-F/2N4R is a recombinant protein designed to study phosphorylation of tau protein by glycogen synthase kinase 3 beta (GSK-3β), a critical kinase implicated in neurodegenerative diseases such as Alzheimer's disease. The tau protein plays an essential role in stabilizing microtubules, and its abnormal phosphorylation leads to the formation of neurofibrillary tangles, which are hallmark features of Alzheimer's pathology. GSK-3β has been identified as a key enzyme that phosphorylates tau at multiple sites, influencing its aggregation and toxicity. Research on Tau-F/2N4R focuses on understanding the molecular mechanisms underlying GSK-3β-mediated tau phosphorylation, aiming to unveil therapeutic targets for intervention. By utilizing this recombinant protein, scientists can investigate the structure-function relationships of phosphorylated tau, assess its impact on microtubule dynamics, and evaluate potential inhibitors of GSK-3β as candidate drugs for slowing or reversing tau pathology. This research is crucial for developing effective treatments for tauopathies, highlighting the relevance of GSK-3β in tau-related neurodegenerative processes.
