Analytical Data
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Gene name
TAF15
- Application
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Alternative Names
TAF15；RBP56；TATA-binding Protein-associated factor 2N
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
148-406aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSSYHSQRE NYSHHTQDDR RDVSRYGEDN RGYGGSQGGG RGRGGYDKDG RGPMTGSSGG DRGGFKNFGG HRDYGPRTDA DSESDNSDNN TIFVQGLGEG VSTDQVGEFF KQIGIIKTNK KTGKPMINLY TDKDTGKPKG EATVSFDDPP SAKAAIDWFD GKEFHGNIIK VSFATRRPEF MRGGGSGGGR RGRGGYRGRG GFQGRGGDPK SGDWVCPNPS CGNMNFARRN SCNQCNEPRP EDSRPSGGDF RGRGYGGERG YR
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Molecular Weight
30 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
Related Products
Protein Description
TAF15 (Tat-interactive protein 15) is a member of the FUS/TLS family of RNA-binding proteins, playing crucial roles in diverse cellular processes such as transcription regulation, RNA processing, and stress response. It has garnered significant attention in recent years due to its involvement in various neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), where pathological aggregation of TAF15 is observed. Research has highlighted the significance of TAF15’s RNA-binding capabilities and its capacity to modulate gene expression by interacting with specific RNA sequences. The study of recombinant TAF15 proteins allows scientists to elucidate the structure-function relationship of this protein and the mechanisms underlying its aggregation in disease states. Furthermore, understanding the dynamics of TAF15 in different cellular environments can help identify potential therapeutic targets for the aforementioned conditions. Given the growing evidence linking TAF15 dysregulation to neurodegeneration, ongoing research aims to characterize its conformational states, binding interactions, and post-translational modifications, paving the way for developing interventions that may alleviate or counteract the detrimental effects associated with TAF15 aggregation. This includes exploring its role in cellular stress responses and how its dysfunction might contribute to pathological processes, thereby broadening our understanding of the molecular underpinnings of neurodegenerative diseases. Overall, TAF15 serves as an important model for studying RNA-binding proteins and their implications in health and disease.
