| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | USP45 |
| Uniprot No | Q70EL2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-289 aa |
| 活性数据 | MRVKDPTKALPEKAKRSKRPTVPHDEDSSDDIAVGLTCQHVSHAISVNHVKRAIAENLWSVCSECLEERRFYDGQLVLTSDIWLCLKCGFQGCGKNSESQHSLKHFKSSRTEPHCIIINLSTWIIWCYECDEKLSTHCNKKVLAQIVDFLQKHASKTQTSAFSRIMKLCEEKCETDEIQKGGKCRNLSVRGITNLGNTCFFNAVMQNLAQTYTLTDLMNEIKESSTKLKIFPSSDSQLDPLVVELSRPGPLTSALFLFLHSMKETEKGPLSPKVLFNQLCQKRVHLHLI |
| 分子量 | 59.1 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. |
以下为人工模拟的参考示例(注意：由于USP45研究较少，以下为假设性示例，建议通过PubMed等数据库验证真实文献)：
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1. **文献名称**: "Characterization of Recombinant Human USP45 and Its Role in DNA Repair"
**作者**: Smith J, et al.
**摘要**: 本研究利用大肠杆菌表达系统纯化了重组人USP45蛋白，发现其通过去泛素化RAD51蛋白增强DNA损伤修复能力，为癌症治疗提供潜在靶点。
2. **文献名称**: "USP45 Regulates Neuronal Apoptosis via p53 Signaling Pathway"
**作者**: Wang L, et al.
**摘要**: 在HEK293细胞中表达重组USP45.证实其通过调控p53泛素化水平抑制神经元凋亡，可能与阿尔茨海默病相关。
3. **文献名称**: "Development of a High-Yield USP45 Protein Production System in Insect Cells"
**作者**: Garcia R, et al.
**摘要**: 优化杆状病毒-昆虫细胞系统实现重组USP45的高效表达，纯化后酶活测定显示其对K48链泛素化底物具有特异性切割功能。
4. **文献名称**: "USP45 Interacts with BRCA1 in Breast Cancer Progression"
**作者**: Chen X, et al.
**摘要**: 通过哺乳动物细胞重组表达技术，发现USP45与BRCA1蛋白直接互作，调控乳腺癌细胞增殖迁移，提示其作为预后标志物的潜力。
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**建议**：使用PubMed、Web of Science等数据库，以“recombinant USP45”“USP45 protein function”为关键词检索最新文献，注意筛选影响因子较高的期刊以获取权威信息。
Ubiquitin-specific protease 45 (USP45) is a member of the deubiquitinating enzyme (DUB) family, which plays a critical role in regulating protein stability and cellular processes by cleaving ubiquitin tags from substrate proteins. As a cysteine protease, USP45 reverses ubiquitination—a post-translational modification that directs proteins for degradation or functional modulation. Unlike other USP family members, USP45 contains extended N-terminal regions that may mediate protein-protein interactions or subcellular localization, though its precise structural and functional features remain less characterized compared to well-studied DUBs.
Recombinant human USP45 protein is typically produced in vitro using expression systems like *E. coli* or mammalian cell lines, enabling researchers to study its enzymatic activity, substrate specificity, and biological roles. Dysregulation of DUBs, including USP45. has been implicated in diseases such as cancer and neurodegeneration, as improper ubiquitination can lead to pathogenic protein accumulation or loss of homeostasis. Emerging studies suggest USP45 may participate in DNA repair pathways and cellular stress responses, though its exact mechanisms and physiological substrates are still under investigation.
The development of recombinant USP45 facilitates biochemical assays, structural studies, and drug discovery efforts targeting DUB-related pathologies. However, further research is needed to clarify its regulatory networks, interaction partners, and therapeutic potential in human diseases.
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