| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UFSP1 |
| Uniprot No | Q6NVU6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMGDKPPG FRGSRDWIGC VEASLCLAHF GGPQGRLCHV PRGVGLHGEL ERLYSHFAGG GGPVMVGGDA DARSKALLGV CVGSGTEAYV LVLDPHYWGT PKSPSELQAA GWVGWQEVSA AFDPNSFYNL CLTSLSSQQQ QRTLD |
| 预测分子量 | 17 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UFSP1重组蛋白的3篇参考文献示例(注：内容为虚构，仅作格式参考)：
1. **文献名称**：*"Recombinant Expression and Enzymatic Characterization of Human UFSP1"*
**作者**：Zhang L, et al.
**摘要**：该研究报道了在大肠杆菌系统中成功表达并纯化重组UFSP1蛋白，证实其具有特异性切割泛素样蛋白修饰的酶活性，并揭示了其底物结合的关键结构域。
2. **文献名称**：*"Structural and Functional Analysis of UFSP1 in Cell Cycle Regulation"*
**作者**：Wang Y, et al.
**摘要**：通过昆虫细胞表达系统获得高纯度UFSP1重组蛋白，结合晶体结构解析和细胞实验，证明UFSP1通过去泛素化作用调控细胞周期蛋白的稳定性。
3. **文献名称**：*"UFSP1 Recombinant Protein Production and Its Role in Autophagy"*
**作者**：Kim S, et al.
**摘要**：研究利用哺乳动物细胞表达重组UFSP1.发现其通过选择性去泛素化参与自噬通路，为UFSP1在疾病中的功能机制提供了新见解。
(注：以上文献为模拟生成，实际研究中请通过学术数据库检索真实文献。)
**Background of UFSP1 Recombinant Protein**
UFSP1 (Ubiquitin-Fold Specific Protease 1) is a cysteine protease that plays a critical role in the ubiquitin-proteasome system (UPS), a major pathway for regulated protein degradation in eukaryotic cells. Unlike canonical deubiquitinating enzymes (DUBs), UFSP1 belongs to a distinct family of proteases that specifically cleave ubiquitin-like (UBL) modifications. It is known to process pro-UBL molecules, such as ubiquitin and ubiquitin-like modifiers (e.g., SUMO or NEDD8), by removing C-terminal extensions to generate mature, functional forms essential for downstream signaling.
UFSP1 is unique in its structural and mechanistic features. It lacks the typical ubiquitin-binding domains found in other DUBs but relies on a conserved catalytic triad (Cys, His, Asp/Glu) for enzymatic activity. Structural studies reveal a compact fold stabilized by zinc coordination, critical for its proteolytic function. Its substrate specificity is tightly regulated, with a preference for ubiquitin precursors over other UBLs, highlighting its specialized role in maintaining ubiquitin homeostasis.
Recombinant UFSP1 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*) for biochemical and functional studies. Purified UFSP1 is widely used to investigate UPS mechanisms, substrate processing, and enzyme kinetics. Recent studies implicate UFSP1 in cellular processes such as DNA repair, immune response modulation, and stress signaling, with dysregulation linked to neurodegenerative diseases and cancer.
The development of UFSP1 recombinant protein has facilitated drug discovery efforts, particularly in designing inhibitors to modulate UPS activity. Its role in cleaving disease-associated ubiquitin conjugates positions it as a potential therapeutic target. Ongoing research aims to unravel its physiological substrates, regulatory networks, and pathophysiological relevance, underscoring its importance in both basic and translational biology.
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