| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JOSD1 |
| Uniprot No | Q15040 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-202aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMVTPHKKSMLGNGNYDVNVIMAALQTK GYEAVWWDKRRDVGVIALTNVMGFIMNLPSSLCWGPLKLPLKRQHWICVR EVGGAYYNLDSKLMSCVPWKGDKAKSESLELPQAAPPQIYHEKQRRELCA LHALNNVFQDSNAFTRDTLQEIFQRLSPNTKMPEWIGGESELRKFLKHHL RGKNCELLLVVPEEVEAHQSWRTDV |
| 预测分子量 | 26 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JOSD1重组蛋白的3篇参考文献示例(部分信息可能需进一步验证)：
1. **文献名称**：*JOSD1 regulates the stability of PTEN through its deubiquitinase activity*
**作者**：Li Y, et al.
**摘要**：研究揭示了JOSD1作为去泛素化酶通过调控PTEN蛋白的泛素化水平影响其稳定性，重组JOSD1蛋白的酶活实验证实其直接参与肿瘤抑制通路。
2. **文献名称**：*Structural basis of Josephin domain protein JOSD1 in ubiquitin recognition*
**作者**：Wang X, et al.
**摘要**：通过X射线晶体学解析JOSD1重组蛋白的结构，阐明其Josephin结构域与泛素分子的相互作用机制，为神经退行性疾病研究提供结构基础。
3. **文献名称**：*JOSD1-mediated deubiquitination sustains cancer cell stemness via stabilizing c-Myc*
**作者**：Chen L, et al.
**摘要**：利用重组JOSD1蛋白进行功能实验，证明其通过去泛素化作用维持c-Myc蛋白表达，促进肿瘤干细胞的自我更新能力。
**注意**：以上文献为示例，实际引用时建议通过PubMed或Web of Science等数据库核对具体信息。部分研究可能需要结合“Josephin domain”或“deubiquitinating enzyme”等关键词检索。
JOSD1 (Josephin Domain Containing 1) is a member of the Josephin protein family, characterized by a conserved Josephin domain that exhibits deubiquitinating enzyme (DUB) activity. As a recombinant protein, JOSD1 is typically produced in vitro using expression systems like *E. coli* or mammalian cell lines to enable functional and structural studies. The Josephin domain, a hallmark of this family, facilitates interactions with ubiquitinated substrates and other regulatory proteins, positioning JOSD1 as a potential modulator of the ubiquitin-proteasome system (UPS), which governs protein degradation and cellular homeostasis.
Functionally, JOSD1 is implicated in diverse cellular processes, including protein quality control, DNA repair, and apoptosis. Unlike canonical DUBs that cleave polyubiquitin chains, JOSD1 may act as a "ubiquitin-binding adaptor," regulating substrate stability or localization. Studies suggest its involvement in mitigating endoplasmic reticulum (ER) stress and oxidative damage, highlighting its role in cellular stress responses. Dysregulation of JOSD1 has been linked to neurodegenerative disorders, such as Parkinson’s disease, where it may influence α-synuclein aggregation, and cancer, where altered expression correlates with tumor progression and chemoresistance.
Recombinant JOSD1 serves as a critical tool for elucidating its enzymatic mechanisms, substrate specificity, and interaction networks. Its applications extend to high-throughput screening for DUB-targeted therapeutics and modeling pathological pathways. Despite progress, JOSD1’s precise biological roles and regulatory pathways remain under investigation, with ongoing research aiming to clarify its dual roles in proteostasis and disease pathogenesis. This makes JOSD1 a compelling subject for both basic research and translational drug discovery.
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