Analytical Data
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Gene name
FAU
- Application
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Alternative Names
FAU；Ubiquitin-like FUBI-ribosomal Protein eS30 fusion Protein
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Species
Human
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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
P62861
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Expression Region
1-133aa
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AA Sequence
MQLFVRAQELHTFEVTGQETVAQIKAHVASLEGIAPEDQVVLLAGAPLEDEATLGQCGVEALTTLEVAGRMLGGKVHGSLARAGKVRGQTPKVAKQEKKKKKTGRAKRRMQYNRRFVNVVPTFGKKKGPNANS
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Molecular Weight
14.3 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
FAU (Fused Atrophy Ubiquitin) is a crucial protein involved in various cellular processes, particularly in the regulation of protein synthesis, cellular stress response, and apoptosis. Its role in cancer and other diseases has garnered significant attention in recent years. Researchers have been investigating FAU's function and potential as a therapeutic target due to its involvement in the regulation of key pathways associated with cellular homeostasis and survival. The increased understanding of FAU's structure and function, facilitated by advances in recombinant protein technology, has led to the development of studies focusing on the protein’s interaction with other molecular players in the cell. By utilizing recombinant DNA technology, scientists are able to produce FAU in a controlled environment, allowing for detailed analysis of its biochemical properties and potential applications in therapy. The insights gained from these studies not only enhance our understanding of fundamental biological processes but also open new avenues for targeted drug development and therapeutic interventions that can exploit the dysregulation of FAU in various diseases. As a result, FAU has emerged as a focus of interest in molecular biology and medicine, positioning it as a promising candidate for innovative therapeutic approaches.
