Analytical Data
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Gene name
ubiF
- Application
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Alternative Names
ubiF；yleB；3-demethoxyubiquinol 3-hydroxylase
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Species
E.coli
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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
P75728
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Expression Region
1-391aa
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AA Sequence
MTNQPTEIAIVGGGMVGGALALGLAQHGFAVTVIEHAEPAPFVADSQPDVRISAISAASVSLLKGLGVWDAVQAMRCHPYRRLETWEWETAHVVFDAAELKLPLLGYMVENTVLQQALWQALEAHPKVTLRVPGSLIALHRHDDLQELELKGGEVIRAKLVIGADGANSQVRQMAGIGVHAWQYAQSCMLISVQCENDPGDSTWQQFTPDGPRAFLPLFDNWASLVWYDSPARIRQLQNMNMAQLQAEIAKHFPSRLGYVTPLAAGAFPLTRRHALQYVQPGLALVGDAAHTIHPLAGQGVNLGYRDVDALIDVLVNARSYGEAWASYPVLKRYQMRRMADNFIMQSGMDLFYAGFSNNLPPLRFMRNLGLMAAERAGVLKRQALKYALGL
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Molecular Weight
46.5 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
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Protein Description
The study of ubiquitin fusion proteins (ubiF) has garnered significant attention in the field of molecular biology due to their crucial role in various cellular processes. Ubiquitin, a small regulatory protein, is known for its involvement in tagging proteins for degradation via the proteasome, thus playing a vital role in maintaining cellular homeostasis, regulating cell cycle progression, and responding to stress. The ubiF family, characterized by the fusion of ubiquitin to other proteins, presents unique opportunities to explore the mechanisms underlying protein stability, degradation pathways, and the regulation of protein quality control. Research into ubiF proteins not only enhances our understanding of ubiquitin-mediated signaling pathways but also has implications for therapeutic interventions in diseases linked to protein misfolding and aggregation, such as neurodegenerative disorders. By investigating the structural and functional properties of ubiF proteins, scientists aim to unravel the complexities of cellular regulation and protein interactions, paving the way for innovative strategies in drug development and disease management.
