Analytical Data
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Gene name
FAU
- Application
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Alternative Names
FAU; Ubiquitin-like protein FUBI
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
NM_001997
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Expression Region
1-133aa
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Molecular Weight
41.4 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
FAU (Factor Associated with HIV-1 Translation) is a protein that plays a critical role in the regulation of viral RNA translation and cellular stress responses. Initially identified as a factor that enhances the translation of HIV-1 mRNA, FAU has since been implicated in various cellular processes, including apoptosis and cell growth regulation. Research into FAU's structure and function has revealed its potential as a target for antiviral therapies, particularly in the context of HIV infection and other viral diseases. Given its multifaceted role, understanding the mechanisms by which FAU interacts with viral and host cell components could provide insights into the development of novel therapeutic strategies. Recent advances in recombinant protein technology have facilitated the production and purification of FAU, enabling further investigation into its functional domains and interaction partners. This research is crucial for unraveling the intricacies of viral pathogenesis and cellular responses, thus opening new avenues for the design of interventions that could disrupt the life cycle of HIV and enhance cellular resistance to viral infections.
