| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NBR2 |
| Uniprot No | O15453 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-82 aa |
| 活性数据 | MWKGGRSHPFLPHSSRCAGSGGQLDSILPHQSPAWGPWGCKDLSSGFPSFLTSSILWKSAVVREPHISPHQAPPYKTSDCIT |
| 分子量 | 34.65 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人NBR2蛋白的模拟参考文献示例(注：文献内容为虚构，仅供参考格式)：
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1. **《Selective Autophagy Mediated by NBR2 Requires Its Recombinant Expression in Human Cells》**
- **作者**: Tanaka, K. et al.
- **摘要**: 研究验证了重组人NBR2蛋白在哺乳动物细胞中的表达对自噬过程的调控作用。通过体外实验发现，NBR2与LC3蛋白相互作用，并通过泛素化依赖性途径促进受损线粒体的清除，揭示了其在选择性自噬中的关键功能。
2. **《Recombinant NBR2 Protein Binds Ubiquitin Chains to Facilitate Aggrephagy》**
- **作者**: Smith, R. & Johnson, L.
- **摘要**: 本研究利用大肠杆菌系统重组表达并纯化了人NBR2蛋白，发现其通过C端UBA结构域特异性结合K63型泛素链，促进聚集蛋白的自噬降解，为神经退行性疾病中蛋白聚集的清除机制提供了新见解。
3. **《NBR2 Overexpression Suppresses Tumor Growth via mTOR Signaling Inhibition》**
- **作者**: Chen, X. et al.
- **摘要**: 通过重组NBR2蛋白的体外功能实验，发现其过表达可抑制mTOR通路活性，进而诱导癌细胞自噬性死亡。研究强调了NBR2在肿瘤治疗中的潜在应用价值。
4. **《Structural Insights into the Zinc Finger Domain of Recombinant Human NBR2》**
- **作者**: Müller, T. et al.
- **摘要**: 采用X射线晶体学解析了重组人NBR2蛋白N端锌指结构域的三维结构，揭示了其与其他自噬受体(如p62)的构象差异，为设计靶向NBR2的小分子药物提供了结构基础。
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注：实际文献需通过学术数据库检索确认，以上内容为示例性模拟。
NBR2 (Neighbor of BRCA1 gene 2) protein is a relatively understudied cellular protein encoded by the *NBR2* gene, located adjacent to the tumor suppressor gene *BRCA1* on chromosome 17q21. Structurally, it shares homology with its paralog NBR1. featuring conserved domains such as a Phox and Bem1 (PB1) domain, LC3-interacting region (LIR), and ubiquitin-associated (UBA) domains. These motifs suggest roles in selective autophagy, where NBR2 may act as a receptor for recruiting ubiquitinated cargo (e.g., damaged organelles or protein aggregates) to autophagosomes via interactions with LC3/GABARAP proteins.
NBR2 is implicated in stress responses, particularly under nutrient deprivation or oxidative conditions. Interestingly, its expression is upregulated by energy stress through AMPK activation, linking it to metabolic regulation. While its precise biological functions remain unclear, studies propose crosstalk with NBR1 or BRCA1. potentially influencing DNA repair pathways or tumorigenesis. Dysregulation of NBR2 has been observed in cancers, including breast and ovarian cancers, though its role as an oncogene or tumor suppressor remains context-dependent. Emerging evidence also hints at its involvement in neurodegenerative diseases due to autophagy-related mechanisms. Current research focuses on clarifying its interactions, regulatory networks, and therapeutic potential as a target for cancer or metabolic disorders. Further studies are needed to unravel its exact physiological and pathological contributions.
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