| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UFD1L |
| Uniprot No | Q92890 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-307aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMFSFNMF DHPIPRVFQN RFSTQYRCFS VSMLAGPNDR SDVEKGGKII MPPSALDQLS RLNITYPMLF KLTNKNSDRM THCGVLEFVA DEGICYLPHW MMQNLLLEEG GLVQVESVNL QVATYSKFQP QSPDFLDITN PKAVLENALR NFACLTTGDV IAINYNEKIY ELRVMETKPD KAVSIIECDM NVDFDAPLGY KEPERQVQHE ESTEGEADHS GYAGELGFRA FSGSGNRLDG KKKGVEPSPS PIKPGDIKRG IPNYEFKLGK ITFIRNSRPL VKKVEEDEAG GRFVAFSGEG QSLRKKGRKP |
| 预测分子量 | 37 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UFD1L重组蛋白的3篇参考文献概览(基于公开研究领域知识模拟，非真实文献)：
1. **标题**：*Functional characterization of UFD1L in ubiquitin-proteasome pathways*
**作者**：Smith A, et al.
**摘要**：研究通过原核表达系统成功纯化重组UFD1L蛋白，并验证其与CDC48/p97复合物的相互作用，揭示其在泛素依赖性蛋白酶体降解中的调控作用。
2. **标题**：*Structural analysis of UFD1L and its role in embryonic development*
**作者**：Chen L, et al.
**摘要**：利用哺乳动物细胞表达重组UFD1L蛋白，结合晶体结构解析，发现其N端结构域对结合VCP蛋白至关重要，并证实UFD1L缺失导致小鼠胚胎神经嵴发育异常。
3. **标题**：*UFD1L recombinant protein rescues cellular defects in DiGeorge syndrome models*
**作者**：Wang X, et al.
**摘要**：通过昆虫表达系统制备高纯度UFD1L重组蛋白，体外实验证明其可恢复迪乔治综合征细胞模型中泛素化底物清除能力，提示潜在治疗价值。
注：以上内容为模拟文献，如需真实文献建议通过PubMed/Google Scholar以“UFD1L recombinant protein”等关键词检索。
**Background of UFD1L Recombinant Protein**
UFD1L (Ubiquitin Fusion Degradation 1 Like) is a conserved eukaryotic protein central to the ubiquitin-proteasome system (UPS), a critical pathway for targeted protein degradation. It functions as a cofactor for the AAA-ATPase p97/VCP (Valosin-Containing Protein), forming part of the p97-UFD1L-NPL4 complex. This complex facilitates the extraction and processing of ubiquitinated substrates from cellular structures or complexes, particularly in endoplasmic reticulum-associated degradation (ERAD) and mitophagy. UFD1L recognizes polyubiquitin chains via its N-terminal ubiquitin-binding region, enabling substrate recruitment for subsequent ATP-dependent unfolding and proteasomal degradation.
UFD1L is implicated in diverse cellular processes, including cell cycle regulation, DNA repair, and stress response. Its dysfunction is linked to developmental disorders, notably DiGeorge syndrome, where hemizygous deletion of chromosome 22q11.2 (encompassing *UFD1L*) contributes to cardiovascular, craniofacial, and immune abnormalities. Studies also suggest roles in cancer progression and neurodegenerative diseases, highlighting its broad pathophysiological relevance.
Recombinant UFD1L proteins are engineered for *in vitro* studies to dissect molecular mechanisms, substrate interactions, and structural dynamics. Produced in systems like *E. coli* or mammalian cells, these proteins often include affinity tags (e.g., His-tag) for purification. Research applications include binding assays, enzymatic activity analyses, and inhibitor screening, aiding drug discovery targeting UPS-related disorders. The recombinant tool has advanced understanding of UFD1L’s regulatory networks and potential therapeutic interventions for diseases tied to protein homeostasis defects.
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