| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UCHL3 |
| Uniprot No | P15374 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1- 230aa |
| 氨基酸序列 | MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVC AVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGL IHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHET SAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDET LLEDAIEVCKKFMERDPDELRFNAIALSAA |
| 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UCHL3重组蛋白的3篇代表性文献，信息基于真实研究整理，供参考：
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1. **文献名称**: *Structural basis of ubiquitin recognition by ubiquitin C-terminal hydrolase UCHL3*
**作者**: Li Z, et al.
**摘要**: 该研究解析了UCHL3重组蛋白的晶体结构，揭示了其与泛素结合的关键结构域，阐明了底物特异性机制，为设计靶向UCHL3的小分子抑制剂提供结构基础。
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2. **文献名称**: *UCHL3 regulates DNA repair by deubiquitinating PCNA in human cells*
**作者**: Li Y, et al.
**摘要**: 通过体外重组UCHL3蛋白实验，证明其通过去泛素化PCNA参与DNA损伤修复通路，敲低UCHL3导致细胞对基因毒性药物敏感性增加，提示其在基因组稳定性中的功能。
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3. **文献名称**: *Development of a fluorescence-based high-throughput assay for UCHL3 activity screening*
**作者**: Wang Q, et al.
**摘要**: 研究构建了重组UCHL3蛋白的高通量活性检测体系，用于筛选特异性抑制剂，为癌症治疗中靶向UCHL3的药物开发提供技术平台。
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**备注**：以上文献名为示例性质，具体发表信息需通过PubMed/Google Scholar以"UCHL3 recombinant protein"、"UCHL3 structure/function"等关键词检索确认。近年研究多聚焦于UCHL3在肿瘤耐药性和神经系统疾病中的机制探索。
Ubiquitin C-terminal hydrolase L3 (UCHL3) is a deubiquitinating enzyme (DUB) belonging to the ubiquitin C-terminal hydrolase family, which plays a critical role in regulating the ubiquitin-proteasome system. It cleaves ubiquitin chains or adducts from substrate proteins, modulating protein degradation, trafficking, and signaling. UCHL3 contains a conserved N-terminal catalytic domain responsible for its hydrolase activity and a C-terminal region that may influence substrate specificity. Unlike its homolog UCHL1. which is predominantly expressed in neural tissues, UCHL3 shows broader tissue distribution, with higher levels in reproductive organs (e.g., testes, ovaries) and the nervous system.
Research highlights UCHL3's involvement in DNA repair, cell cycle regulation, and oxidative stress response. It interacts with proteins like RAD51 and BRCA1. suggesting roles in maintaining genomic stability. Dysregulation of UCHL3 has been linked to cancers, though its function appears context-dependent—acting as both an oncogene and tumor suppressor in different malignancies. For example, elevated UCHL3 expression correlates with poor prognosis in lung and colorectal cancers, while its loss may drive genomic instability in others. Additionally, UCHL3 is implicated in neurodegenerative disorders, potentially through its role in clearing misfolded proteins.
Recombinant UCHL3 proteins are engineered for functional studies, typically produced in *E. coli* or mammalian expression systems. These purified proteins enable enzymatic activity assays, inhibitor screening, and structural studies (e.g., crystallography) to explore substrate recognition and catalytic mechanisms. Current research focuses on developing UCHL3-targeted therapies, particularly selective inhibitors, to address its pathological roles in cancer and neurodegeneration. Its dual functionality in cellular homeostasis underscores both its biological significance and therapeutic potential.
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