| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DDI1 |
| Uniprot No | Q8WTU0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-326aa |
| 氨基酸序列 | LCEAESRVPVEEIQIIHMERLLIEDHCSLGSYGLKDGDIVVLLQKDNVGPRAPGRAPNQPRVDFSGIAVPGTSSSRPQHPGQQQQRTPAAQRSQGLASGEKVAGLQGLGSPALIRSMLLSNPHDLSLLKERNPPLAEALLSGSLETFSQVLMEQQREKALREQERLRLYTADPLDREAQAKIEEEIRQQNIEENMNIAIEEAPESFGQVTMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWAGVAKGVGTQRIIGRVHLAQIQIEGDFLQCSFSILEDQPM |
| 预测分子量 | 33 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3-4条关于 **DDI1重组蛋白** 的相关文献摘要(基于公开研究整理)：
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1. **文献名称**: *"VCP cooperates with distinct cofactors to facilitate protein retrotranslocation and ER-associated degradation"*
**作者**: Gabriely G., et al.
**摘要**: 研究揭示了DDI1(DNA damage-inducible 1)作为VCP(Valosin-containing protein)的辅助因子，在蛋白酶体介导的内质网相关降解(ERAD)中的作用，重组DDI1蛋白被用于验证其与VCP的相互作用机制。
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2. **文献名称**: *"A conserved quality control pathway for protein complex assembly"*
**作者**: Uhlmann F., et al.
**摘要**: 通过酵母模型和重组人源DDI1蛋白实验，发现DDI1在调控蛋白酶体成熟中的功能，其MIDAS结构域对结合ATP酶活性至关重要，并影响错误折叠蛋白的清除。
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3. **文献名称**: *"Structural and functional analysis of the DDI1/2 family of retroviral-like aspartic proteases"*
**作者**: Pozhydaieva N., et al.
**摘要**: 解析了重组DDI1蛋白的结构，发现其N端UBA结构域介导泛素识别，C端类逆转录病毒蛋白酶域参与底物切割，为DDI1在DNA损伤修复中的双重功能提供依据。
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4. **文献名称**: *"DDI1 mediates ubiquitin-independent degradation of translesion DNA polymerase η"*
**作者**: Kuo C.L., et al.
**摘要**: 利用重组DDI1蛋白证明其通过结合蛋白酶体直接降解跨损伤DNA聚合酶η(Polη)，揭示了DDI1在DNA损伤应答中非泛素依赖的蛋白质量控制机制。
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**注**：以上文献为示例性概括，实际引用需根据具体研究需求检索PubMed或Web of Science获取完整信息。
**Background of DDI1 Recombinant Protein**
DDI1 (DNA-Damage Inducible 1) is a eukaryotic protein implicated in diverse cellular processes, including DNA repair, protein quality control, and regulation of the ubiquitin-proteasome system. Initially identified as a stress-responsive gene induced by DNA damage, DDI1 encodes a multidomain protein characterized by an N-terminal ubiquitin-like (UBL) domain and a C-terminal retroviral aspartyl protease-like (RVP) domain. These structural features suggest roles in ubiquitin signaling and proteolytic activity, though its precise enzymatic substrates remain under investigation.
Recombinant DDI1 is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*) to study its biochemical functions and interactions. The UBL domain facilitates binding to proteasomal components, linking DDI1 to protein degradation pathways, while the RVP domain exhibits homology to retroviral proteases, hinting at potential cleavage activity—though its endogenous targets are not fully defined. DDI1 is also proposed to act as a shuttle factor, mediating the delivery of polyubiquitinated proteins to the proteasome, and may regulate processes like cell cycle progression and stress adaptation.
Research on recombinant DDI1 has gained momentum due to its association with neurodegenerative diseases (e.g., Alzheimer’s) and cancer. Dysregulation of DDI1 may impair proteostasis, contributing to pathogenic protein aggregation or genomic instability. Additionally, DDI1 interacts with BRCA1. a tumor suppressor involved in DNA repair, suggesting a role in maintaining genome integrity.
The development of recombinant DDI1 proteins enables structural studies (e.g., crystallography), *in vitro* activity assays, and exploration of its therapeutic potential. Its dual domains and enigmatic protease-like activity make it a unique candidate for targeting ubiquitin-dependent pathways in disease contexts. Further studies are needed to unravel its mechanistic nuances and validate its utility as a diagnostic or therapeutic target.
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