Analytical Data
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Gene name
UfSP1
- Application
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Alternative Names
Ufm1-specific protease 1; UFSP1; Homo sapiens; Human; Hydrolase; Protease; Thiol protease
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6NVU6
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Expression Region
M1-D142
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Protein Length
Partial
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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
UfSP1 is a recently identified member of the ubiquitin-specific protease (USP) family, which plays a critical role in protein homeostasis by regulating ubiquitination processes. Ubiquitination is a post-translational modification that tags proteins for degradation, thereby influencing cellular processes such as cell cycle regulation, DNA repair, and signal transduction. The dysfunction of USP enzymes has been implicated in various diseases, including cancer and neurodegenerative disorders, making them promising targets for therapeutic intervention. Recent studies have highlighted that UfSP1 exhibits a unique substrate specificity and activity profile compared to other USPs, suggesting its potential involvement in specific cellular pathways. The characterization of UfSP1's structure and function is essential to elucidate its biological roles and potential as a drug target. Understanding the regulatory mechanisms governing UfSP1 activity may pave the way for novel therapeutic strategies to manipulate ubiquitin signaling in disease contexts. Given the increasing interest in the ubiquitin-proteasome system as a target for drug development, researching UfSP1 can provide valuable insights into the intricacies of cellular regulation and the development of new treatments.
