| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NOL6 |
| Uniprot No | Q9H6R4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-200 aa |
| 活性数据 | MVIVTPQDRKNSVWTQDGPSAQILQQLVVLAAEALPMLEKQLMDPRGPGDIRTVFRPPLDIYDVLIRLSPRHIPRHRQAVDSPAASFCRGLLSQPGPSSLMPVLGYDPPQLYLTQLREAFGDLALFFYDQHGGEVIGVLWKPTSFQPQPFKASSTKGRMVMSRGGELVMVPNVEAILEDFAVLGEGLVQTVEARSERWTV |
| 分子量 | 47.74 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NOL6蛋白的3篇文献参考(虚构示例，仅作格式说明)：
1. **文献名称**: *Molecular Cloning and Characterization of Human NOL6: A Ribosomal RNA Processing Factor*
**作者**: Tanaka, K. et al.
**摘要**: 本研究首次克隆并表达了重组人NOL6蛋白，证实其定位于细胞核仁，并证明其通过结合rRNA前体参与核糖体亚基的成熟。
2. **文献名称**: *Structural Insights into the Function of NOL6 in Ribosome Biogenesis*
**作者**: Lee, S. & Kim, J.
**摘要**: 通过晶体学解析重组NOL6蛋白结构，发现其C端结构域具有核酸酶活性，并揭示了其在rRNA加工中的催化机制。
3. **文献名称**: *NOL6 Interaction with DDX21 Links Ribosome Synthesis to Cell Proliferation*
**作者**: Müller, R. et al.
**摘要**: 本文利用重组NOL6蛋白进行免疫共沉淀实验，鉴定其与解旋酶DDX21的相互作用，并证明二者协同调控细胞周期相关rRNA代谢。
注：以上文献为模拟示例，实际研究中需根据具体数据库(如PubMed)检索真实发表文献。
**Background of Recombinant Human NOL6 Protein**
The nucleolar protein NOL6 (Nucleolar Protein 6) is a conserved eukaryotic protein primarily localized in the nucleolus, a subcellular compartment critical for ribosomal RNA (rRNA) biogenesis. Human NOL6 is implicated in pre-rRNA processing and ribosome assembly, though its exact molecular mechanisms remain partially understood. Studies suggest it interacts with other nucleolar components, such as ribonucleoproteins (RNPs), and may play a role in stabilizing RNA-protein complexes during rRNA maturation.
Structurally, NOL6 contains conserved domains associated with RNA binding and protein-protein interactions, though its full functional regions are still under investigation. Dysregulation of nucleolar proteins, including NOL6. has been linked to cellular stress responses and diseases, such as cancer and ribosomopathies. Recombinant human NOL6 protein is typically produced using expression systems like *E. coli* or mammalian cells, enabling researchers to study its biochemical properties, interactions, and role in ribosome biogenesis.
Research applications include *in vitro* binding assays, enzymatic activity studies, and exploring its potential as a biomarker or therapeutic target. The recombinant form allows for controlled experimentation, aiding in elucidating NOL6's contribution to nucleolar function and disease pathology. Further studies are needed to fully unravel its biological significance and translational potential.
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