Analytical Data
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Gene name
USP2
- Application
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Biological Activity
The fundamental role of USP2 is specific removal of ubiquitin from substrates. USP2 catalyses the ubiquitin from the substrate Ub-Rho110 to release fluorophores. Rho110 will release 535 nM emission light under the excitation condition of 485 nM. The signal of which can be quickly and reliably captured using a microplate reader.
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Alternative Names
USP2；UBP41；Ubiquitin carboxyl-terminal hydrolase 2
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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
O75604
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Expression Region
259-605aa
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Molecular Weight
40 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
Identification
Protein Description
USP2 (Ubiquitin-specific protease 2) is a member of the deubiquitinating enzyme family, which plays a crucial role in the regulation of cellular processes by removing ubiquitin moieties from target proteins. Ubiquitination is a post-translational modification that typically marks proteins for degradation via the proteasome, thus controlling protein levels and signaling pathways in the cell. Research into USP2 has gained momentum due to its involvement in various biological functions, including cell cycle regulation, DNA repair, and apoptosis, as well as its implications in cancer biology. Studies have shown that USP2 can stabilize several oncoproteins, such as MDM2 and cyclin D1, leading to enhanced tumorigenesis. Additionally, USP2 has been implicated in the modulation of immune responses and the pathogenesis of neurodegenerative diseases. The enzymatic activity and substrate specificity of USP2 make it a potential target for therapeutic intervention, particularly in cancer treatment, where its inhibition could restore the degradation of aberrant proteins. As a result, understanding the biochemical properties and regulatory mechanisms of USP2 through studies involving its recombinant protein is essential. Researchers have focused on expressing and purifying USP2 recombinant protein to elucidate its functions, interactions, and structural characteristics, providing valuable insights that could lead to the development of novel therapeutic strategies targeting this enzyme in various diseases.
