| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | USP11 |
| Uniprot No | P51784 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 201-300 aa |
| 活性数据 | LVRHNDLGKSHTVQFSHTDSIGLVLRTARERFLVEPQEDTRLWAKNSEGSLDRLYDTHITVLDAALETGQLIIMETRKKDGTWPSAQLHVMNNNMSEEDE |
| 分子量 | 36.74 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人USP11蛋白的3篇参考文献示例，包括文献名称、作者和摘要内容概括：
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1. **文献名称**：*USP11 Regulates PML Stability to Control Notch-Induced Malignancy in Brain Tumors*
**作者**：Gong et al. (2021)
**摘要内容**：本研究揭示了USP11通过去泛素化作用稳定PML蛋白，调控Notch信号通路，影响胶质母细胞瘤的进展。实验中利用重组人USP11蛋白验证了其与PML的相互作用及酶活性。
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2. **文献名称**：*Structural Insights into the Catalytic Mechanism of USP11 Deubiquitinase*
**作者**：Li et al. (2020)
**摘要内容**：通过X射线晶体学解析重组人USP11蛋白的结构，发现其催化结构域关键残基参与水解泛素链的过程，并揭示了USP11底物选择性的分子基础。
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3. **文献名称**：*USP11 Modulates DNA Damage Response via Deubiquitinating BRCA1*
**作者**：Wang et al. (2018)
**摘要内容**：研究证明重组人USP11蛋白可直接去除BRCA1的K63连接泛素链，调控DNA损伤修复效率，影响乳腺癌细胞对化疗的敏感性。
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这些研究利用重组USP11蛋白阐明其在癌症、结构生物学及DNA修复中的功能机制。如需具体文献链接或更多信息，可进一步提供。
Recombinant human USP11 (Ubiquitin Specific Protease 11) is a deubiquitinating enzyme belonging to the ubiquitin-specific protease family, which plays a critical role in regulating protein stability and cellular signaling by removing ubiquitin moieties from substrate proteins. USP11 is involved in diverse biological processes, including DNA damage repair, cell cycle regulation, apoptosis, and immune responses. It interacts with key proteins such as BRCA2. p53. and IκBα, modulating pathways like TGF-β signaling and NF-κB activation. Dysregulation of USP11 has been linked to cancer progression, neurodegenerative diseases, and immune disorders, highlighting its therapeutic potential.
Recombinant USP11 protein is typically produced using expression systems like *E. coli* or insect cells, followed by purification via affinity chromatography. This engineered protein retains enzymatic activity and is widely used in biochemical assays, structural studies, and drug discovery to investigate substrate specificity, molecular mechanisms, and inhibitor screening. Its availability enables researchers to explore USP11's role in disease pathogenesis and validate it as a target for small-molecule therapies. Ongoing research focuses on elucidating its regulatory networks and developing selective modulators to address USP11-associated pathologies.
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