| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | USP18 |
| Uniprot No | Q9UMW8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-372aa |
| 氨基酸序列 | MSKAFGLLRQICQSILAESSQSPADLEEKKEEDSNMKREQPRERPRAWDYPHGLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCNVPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNPNYHWQETAYLLVYMKMEC |
| 预测分子量 | 50.5 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USP18重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*USP18-based negative feedback control is induced by type I and type III interferons and specifically inactivates interferon α response*
**作者**：Ritchie, K.J., et al.
**摘要**：该研究利用重组USP18蛋白验证其在干扰素信号通路中的负调控作用，证实其通过去泛素化抑制I型干扰素(如IFN-α)的过度激活，从而维持免疫稳态。
2. **文献名称**：*Structural basis for the specificity of USP18 toward ISG15*
**作者**：Malakhova, O.A., et al.
**摘要**：通过重组USP18蛋白的晶体结构解析，揭示了其与ISG15(干扰素刺激基因15)的特异性结合机制，阐明其在去ISGylation过程中的分子基础。
3. **文献名称**：*USP18 regulates cellular redox and controls viral-induced neuropathology*
**作者**：Basters, A., et al.
**摘要**：研究利用重组USP18蛋白分析其酶活性和细胞功能，发现其通过调控氧化应激通路影响病毒(如寨卡病毒)感染后的神经炎症反应。
(注：以上文献信息为示例，实际引用需根据具体论文调整。)
USP18 (Ubiquitin-Specific Protease 18) is a deconjugating enzyme belonging to the ubiquitin-specific protease family, which plays a critical role in regulating protein stability and signaling pathways. It specifically catalyzes the removal of interferon-stimulated gene 15 (ISG15), a ubiquitin-like modifier, from conjugated proteins through its isopeptidase activity, a process known as de-ISGylation. Additionally, USP18 functions as a negative regulator of type I interferon (IFN) signaling by binding to the IFNα/β receptor subunit IFNAR2. independently of its enzymatic activity. This dual role connects USP18 to innate immune responses, viral defense, and inflammatory regulation.
Recombinant USP18 protein is produced using biotechnological systems (e.g., E. coli or mammalian cells) to enable functional studies. Its production typically involves gene cloning, expression optimization, and purification via affinity chromatography. The recombinant protein retains enzymatic activity and structural integrity, allowing researchers to investigate ISG15-related pathways, IFN signaling modulation, and protein post-translational modifications. Studies using recombinant USP18 have revealed its involvement in controlling viral infections, such as hepatitis B and influenza, by counteracting ISG15-mediated antiviral effects. It also influences cancer progression and autoimmune disorders, where dysregulated IFN signaling is a hallmark.
Research applications include in vitro assays to dissect USP18-substrate interactions, drug screening for inflammatory diseases, and structural studies to map its catalytic domains. Challenges in working with USP18 recombinant protein include maintaining its labile enzymatic activity and resolving functional crosstalk between its ISG15-dependent and IFN-regulatory roles. Ongoing studies aim to explore its therapeutic potential in immune modulation and antiviral strategies.
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