| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | USP15 |
| Uniprot No | Q9Y4E8-4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-235aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAEGGAADLDTQRSDIATLLKTSLRKG DTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQNVYPGPIDNSGLLKDGDAQ SLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVVEQGMFVKHC KVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKET RLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRGPSTP KKPLEQSC |
| 预测分子量 | 30 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USP15重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*USP15 regulates TGF-β signaling by deubiquitinating the type I TGF-β receptor*
**作者**：Inui, M. et al. (2011)
**摘要**：该研究利用USP15重组蛋白进行体外酶活实验，证明其通过去泛素化TGF-β受体I型(TβRI)增强TGF-β信号通路，揭示了USP15在肿瘤发生和纤维化中的潜在作用。
2. **文献名称**：*Structural basis of substrate specificity and deubiquitinating activity of USP15*
**作者**：Vlasschaert, C. et al. (2015)
**摘要**：通过表达并纯化USP15重组蛋白，结合X射线晶体学分析其催化结构域，阐明了USP15的底物识别机制及催化活性关键残基，为靶向USP15的药物设计提供结构基础。
3. **文献名称**：*USP15 interacts with the TAK1–TAB2/3 complex to modulate innate immune signaling*
**作者**：Eichhorn, P.J. et al. (2012)
**摘要**：研究通过重组USP15蛋白进行体外结合实验，发现其与TAK1-TAB2/3复合物相互作用，负调控NF-κB和MAPK信号通路，表明USP15在炎症和免疫应答中的调控作用。
4. **文献名称**：*USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy*
**作者**：Cornelissen, T. et al. (2014)
**摘要**：利用重组USP15蛋白及细胞模型，发现其通过去泛素化线粒体蛋白抑制Parkin介导的线粒体自噬，提示USP15在神经退行性疾病(如帕金森病)中的潜在病理机制。
这些文献涵盖了USP15重组蛋白在信号通路调控、结构解析及疾病机制中的关键研究。
USP15 (Ubiquitin-specific protease 15) is a deubiquitinating enzyme (DUB) belonging to the ubiquitin-specific protease family, which plays a critical role in regulating cellular processes by removing ubiquitin chains from target proteins. It is involved in maintaining protein homeostasis, modulating signal transduction pathways, and influencing DNA repair mechanisms. Structurally, USP15 contains a conserved catalytic domain responsible for its enzymatic activity, as well as N-terminal and C-terminal regulatory regions that mediate substrate recognition and interaction with binding partners.
Recombinant USP15 protein is engineered through molecular cloning techniques, typically expressed in mammalian or bacterial systems, and purified to high homogeneity for functional studies. This engineered protein retains the enzymatic activity of native USP15. enabling researchers to investigate its role in ubiquitin-dependent pathways such as TGF-β signaling, NF-κB activation, and Wnt/β-catenin regulation. USP15 has been implicated in diverse physiological and pathological contexts, including cancer progression, neurodegenerative diseases (e.g., Parkinson’s disease), and immune responses, where it exhibits both oncogenic and tumor-suppressive functions depending on cellular context.
Studies using recombinant USP15 have revealed its ability to deubiquitinate substrates like SMADs, KEAP1. and TRIM25. influencing processes such as autophagy, oxidative stress response, and viral immunity. Its dual role in stabilizing or degrading substrates underscores its regulatory complexity. Recombinant USP15 is widely utilized in biochemical assays, structural analyses, and drug discovery efforts aiming to develop selective DUB inhibitors. Understanding USP15's mechanisms may offer therapeutic opportunities for diseases linked to dysregulated ubiquitination, though its context-dependent functions necessitate careful target validation in specific pathological settings.
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