Analytical Data
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Gene name
FBXO39
- Application
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Alternative Names
FBXO39; FBX39F-box only protein 39
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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
Q8N4B4
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Expression Region
1-442aa
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AA Sequence
MDEESELIQPQDQSCWAFLPDLCLCRVFWWLGDRDRSRAALVCRKWNQMMYSAELWRYRTITFSGRPSRVHASEVESAVWYVKKFGRYLEHLEVKFMNPYNAVLTKKFQVTMRGLLSCLSKSNNRLKSLSIQYLELDRLVWRNSIRSSFISSLSFFLKKMGKRLDYLNLKGARLTVEQGCQILDSLSYMRNENVISELNIEDYFSHHLAVYNSPQFKKTMSTFHNLVSLNLNYNCISDELLENLCENASTLRTINIKCHVHDPHGQVIWGMSWAKLARQATNLKVNFFFERIMKYERLARILLQEIPIRSISLRSCYFSDPDCSMRPTLIDLLPTFRHTLQKLTCEFNNNHESLDEELHLLIISCRKLFYFKIWAFLDVSFVERILKSQKERQCALRVFKARIYTNRYETNEEDKTLQEIYRKYRKLIESELSYFVIVYSVM
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Molecular Weight
74.14 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
FBXO39, a member of the F-box protein family, plays a pivotal role in the ubiquitin-proteasome system, which is crucial for regulating protein degradation and turnover in eukaryotic cells. The study of FBXO39 has gained importance due to its involvement in various biological processes, including cell cycle regulation, signal transduction, and the modulation of protein interactions. Dysregulation of FBXO39 expression has been implicated in several diseases, including cancer, where it may influence tumor progression and metastasis by affecting the stability of key regulatory proteins. Research has focused on the identification of substrates for FBXO39, elucidating its interacting partners, and understanding its mechanistic roles in cellular pathways. Advances in recombinant protein technologies have enabled the production of FBXO39 for in vitro studies, facilitating the exploration of its function and interactions at a molecular level. Furthermore, characterizing FBXO39’s structure and function may provide insights into its potential as a therapeutic target, as manipulating its activity could offer novel strategies for disease intervention. Thus, the investigation of FBXO39 and its recombinant protein form represents a promising frontier in understanding cellular dynamics and developing innovative therapeutic approaches.











