Analytical Data
-
Gene name
USP3
- Application
-
Biological Activity
The fundamental role of USP3 is specific removal of ubiquitin from substrates. USP3 catalyses the ubiquitin from the substrate Ub-Rho110 to release fluorophores. Rho110 will release 535nM emission light under the excitation condition of 485nM. The signal of which can be quickly and reliably captured using a microplate reader. The concentration of USP3 used is 1.5 nM, and the reaction lasts for 30 minutes. Under these conditions, the signal-to-noise ratio (S/N) of the signal box is greater than or equal to 10.
-
Species
Human
-
Source
Baculovirus
-
Tag
N-GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y6I4-1
-
Expression Region
E2-L520
-
Protein Length
Partial
-
Molecular Weight
85.4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
USP3 (Ubiquitin Specific Peptidase 3) is a deubiquitinating enzyme that plays a crucial role in regulating various cellular processes by removing ubiquitin moieties from target proteins, thereby influencing their stability, localization, and function. Research on USP3 has gained momentum due to its involvement in critical biological pathways, including cell cycle regulation, DNA damage response, and signal transduction. Dysregulation of USP3 has been linked to several diseases, including cancer, neurodegenerative disorders, and viral infections. The potential therapeutic implications of modulating USP3 activity have sparked interest in its biomedical applications. Despite its significance, the structural and functional characterization of USP3 has been limited. The generation of recombinant USP3 protein provides a valuable tool for understanding its biochemical properties, substrate specificity, and mechanism of action. Studies utilizing recombinant USP3 can elucidate its role in cellular contexts, offer insights into its interactions with other cellular proteins, and pave the way for the development of small molecule inhibitors that could target aberrantly elevated USP3 activity in pathologies. Thus, the exploration of USP3 through recombinant protein research embodies a promising avenue for advancing our understanding of ubiquitin-mediated regulation in health and disease.
