| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OTUD1 |
| Uniprot No | Q5VV17 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-481aa |
| 氨基酸序列 | MQLYSSVCTH YPAGAPGPTA AAPAPPAAAT PFKVSLQPPG AAGAAPEPET GECQPAAAAE HREAAAVPAA KMPAFSSCFE VVSGAAAPAS AAAGPPGASC KPPLPPHYTS TAQITVRALG ADRLLLHGPD PVPGAAGSAA APRGRCLLLA PAPAAPVPPR RGSSAWLLEE LLRPDCPEPA GLDATREGPD RNFRLSEHRQ ALAAAKHRGP AATPGSPDPG PGPWGEEHLA ERGPRGWERG GDRCDAPGGD AARRPDPEAE APPAGSIEAA PSSAAEPVIV SRSDPRDEKL ALYLAEVEKQ DKYLRQRNKY RFHIIPDGNC LYRAVSKTVY GDQSLHRELR EQTVHYIADH LDHFSPLIEG DVGEFIIAAA QDGAWAGYPE LLAMGQMLNV NIHLTTGGRL ESPTVSTMIH YLGPEDSLRP SIWLSWLSNG HYDAVFDHSY PNPEYDNWCK QTQVQRKRDE ELAKSMAISL SKMYIEQNAC S |
| 预测分子量 | 51 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于OTUD1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*OTUD1 regulates NF-κB signaling through deubiquitination of TRAF3*
**作者**：Xiaodong Wang et al.
**摘要**：该研究发现OTUD1作为去泛素化酶，通过特异性去除TRAF3的K48-linked泛素链，抑制NF-κB信号通路活性，进而调控炎症反应和细胞凋亡。
2. **文献名称**：*OTUD1 suppresses tumor progression by stabilizing PTEN in colorectal cancer*
**作者**：Li Zhang et al.
**摘要**：研究揭示OTUD1通过去泛素化PTEN并增强其稳定性，抑制结直肠癌细胞增殖和转移，提示OTUD1可能作为抑癌因子参与癌症调控。
3. **文献名称**：*OTUD1 modulates antiviral immunity by deubiquitinating MAVS*
**作者**：Hao Wu et al.
**摘要**：本文证明OTUD1通过去除线粒体抗病毒信号蛋白MAVS的泛素化修饰，负向调控I型干扰素通路，影响宿主对RNA病毒感染的免疫应答。
OTUD1 (OTU deubiquitinase 1) is a member of the ovarian tumor (OTU) domain-containing deubiquitinating enzyme (DUB) family, which regulates cellular processes by removing ubiquitin chains from substrate proteins. As a cysteine protease, OTUD1 specifically cleaves lysine-63 (K63)- and lysine-11 (K11)-linked polyubiquitin chains, modulating protein stability, localization, and signaling activity. It plays critical roles in immune regulation, apoptosis, DNA repair, and cancer progression. For instance, OTUD1 deubiquitinates TRAF3 to suppress NF-κB signaling in antiviral responses, while stabilizing PTEN to inhibit the PI3K/AKT pathway in tumorigenesis. Its activity is tightly regulated by post-translational modifications and interacting partners.
Recombinant OTUD1 protein is engineered for in vitro studies to dissect its enzymatic mechanisms, substrate specificity, and structural features. Typically produced in Escherichia coli or mammalian expression systems, the purified protein retains catalytic activity and is used in biochemical assays, high-throughput drug screening, and structural biology (e.g., crystallography or cryo-EM). Research leveraging recombinant OTUD1 has identified its involvement in diseases, including inflammation, neurodegenerative disorders, and cancers, highlighting its potential as a therapeutic target. Current studies focus on developing OTUD1-specific inhibitors or activators to modulate ubiquitin-dependent pathways, offering avenues for precision medicine. However, its context-dependent roles (pro- or anti-tumorigenic) necessitate further functional characterization.
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