Analytical Data
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Gene name
FRAT1
- Application
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Alternative Names
FRAT1Proto-oncogene FRAT1; Frequently rearranged in advanced T-cell lymphomas 1; FRAT-1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92837
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Expression Region
1-279aa
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AA Sequence
MPCRREEEEE AGEEAEGEEE EEDSFLLLQQ SVALGSSGEV DRLVAQIGET LQLDAAQHSP ASPCGPPGAP LRAPGPLAAA VPADKARSPA VPLLLPPALA ETVGPAPPGV LRCALGDRGR VRGRAAPYCV AELATGPSAL SPLPPQADLD GPPGAGKQGI PQPLSGPCRR GWLRGAAASR RLQQRRGSQP ETRTGDDDPH RLLQQLVLSG NLIKEAVRRL HSRRLQLRAK LPQRPLLGPL SAPVHEPPSP RSPRAACSDP GASGRAQLRT GDGVLVPGS
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Molecular Weight
29.0 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
FRAT1 (Frat Associated Protein 1) is a crucial component in the Wnt signaling pathway, which plays a significant role in cell proliferation, differentiation, and development. Dysregulation of this pathway has been implicated in various diseases, including cancer, making FRAT1 a potential target for therapeutic intervention. Research has shown that FRAT1 functions as a key regulator, stabilizing β-catenin and promoting Wnt target gene expression. The understanding of FRAT1's structure and interactions at the molecular level is essential for developing novel strategies to modulate its activity. Recombinant FRAT1 proteins are crucial for studying its biological functions, interactions with other proteins, and potential as a drug target. Producing and characterizing FRAT1 recombinant proteins enables researchers to investigate its role in pathological conditions and assess the effects of small molecules on Wnt signaling. Additionally, gaining insights into the mechanisms of FRAT1’s action may provide valuable information for designing inhibitors or activators that could be utilized in clinical settings. Continued research on FRAT1 and its associated pathways holds promise for innovative approaches in cancer therapy and regenerative medicine.











