| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NOP16 |
| Uniprot No | Q9Y3C1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-178aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMPKAKGK TRRQKFGYSV NRKRLNRNAR RKAAPRIECS HIRHAWDHAK SVRQNLAEMG LAVDPNRAVP LRKRKVKAME VDIEERPKEL VRKPYVLNDL EAEASLPEKK GNTLSRDLID YVRYMVENHG EDYKAMARDE KNYYQDTPKQ IRSKINVYKR FYPAEWQDFL DSLQKRKMEV E |
| 预测分子量 | 24 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. |
以下是虚构的关于NOP16重组蛋白的参考文献示例(仅供示例参考，非真实文献)：
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1. **标题**: *Functional Characterization of Recombinant NOP16 in Ribosomal RNA Processing*
**作者**: Smith A, et al.
**期刊**: *Journal of Molecular Biology* (2020)
**摘要**: 本研究通过在大肠杆菌中重组表达并纯化NOP16蛋白，验证其与18S rRNA前体的结合能力，证实NOP16在核糖体小亚基组装中通过RNA识别基序(RRM)调控rRNA加工。
2. **标题**: *Structural Insights into NOP16-Protein Interactions via Yeast Two-Hybrid Screening*
**作者**: Chen L, et al.
**期刊**: *Biochemical and Biophysical Research Communications* (2018)
**摘要**: 利用重组NOP16蛋白进行酵母双杂交筛选，鉴定出与核仁蛋白NOP58和FIB1的相互作用，提示其在核糖体生物合成复合体中的协同功能。
3. **标题**: *Expression Optimization and Crystallization of Recombinant Human NOP16*
**作者**: García-Ruiz E, et al.
**期刊**: *Protein Expression and Purification* (2019)
**摘要**: 通过哺乳动物细胞表达系统优化人源NOP16重组蛋白产量，并利用X射线晶体学解析其N端结构域的三维结构，揭示了潜在的RNA结合位点。
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**注意**：以上文献信息为模拟生成，实际研究中请通过PubMed、Web of Science或Google Scholar等平台检索真实文献。
NOP16. a nucleolar protein encoded by the *NOP16* gene, plays a crucial role in ribosome biogenesis and cellular proliferation. It is implicated in the early stages of 18S rRNA processing within the small ribosomal subunit. As a conserved component of the ribosome assembly machinery, NOP16 interacts with other nucleolar proteins and RNA molecules to ensure proper rRNA maturation, a process vital for protein synthesis and cell viability.
Recombinant NOP16 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to produce a purified, biologically active form for research. Its recombinant version typically retains functional domains necessary for rRNA binding and protein-protein interactions, enabling studies on ribosome assembly mechanisms, nucleolar dynamics, and links to diseases. Notably, dysregulated NOP16 expression has been observed in certain cancers, suggesting its potential as a biomarker or therapeutic target.
The production of recombinant NOP16 involves cloning the gene into expression vectors, optimizing conditions for solubility, and employing affinity chromatography (e.g., His-tag purification). This tool supports *in vitro* analyses, including binding assays, structural studies, and screening for inhibitors affecting ribosome biogenesis. Its applications extend to investigating cellular stress responses, as nucleolar function is sensitive to metabolic or genotoxic disruptions. Ongoing research aims to clarify NOP16's role in pathological contexts, such as tumorigenesis, and its utility in diagnostic or drug development pipelines.
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