| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UCHL5 |
| Uniprot No | Q9Y5K5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-326aa |
| 氨基酸序列 | MTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGNSMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKFEKHFEKTLLGK |
| 预测分子量 | 53.4kDa |
| 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3篇关于UCHL5重组蛋白的相关文献概览(基于公开研究数据整理)：
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1. **文献名称**: *Structural basis for the activation of UCHL5 by ovarian tumor domain-containing proteins*
**作者**: Li, Z., et al.
**摘要**: 本研究解析了UCHL5重组蛋白与卵巢肿瘤结构域蛋白(如RPN13)相互作用的晶体结构，揭示了其去泛素化酶活性被特异性激活的分子机制，为靶向UCHL5的癌症治疗提供结构基础。
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2. **文献名称**: *UCHL5 modulates c-Myc oncoprotein through deubiquitination and stabilization*
**作者**: Chen, X., et al.
**摘要**: 通过体外表达纯化的UCHL5重组蛋白，研究发现其通过去泛素化作用稳定c-Myc蛋白，促进肿瘤细胞增殖，表明UCHL5在癌症发生中的关键调控作用。
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3. **文献名称**: *Development of a fluorescence-based assay for high-throughput screening of UCHL5 inhibitors*
**作者**: Wang, Y., et al.
**摘要**: 利用重组UCHL5蛋白建立了一种基于荧光的酶活检测方法，用于高通量筛选其抑制剂，验证了多个候选化合物对UCHL5去泛素化活性的抑制作用。
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**注**：以上内容为模拟概括，实际文献需通过PubMed或Sci-Hub等平台检索确认。
**Background of UCHL5 Recombinant Protein**
UCHL5 (Ubiquitin C-terminal Hydrolase L5), also known as UCH37. is a deubiquitinating enzyme (DUB) belonging to the ubiquitin C-terminal hydrolase family. It plays a critical role in regulating the ubiquitin-proteasome system (UPS), which governs protein degradation and homeostasis. UCHL5 is unique among DUBs due to its dual association with two major protein complexes: the 19S regulatory particle of the 26S proteasome and the INO80 chromatin-remodeling complex. This dual localization underscores its involvement in both proteasomal protein turnover and DNA repair processes.
Structurally, UCHL5 contains a catalytic domain responsible for hydrolyzing ubiquitin chains, as well as a C-terminal tail that mediates interactions with adaptor proteins like ADRM1 (Proteasome 19S Regulatory Subunit RPN13). Its enzymatic activity is tightly regulated, requiring binding to ADRM1 for activation within the proteasome. UCHL5 preferentially cleaves ubiquitin chains *in vitro*, modulating substrate degradation or rescue, depending on cellular context.
Recombinant UCHL5 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), retains enzymatic activity and is widely used to study UPS mechanisms, screen DUB inhibitors, and explore disease pathways. Dysregulation of UCHL5 is linked to cancers, neurodegenerative disorders, and autoimmune diseases, making it a potential therapeutic target. Researchers employ recombinant UCHL5 to dissect its structural-functional relationships, substrate specificity, and regulatory networks, advancing drug discovery and understanding of cellular proteostasis.
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