Analytical Data
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Gene name
USP8
- Application
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Alternative Names
HumORF8; UBPY; Ubiquitin Carboxyl-Terminal Hydrolase 8; Ubiquitin Specific Protease 8; Deubiquitinating enzyme 8; Ubiquitin isopeptidase Y; Ubiquitin thioesterase 8
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P40818
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Expression Region
Thr777~Thr1118
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Molecular Weight
43kDa
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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
USP8 (Ubiquitin-Specific Protease 8) is an important deubiquitinating enzyme that plays a pivotal role in the regulation of various cellular processes by removing ubiquitin moieties from target proteins, thus controlling their stability and activity. Dysregulation of USP8 has been linked to various diseases, including cancers and neurodegenerative disorders. As a result, understanding its structure and function is crucial for elucidating its biological roles and potential as a therapeutic target. Recent research has revealed that USP8 is involved in key signaling pathways, including those governing cell cycle progression and apoptosis, while mutations in the USP8 gene have been associated with Cushing's disease, a condition characterized by excessive cortisol production. The expression and activity of USP8 can be influenced by various factors, including post-translational modifications and protein-protein interactions, making it a complex but fascinating subject of study. The recombination and purification of USP8 protein for functional assays and structural studies are essential for advancing our knowledge of its mechanisms. Investigating the enzymatic activity of USP8 and its impact on substrate proteins can provide insights into how its dysregulation contributes to disease pathogenesis and may guide the development of novel therapeutic strategies. In light of its significance, ongoing research aims to elucidate the molecular mechanisms underlying USP8's functions, offering the potential for innovative approaches to modulate its activity in disease contexts.
