Analytical Data
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Gene name
USP2
- Application
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Alternative Names
UBP41; Ubiquitin carboxyl-terminal hydrolase 2; Ubiquitin Specific Protease 2; 41 kDa ubiquitin-specific protease; Deubiquitinating enzyme 2; Ubiquitin thioesterase 2
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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 95% as determined by SDS-PAGE.
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Uniprot
O75604
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Expression Region
Met1~Gly206
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Molecular Weight
25kDa
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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
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Protein Description
USP25, a member of the ubiquitin-specific protease (USP) family, plays a crucial role in the regulation of ubiquitination, a post-translational modification that influences protein stability, localization, and function. Understanding USP25's function is essential due to its involvement in various cellular processes, including cell cycle regulation, DNA repair, and immune response. Abnormal activity of USP25 has been implicated in several diseases, including cancer, where it can influence tumorigenesis by modulating the degradation of key regulatory proteins. Recent studies have identified USP25 as a potential therapeutic target, making the characterization of its structure and function critical for the development of novel interventions. The expression and purification of recombinant USP25 protein allow researchers to investigate its enzymatic activity and interactions with substrates and other proteins, providing insights into its biological roles and potential as a drug target. Investigating USP25's mechanisms and its impact on cellular pathways could aid in identifying biomarkers for disease progression and therapeutic responses, thus highlighting the importance of ongoing research in this area.











