| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NUMA1 |
| Uniprot No | Q14980 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 200-306aa |
| 氨基酸序列 | SPASPMGDILQTPQFQMRRLKKQLADERSNRDELELELAENRKLLTEKDA QIAMMQQRIDRLALLNEKQAASPLEPKELEELRDKNESLTMRLHETLKQC QDLKTEK |
| 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. |
1. **"Structural analysis of the mitotic apparatus protein NuMA"**
- *Author: Gueth-Hallonet C, et al.*
- 摘要：该研究通过重组表达NuMA蛋白片段，解析了其在中体形成中的结构功能，证实NuMA通过卷曲螺旋结构域介导多聚化，对纺锤体组装至关重要。
2. **"NuMA phosphorylation regulates spindle assembly and chromosome segregation"**
- *Author: Compton DA, et al.*
- 摘要：利用重组NuMA蛋白进行磷酸化实验，发现其磷酸化状态影响纺锤体微管锚定能力，揭示NuMA在有丝分裂中的动态调控机制。
3. **"Recombinant NuMA fragments induce nuclear reformation in vitro"**
- *Author: Salina D, et al.*
- 摘要：通过体外重构实验证明，NuMA重组蛋白与核膜成分互作，促进分裂后细胞核的重建，为核结构维持提供分子依据。
4. **"NuMA overexpression disrupts microtubule organization in cancer cells"**
- *Author: Zhang X, et al.*
- 摘要：在肿瘤模型中表达重组NuMA，发现其异常定位导致微管紊乱，提示NuMA失调可能与染色体不稳定性及肿瘤进展相关。
**Background of NUMA1 Recombinant Protein**
NUMA1 (Nuclear Mitotic Apparatus Protein 1), also known as SP-H antigen, is a critical structural protein involved in maintaining nuclear architecture and regulating mitotic processes. It is predominantly localized to the nucleus during interphase, where it contributes to the organization of chromatin and the stabilization of the nuclear matrix. During mitosis, NUMA1 relocates to the spindle poles, playing a key role in the assembly and stabilization of the mitotic spindle, ensuring accurate chromosome segregation.
Structurally, NUMA1 contains a globular N-terminal domain, a central coiled-coil region mediating dimerization, and a C-terminal microtubule-binding domain. Its interaction with dynein-dynactin complexes and other spindle-associated proteins underscores its importance in spindle pole formation and cell cycle progression. Dysregulation of NUMA1 has been linked to mitotic errors, genomic instability, and diseases such as cancer.
Recombinant NUMA1 protein is engineered using expression systems like *E. coli* or mammalian cells, enabling studies on its biochemical properties, interactions, and functional mechanisms. Researchers utilize this tool to investigate NUMA1's roles in nuclear organization, mitotic regulation, and its potential as a therapeutic target. Additionally, recombinant NUMA1 aids in exploring autoantibody interactions in autoimmune disorders, as NUMA1 is a known target in conditions like systemic sclerosis.
Overall, NUMA1 recombinant protein serves as a vital resource for dissecting cellular dynamics, advancing cancer research, and understanding pathologies linked to nuclear and mitotic dysfunction.
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