Analytical Data
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Gene name
USP4
- Application
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Alternative Names
UNP; UNPH
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Species
Human
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Source
Baculovirus
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Tag
His;Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13107-1
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Expression Region
A2-N963
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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
USP4 (Ubiquitin Specific Peptidase 4) 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. The importance of USP4 lies in its involvement in various signaling pathways, including those related to inflammation, stress responses, and cancer progression. Research has shown that USP4 can modulate the stability and activity of several key proteins, thereby influencing cell proliferation, apoptosis, and differentiation. Its dysregulation has been implicated in several diseases, particularly cancer, making it a potential therapeutic target. As a result, the study of recombinant USP4 protein has gained significant interest, providing a valuable tool for elucidating its biological functions and mechanisms of action. Understanding the structure and function of USP4 can also aid in the development of novel inhibitors that can selectively disrupt its activity, offering a promising avenue for cancer treatment and other pathologies associated with ubiquitin-mediated processes. Furthermore, the characterization of USP4's interactions with other proteins and its role in the ubiquitin-proteasome system can enhance our understanding of complex cellular networks and contribute to the advancement of targeted therapies in oncology.
