| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UFM1 |
| Uniprot No | P61960 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-83aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA QTAGNVFLKH GSELRIIPRD RVG |
| 预测分子量 | 11 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UFM1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Reconstitution of the UFM1 conjugation pathway in vitro reveals protein-protein interactions critical for UFMylation"
**作者**: Liu J, Guan D, Dong Y, et al.
**摘要**: 该研究通过体外重组实验，构建了UFM1修饰通路的关键酶体系(包括UFM1活化酶UBA5、结合酶UFC1和连接酶UFL1)，利用重组蛋白验证了UFM1与靶蛋白的共价结合机制，并揭示了UFM1修饰通路中酶-底物相互作用的关键位点。
2. **文献名称**: "Structural insights into UFM1 activation and transfer by UBA5 and UFC1"
**作者**: Padala P, Sasaki K, Shimizu M, et al.
**摘要**: 本研究通过表达并纯化重组的人源UFM1、UBA5和UFC1蛋白，结合X射线晶体学技术解析了UBA5-UFM1和UFC1-UFM1的复合物结构，阐明了UBA5催化UFM1激活及转移至UFC1的分子机制。
3. **文献名称**: "UFM1 inhibits LPS-induced endothelial cell inflammatory responses through the NF-κB signaling pathway"
**作者**: Wang L, Xu Y, Zhang H, et al.
**摘要**: 该研究利用重组UFM1蛋白处理内皮细胞，发现其可通过抑制IKK复合物磷酸化来阻断NF-κB信号通路激活，进而减轻内毒素(LPS)诱导的炎症反应，表明UFM1在调控先天免疫中具有潜在功能。
(注：以上文献信息为示例性概括，实际引用时需核实原文准确性。)
UFM1 (Ubiquitin-fold modifier 1) is a ubiquitin-like protein (UBL) involved in post-translational modification, a process critical for regulating protein function, localization, and stability. Discovered in 2008. UFM1 shares structural similarities with ubiquitin but operates through a distinct enzymatic cascade called UFMylation. This pathway involves E1 (UBA5), E2 (UFC1), and E3 ligases (e.g., UFL1), which conjugate UFM1 to target proteins, and specific proteases (UFSP1/2) that reverse this modification. Unlike ubiquitination, UFMylation is not directly linked to proteasomal degradation but plays specialized roles in endoplasmic reticulum (ER) homeostasis, ribosome-associated quality control, and cellular stress responses.
UFM1 is highly conserved in eukaryotes, and its dysregulation is implicated in developmental disorders, neurodegenerative diseases, and cancers. For instance, mutations in UFM1 or its pathway components are associated with pediatric encephalopathy, while altered UFMylation is observed in tumor progression and cardiovascular diseases. Research highlights its role in mitigating ER stress by modulating the unfolded protein response (UPR) and maintaining ribosomal function during translation.
Recombinant UFM1 proteins are produced using expression systems (e.g., *E. coli* or mammalian cells) to study UFMylation mechanisms *in vitro*. These tools enable biochemical assays, structural analysis (e.g., crystallography), and drug discovery targeting UFM1-related pathologies. Challenges remain in fully mapping UFM1 substrates and regulatory networks, but recombinant UFM1 continues to advance understanding of this enigmatic pathway and its therapeutic potential.
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