Analytical Data
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Gene name
Grancalcin/GCA
- Application
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Alternative Names
GCA; GCL; Grancalcin
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P28676
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Expression Region
1-217aa
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Molecular Weight
51 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
The Tau-F/2N4R recombinant protein is a crucial element in the study of tauopathies, neurodegenerative disorders characterized by the aggregation of tau protein in the brain. Tau protein plays an essential role in stabilizing microtubules, and its dysfunction leads to tau hyperphosphorylation and the formation of neurofibrillary tangles, a hallmark of diseases such as Alzheimer's. The Tau-F isoform, a specific variant of tau, is particularly relevant due to its four repeat domains (2N4R), making it a prime candidate for investigating tau's pathological roles. Research on Tau-F/2N4R aims to elucidate the mechanisms behind tau aggregation and propagation, providing insights into disease progression and potential therapeutic targets. Recombinant expression systems allow for the production of this protein in controlled environments, facilitating studies on its biophysical properties, interaction with other cellular components, and the effects of various post-translational modifications. By understanding the structural and functional characteristics of Tau-F/2N4R, researchers hope to develop strategies for intervention and treatment of tau-related neurodegenerative conditions, thus addressing a critical unmet need in the field of neuroscience.
