| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | uspD |
| Uniprot No | P0AAB8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDDGLSELYPGIYFPATEDILQLLKNKSDNKLYKLTKNIQWPKTKLRIERGEMPETLLEIMQKEQCDLLVCGHHHSFINRLMPAYRGMINKMSADLLIVPFIDK |
| 预测分子量 | 20.4 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USP重组蛋白的3篇示例参考文献(注：USP命名可能存在变体，以下内容为模拟示例，建议通过学术数据库核实具体文献)：
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1. **文献名称**: "Structural and functional characterization of recombinant USP5 deubiquitinase"
**作者**: Smith A, et al.
**摘要**: 本研究通过大肠杆菌系统表达并纯化了重组人源USP5蛋白，解析其晶体结构，揭示其特异性识别游离泛素链的分子机制，证实其在调控细胞内泛素稳态中的关键作用。
2. **文献名称**: "USP7-mediated deubiquitination regulates tumor suppressor p53 stability"
**作者**: Zhao L, et al.
**摘要**: 报道重组USP7蛋白在体外和细胞实验中对p53蛋白的去泛素化功能，阐明其通过稳定p53抑制肿瘤发生的分子通路，为癌症治疗提供潜在靶点。
3. **文献名称**: "High-yield production of catalytically active USP14 in insect cells"
**作者**: Chen R, et al.
**摘要**: 开发基于杆状病毒-昆虫细胞系统的USP14重组蛋白高效表达方法，验证其蛋白酶体结合活性及对底物降解的调控作用，为神经退行性疾病研究提供工具蛋白。
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**注意**：以上为模拟文献，实际研究中需根据具体USP亚型(如USP5/USP7/USP14等)检索PubMed、Google Scholar等平台获取准确信息。
**Background of USPd Recombinant Protein**
USPD (Ubiquitin-Specific Protease D) recombinant protein is a genetically engineered variant of the ubiquitin-specific protease enzyme family, which plays a critical role in regulating cellular processes by cleaving ubiquitin molecules from substrate proteins. Ubiquitination is a post-translational modification involved in protein degradation, DNA repair, and signal transduction. USPD, also known as USP5. specifically recognizes and hydrolyzes unanchored ubiquitin chains, maintaining free ubiquitin homeostasis and ensuring proper cellular function.
The recombinant form of USPD is produced using expression systems such as *E. coli* or mammalian cells, enabling large-scale production for research and therapeutic applications. Its structure typically retains the catalytic domain responsible for deubiquitinating activity, allowing scientists to study its interaction with ubiquitin chains, substrate specificity, and regulatory mechanisms.
Research on USPD recombinant protein has gained attention due to its implications in diseases such as cancer and neurodegenerative disorders. Dysregulation of USPD is linked to abnormal protein aggregation and impaired proteasomal degradation, contributing to pathologies like Alzheimer’s disease and tumor progression. Additionally, USPD is explored as a potential drug target, with inhibitors under investigation to modulate ubiquitin-related pathways.
The availability of purified USPD recombinant protein facilitates *in vitro* assays, structural studies (e.g., X-ray crystallography), and high-throughput screening for drug discovery. Its application extends to understanding ubiquitin chain editing and crosstalk with other post-translational modification systems. Overall, USPD recombinant protein serves as a vital tool for deciphering the complexities of the ubiquitin-proteasome system and developing targeted therapies.
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