Analytical Data
-
Gene name
Tau-C/2N3R
- Application
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P10636-5
-
Expression Region
M1-L410
-
Molecular Weight
55-65 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
The Tau-F/2N4R recombinant protein is an essential focus of research in the context of neurodegenerative diseases, particularly Alzheimer's disease and frontotemporal dementia. Tau protein, a microtubule-associated protein that stabilizes microtubules in neurons, exists in multiple isoforms resulting from alternative splicing of the MAPT gene. The 2N4R isoform, characterized by its two N-terminal and four repeat domains, is particularly implicated in tauopathies due to its propensity to form toxic aggregates. These aggregates disrupt neuronal function and contribute to cell death. The Tau-F/2N4R construct serves as a valuable tool for studying the aggregation properties and pathobiology of tau in vitro and in vivo. Understanding the mechanisms by which Tau-F/2N4R aggregates form, how they interact with other cellular components, and their role in neurodegeneration is crucial for developing therapeutic strategies. Research on this recombinant protein also facilitates the screening of potential drugs aimed at preventing or reversing tau aggregation, ultimately contributing to novel approaches for treating tau-related disorders. Thus, the study of Tau-F/2N4R not only illuminates fundamental aspects of tau pathology but also holds promise for advancing therapeutic interventions in neurodegenerative diseases.
