Analytical Data
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Gene name
USP52
- Application
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Alternative Names
KIAA0710; USP52
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Species
Human
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Source
Baculovirus
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Tag
His;GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q504Q3-1
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Expression Region
M486-R924
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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
USP52, a member of the ubiquitin-specific protease family, plays a crucial role in regulating protein degradation and cellular homeostasis by deubiquitinating target proteins. The dysregulation of deubiquitinases like USP52 has been implicated in various diseases, including cancer, neurodegenerative disorders, and immune dysfunctions. Research has shown that USP52 can influence critical cellular processes such as signal transduction, cell cycle progression, and apoptosis, making it a potential therapeutic target. Additionally, studies indicate that USP52 interacts with key signaling pathways, including the PI3K/Akt and NF-κB pathways, further emphasizing its importance in modulating cellular responses to stress and inflammation. Given its pivotal role in these physiological and pathological processes, understanding the mechanisms underlying USP52 function and regulation is essential for developing novel strategies for therapeutic intervention. Ongoing investigations into the structural and functional characterization of USP52, coupled with advancements in proteomic and genomic technologies, aim to delineate its specific substrates and regulatory mechanisms. This research not only contributes to the fundamental knowledge of ubiquitin-mediated signaling but also holds promise for identifying biomarkers and therapeutic targets in cancer and other diseases associated with aberrant ubiquitination.
