Analytical Data
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基因名
USP3
- Application
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生物活性
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.
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种属
Human
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表达系统
Baculovirus
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标签
N-GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y6I4-1
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表达区间
E2-L520
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蛋白长度
Partial
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分子量
85.4 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
