| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | UCHL4 |
| Uniprot No | P58321 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-233aa |
| 氨基酸序列 | MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMESE LLSIIPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGT IGLIHAIANN KDKVHFESGS TLKKFLEESV SMSPEERAKY LENYDAIRVT HETSAHEGQT EAPSIDEKVD LHFIALVHVD GHLYELDGWK PFPINHGKTS DETLLEDVIK VCKKFMERDP DELRFNAIAL SAA |
| 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UCHL4重组蛋白的示例参考文献(**注：因UCHL4研究较少，以下为假设性示例，实际文献需通过学术数据库验证**)：
1. **文献名称**: "Cloning, Expression, and Functional Characterization of Recombinant UCHL4 Deubiquitinating Enzyme"
**作者**: Zhang Y, et al.
**摘要**: 本研究报道了人源UCHL4基因的克隆及在大肠杆菌中的重组表达，通过亲和层析纯化获得高纯度蛋白。酶活性分析表明，重组UCHL4对K48-linked多聚泛素链具有特异性水解活性，提示其在蛋白酶体途径中的潜在作用。
2. **文献名称**: "Structural Insights into UCHL4 Substrate Specificity via Crystallographic Analysis"
**作者**: Thompson R, et al.
**摘要**: 通过X射线晶体学解析了UCHL4重组蛋白的三维结构，揭示了其催化口袋的关键氨基酸残基。实验表明，UCHL4对长链泛素底物的结合依赖于C端螺旋区域的构象变化，为设计靶向抑制剂提供了结构基础。
3. **文献名称**: "UCHL4 Regulates Mitochondrial Function via Modulating Parkin Ubiquitination in Neuronal Cells"
**作者**: Lee S, et al.
**摘要**: 研究利用重组UCHL4蛋白验证其在神经元线粒体质量控制中的作用。过表达UCHL4可增强Parkin的泛素化修饰，促进受损线粒体清除，提示UCHL4可能参与神经退行性疾病的病理机制。
**建议**：实际研究中请通过PubMed、Google Scholar等平台，以关键词“UCHL4 recombinant”“UCHL4 deubiquitinase”检索最新文献，或结合UniProt数据库(ID: Q9Y5K5)获取相关研究线索。
**Background of UCHL4 Recombinant Protein**
UCHL4 (Ubiquitin C-terminal Hydrolase L4), a member of the ubiquitin C-terminal hydrolase (UCH) family, is a deubiquitinating enzyme (DUB) involved in the regulation of protein turnover and cellular signaling. UCH enzymes catalyze the cleavage of ubiquitin precursors or polyubiquitin chains, modulating substrate stability, localization, or activity within the ubiquitin-proteasome system (UPS). UCHL4 is characterized by its conserved catalytic domain, which enables hydrolytic activity toward ubiquitin adducts. While its biological roles remain less explored compared to other UCH isoforms (e.g., UCHL1 or UCHL3), studies suggest UCHL4 participates in diverse processes, including immune response regulation, DNA repair, and cell cycle control. Dysregulation of UCHL4 has been implicated in pathological conditions such as cancer and neurodegenerative disorders, highlighting its therapeutic potential.
Recombinant UCHL4 protein is produced via genetic engineering, typically using *E. coli* or mammalian expression systems, to ensure high purity and functional integrity. This engineered protein retains enzymatic activity, making it a vital tool for *in vitro* studies, including substrate identification, enzymatic kinetics, and interaction profiling. Researchers leverage recombinant UCHL4 to investigate its role in ubiquitin dynamics, particularly its preference for specific ubiquitin linkages (e.g., K48 or K63) and its interplay with regulatory proteins. Additionally, it serves as a reagent for screening small-molecule inhibitors or activators, aiding drug discovery efforts targeting UPS-related diseases.
The development of UCHL4 recombinant protein has advanced mechanistic insights into deubiquitination processes, offering a platform to dissect its physiological and pathological relevance. Ongoing research aims to clarify its tissue-specific functions, post-translational modifications, and potential as a biomarker or therapeutic target. As the interplay between ubiquitination and cellular homeostasis gains attention, UCHL4 remains a focal point for understanding disease mechanisms and developing precision therapies.
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