Analytical Data
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Gene name
uspF
- Application
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Alternative Names
uspF; ynaF; yzzL; b1376; JW1370Universal stress protein F
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P37903
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Expression Region
1-144aa
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Molecular Weight
32 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
The study of the USP family of proteins, particularly USP15, has garnered significant interest due to their critical roles in various cellular processes, including protein deubiquitination, cell signaling, and the regulation of apoptosis. Ubiquitination is a post-translational modification that typically tags proteins for degradation; thus, deubiquitinases like USP15 reverse this process, influencing protein stability and function. Dysregulation of USP proteins has been implicated in various diseases, including cancer, neurodegenerative disorders, and immune dysfunctions. USP15 is particularly noteworthy for its involvement in the NF-κB signaling pathway, which is crucial for inflammatory responses and has implications in tumorigenesis. Recombinant USP15 protein serves as a valuable tool for studying its enzymatic activity, substrate specificity, and interactions with other cellular proteins. By expressing and purifying USP15 as a recombinant protein, researchers can perform in-depth biochemical assays and structural analyses, leading to a better understanding of its function in health and disease. Investigating the mechanisms by which USP15 modulates protein interactions and signaling pathways could illuminate potential therapeutic targets for conditions driven by its dysregulation. Therefore, research focused on USP15 and its recombinant protein presents promising avenues for advancement in molecular biology and therapeutic development.
