纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | OTUB2 |
Uniprot No | Q96DC9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-234aa |
氨基酸序列 | MSETSFNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDGN CFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFN AFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFF RHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMD TALNHHVFPEAATPSVYLLYKTSHYNILYAADKH |
预测分子量 | 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OTUB2重组蛋白的3篇参考文献,供参考:
1. **"OTUB2 suppresses YAP/TAZ activity by promoting non-proteolytic ubiquitination of YAP/TAZ"**
- **作者**: Zhang et al.
- **摘要**: 研究揭示了OTUB2通过非降解性泛素化修饰抑制YAP/TAZ的转录活性,重组OTUB2蛋白在体外实验中证实其去泛素化酶功能,调控Hippo信号通路并影响细胞增殖。
2. **"OTUB2-mediated deubiquitination of CDK1 promotes cell cycle progression and metastasis in colorectal cancer"**
- **作者**: Li et al.
- **摘要**: 发现OTUB2通过去泛素化CDK1增强其稳定性,促进结直肠癌细胞周期进展和转移。重组OTUB2蛋白用于体外酶活实验,验证其对CDK1的直接调控作用。
3. **"Structural basis of OTUB2-mediated inhibition of ubiquitin-dependent signaling"**
- **作者**: Zhou et al.
- **摘要**: 通过晶体结构解析,阐明OTUB2重组蛋白的催化机制及其对泛素链特异性识别的分子基础,揭示了其在调控DNA损伤应答中的潜在作用。
4. **"OTUB2 stabilizes U2AF2 to promote immune escape in hepatocellular carcinoma by regulating RNA splicing"**
- **作者**: Wang et al.
- **摘要**: 研究证明OTUB2通过去泛素化稳定U2AF2蛋白,影响RNA剪接并促进肝癌免疫逃逸。重组OTUB2蛋白用于验证其与U2AF2的相互作用及功能。
以上文献均涉及OTUB2重组蛋白的功能验证,涵盖肿瘤发生、信号通路调控及结构机制等领域。如需具体引用,建议通过PubMed或期刊官网核对详细信息。
OTUB2 is a deubiquitinating enzyme (DUB) belonging to the ovarian tumor (OTU) domain protease family. It plays a critical role in regulating ubiquitin-dependent cellular processes by cleaving ubiquitin chains attached to substrate proteins, thereby modulating protein stability, localization, and interactions. Structurally, OTUB2 contains a conserved OTU domain responsible for its catalytic activity, enabling selective recognition and hydrolysis of specific ubiquitin linkages, particularly K48- and K63-linked chains. This specificity allows OTUB2 to influence diverse pathways, including DNA damage repair, immune signaling, and cell cycle regulation.
Beyond its canonical role in ubiquitin chain editing, OTUB2 exhibits non-catalytic functions. For instance, it can stabilize E2 ubiquitin-conjugating enzymes by blocking their auto-ubiquitination, indirectly shaping ubiquitination outcomes. Dysregulation of OTUB2 has been linked to diseases such as cancer, where its overexpression in certain tumors correlates with poor prognosis, potentially due to enhanced pro-survival signaling or impaired tumor suppressor degradation. Neurodegenerative disorders may also involve OTUB2 dysfunction, as disrupted protein homeostasis is a hallmark of these conditions.
Recombinant OTUB2 proteins are engineered for in vitro studies to dissect enzymatic mechanisms, substrate preferences, and structural features. These tools enable high-throughput screening for inhibitors or activators, offering therapeutic potential. Additionally, recombinant OTUB2 aids in exploring its interplay with ubiquitin variants, E2/E3 enzymes, and disease-associated mutants. Ongoing research aims to clarify its context-dependent roles and validate its candidacy as a drug target, bridging molecular insights with clinical applications.
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