Analytical Data
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Gene name
uspA
- Application
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Alternative Names
uspA；Universal stress Protein A
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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
Q8Z268
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Expression Region
2-144aa
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AA Sequence
AYKHILIAVDLSPESKVLVEKAVSMARPYNAKISLIHVDVNYSDLYTGLI DVNLGDMQKRISKETHHALTELSTNAGYPITETLSGSGDLGQVLVDAIKK YDMDLVVCGHHQDFWSKLMSSARQLINTVHVDMLIVPLRDEEE
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Molecular Weight
19.9 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 USP (ubiquitin-specific protease) A, a family of cysteine proteases, has garnered significant attention in recent years due to its critical role in regulating cellular processes through the removal of ubiquitin from target proteins. Ubiquitination is a post-translational modification that controls protein stability, localization, and activity, influencing various biological functions such as cell cycle progression, apoptosis, and DNA repair. Dysregulation of USP enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and immune dysfunctions, making them promising targets for therapeutic interventions. Research has focused on the recombinant expression of USP A proteins to better understand their structure-function relationships and to develop small-molecule inhibitors. By generating these recombinant proteins, scientists aim to elucidate the mechanisms through which USP A modulates ubiquitin signaling pathways and to identify potential biomarkers for disease progression. Additionally, recombinant USP A proteins serve as valuable tools for high-throughput screening assays aimed at discovering novel pharmacological agents that can selectively inhibit aberrant USP activities in pathological conditions. Overall, the exploration of USP A through recombinant technology not only enhances our understanding of ubiquitin-mediated signaling but also paves the way for innovative treatment strategies in various diseases linked to protein homeostasis.
