Analytical Data
-
基因名
USP29
-
简介
USP29 protein, as a deubiquitinating enzyme, plays a crucial role in innate antiviral immunity by mediating "Lys-48" deubiquitination of CGAS. This effect stabilizes CGAS, an important sensor of the cellular response to viral infection, emphasizing the importance of USP29 in regulating CGAS activity. USP29 Protein, Human (sf9, FLAG) is the recombinant human-derived USP29 protein, expressed by sf9 insect cells , with N-Flag labeled tag.
- Application
-
别名
USP29; Ubiquitin carboxyl-terminal hydrolase 29; Deubiquitinating enzyme 29; Ubiquitin thioesterase 29; Ubiquitin-specific-processing protease 29
-
种属
Human
-
表达系统
Baculovirus
-
标签
N-Flag
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q9HBJ7
-
表达区间
I2-A922
-
蛋白长度
Partial
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
USP29, a member of the ubiquitin-specific protease (USP) family, plays a crucial role in regulating the ubiquitin-proteasome system, which is vital for maintaining cellular homeostasis and regulating various biological processes. The dysregulation of this system is often linked to numerous diseases, including cancer, neurodegenerative disorders, and immune diseases. Recent studies have indicated that USP29 is involved in modulating key signaling pathways, such as those related to tumor suppression and inflammation. By deubiquitinating specific substrate proteins, USP29 can alter their stability and activity, thus influencing cellular responses to stress and promoting cell survival. Furthermore, emerging evidence suggests that USP29 has potential as a therapeutic target, as manipulating its activity may restore normal cellular functions in disease contexts. These insights into USP29's molecular mechanisms have propelled research into its structural properties and interactions with substrates, paving the way for potential drug development aimed at targeting aberrant USP29 activity in various pathologies. The study of USP29 recombinant proteins not only enhances our understanding of its biological functions but also provides valuable tools for pharmacological interventions that could lead to novel treatments for diseases associated with USP dysregulation.
