Analytical Data
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Gene name
FBXO4
- Application
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Alternative Names
/
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UKT5
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Expression Region
1-387aa
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Molecular Weight
48.2 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
FBXO4, a member of the F-box protein family, plays a crucial role in the ubiquitin-proteasome system, which is essential for protein degradation and regulation of various cellular processes. Studies have shown that FBXO4 functions as an E3 ubiquitin ligase, facilitating the ubiquitination of target proteins and thus influencing cell cycle regulation, apoptosis, and cellular signaling pathways. Its involvement in the degradation of specific substrates has garnered attention in the context of cancer biology, particularly due to its potential roles in tumor suppression and modulation of oncogenic pathways. Recent research has indicated that FBXO4 may have therapeutic implications, particularly in targeting malignant cells. The reconstitution of FBXO4 as a recombinant protein is essential for characterizing its biochemical properties and understanding its interaction with substrates. By producing FBXO4 in a controlled environment, researchers can explore its molecular mechanisms, identify binding partners, and evaluate its potential as a therapeutic target. The study of FBXO4 in recombinant form aims to elucidate its role in cellular homeostasis and its contributions to disease states, paving the way for innovative approaches in cancer treatment and other disorders associated with dysregulated protein degradation.
