Analytical Data
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Gene name
Tau-F/2N4R Pre-formed
- Application
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Species
Human
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Source
E. coli
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Tag
Tag Free
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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
Q244-E372
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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
The Tau-F/2N4R pre-formed recombinant protein is of significant interest in neurodegenerative research, particularly in the context of tauopathies, which are a group of disorders characterized by the aggregation of tau protein, leading to neurodegeneration and cognitive decline. Tau protein is involved in stabilizing microtubules in neuronal cells, but its hyperphosphorylation and subsequent misfolding can result in the formation of neurofibrillary tangles, a hallmark found in diseases such as Alzheimer's disease and frontotemporal dementia. The 2N4R isoform of tau, which contains two N-terminal inserts and four repeat domains, is predominantly expressed in the human brain and is particularly relevant in the study of these pathologies. Research into pre-formed tau aggregates, like Tau-F/2N4R, is crucial as they can induce a prion-like propagation of tau pathology in model systems, thereby facilitating the understanding of tau dynamics, aggregation mechanisms, and spreading in the brain. This recombinant protein serves as a valuable tool for in vitro and in vivo studies, enabling scientists to dissect the biochemical and cellular processes underlying tau aggregation and toxicity. Furthermore, it holds potential for therapeutic exploration, aiming to develop strategies that can inhibit tau propagation, ultimately contributing to the development of effective treatments for tau-related diseases. Overall, the study of Tau-F/2N4R pre-formed aggregates is pivotal in advancing our understanding of tauopathies and exploring novel therapeutic avenues for managing these debilitating conditions.











