Analytical Data
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Gene name
TAF15
- Application
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Alternative Names
RBP56; TAF2N
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Species
Human
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92804
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Expression Region
S148-R406
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Protein Length
Partial
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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
TAF15 (TATA-binding protein-associated factor 15) is a member of the FUS/TLS (Fused in Sarcoma/Translocated in Liposarcoma) protein family, which plays a crucial role in various cellular processes, including transcription regulation, RNA metabolism, and stress response. Research on TAF15 has gained significant attention due to its involvement in several neurodegenerative diseases, such as Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD), where TAF15 aggregates in pathological cellular inclusions. Understanding TAF15 at the molecular level is critical for elucidating its function and its potential contributions to disease mechanisms. The study of recombinant TAF15 protein offers an invaluable tool for investigating its biochemical properties, functional domains, and interaction partners. By producing TAF15 in a recombinant system, researchers can analyze its oligomerization tendencies, post-translational modifications, and binding affinities with nucleic acids or other proteins, enriching our understanding of its role in cellular processes. Additionally, this research may inform therapeutic strategies aimed at mitigating the effects of protein misfolding and aggregation associated with neurodegeneration. Overall, TAF15 represents a pivotal focus in the intersection of basic and applied research within cellular and molecular biology, promising insights that could lead to novel interventions in managing neurodegenerative diseases.
