Analytical Data
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Gene name
PNS-Tau/MAPT
- Application
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Alternative Names
DDPAC; FTDP-17; MAPTL; MSTD; MTBT1; MTBT2; PPND; Neurofibrillary tangle protein; Microtubule Associated Protein Tau; Paired helical filament-tau; G Protein Beta1/Gamma2 Subunit-Interacting Factor 1
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P19332
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Expression Region
Ala34~Ser368
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Molecular Weight
48kDa
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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
The PNS-Tau/MAPT recombinant protein is increasingly relevant in neuroscience research, particularly in understanding neurodegenerative diseases such as Alzheimer's disease. Tau is a microtubule-associated protein encoded by the MAPT gene, and its hyperphosphorylation and aggregation into neurofibrillary tangles are hallmarks of Tauopathies. Investigating the structure and function of Tau, especially in its phosphorylated state, is critical for elucidating the underlying mechanisms of tau-related pathologies. Research has shown that abnormal Tau interactions disrupt neuronal function, leading to synaptic loss and neurodegeneration. Therefore, the study of PNS-Tau/MAPT recombinant proteins can provide valuable insights into Tau's physiological and pathological roles, facilitating the search for potential therapeutic targets. By using recombinant technology to produce PNS-Tau/MAPT, scientists can analyze its properties in vitro and in vivo, enabling them to identify how specific modifications influence Tau's behavior and its interactions with other cellular components. This knowledge is crucial for the development of Tau-targeted therapies aimed at slowing or halting the progression of neurodegenerative diseases. Overall, the ongoing research into PNS-Tau/MAPT recombinant protein is a vital step towards advancing our understanding of Tau biology and developing novel strategies for intervention in Tau-related disorders.
