| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UTP23 |
| Uniprot No | Q9BRU9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-249aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMKITRQKHAKKHLGFFRNNFGVREPYQ ILLDGTFCQAALRGRIQLREQLPRYLMGETQLCTTRCVLKELETLGKDLY GAKLIAQKCQVRNCPHFKNAVSGSECLLSMVEEGNPHHYFVATQDQNLSV KVKKKPGVPLMFIIQNTMVLDKPSPKTIAFVKAVESGQLVSVHEKESIKH LKEEQGLVKNTEQSRRKKRKKISGPNPLSCLKKKKKAPDTQSSASEKKRK RKRIRNRSNPKVLSEKQNAEGE |
| 预测分子量 | 31 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. |
以下是关于UTP23重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: *"Recombinant UTP23 facilitates pre-rRNA processing in vitro"*
**作者**: Smith A, et al.
**摘要**: 该研究通过在大肠杆菌中表达并纯化重组UTP23蛋白，证明其在体外能促进18S rRNA前体的剪切，揭示了UTP23在核糖体小亚基成熟中的直接作用机制。
2. **文献名称**: *"Structural insights into UTP23 in the U3 snoRNP complex"*
**作者**: Chen L, et al.
**摘要**: 作者利用重组人源UTP23蛋白进行冷冻电镜分析，解析了其与U3 snoRNP复合物结合的分子结构，阐明了UTP23通过特定结构域介导复合物组装的功能。
3. **文献名称**: *"Functional characterization of yeast UTP23 in ribosome biogenesis"*
**作者**: Tanaka K, et al.
**摘要**: 通过重组表达酵母UTP23蛋白，结合基因敲除实验，发现UTP23缺失导致rRNA加工停滞，证实其在核糖体RNA转录早期阶段的调控作用。
注：以上文献为示例性质，实际文献需根据具体数据库检索结果调整。建议通过PubMed或Web of Science以“UTP23 recombinant”为关键词查找最新研究。
The UTP23 protein is a critical component of the small subunit (SSU) processome, a large ribonucleoprotein complex essential for the biogenesis of 18S ribosomal RNA (rRNA) in eukaryotic cells. As part of the UTP (U3 small nucleolar RNA-associated protein) complex, UTP23 plays a role in the early stages of ribosomal subunit assembly, particularly in the processing and folding of precursor rRNA (pre-rRNA). It facilitates the cleavage of the 35S pre-rRNA transcript at specific sites, enabling the maturation of the 18S rRNA component of the 40S ribosomal subunit. Dysregulation of UTP23 has been implicated in ribosomopathies and cancers due to its fundamental role in ribosome synthesis, which directly impacts cellular growth and proliferation.
Recombinant UTP23 protein is produced through molecular cloning techniques, where the UTP23 gene is expressed in heterologous systems like *E. coli* or yeast. This allows researchers to obtain purified, functional UTP23 for structural and mechanistic studies. The recombinant protein is widely used to investigate ribosome assembly pathways, dissect interactions with other SSU processome components (e.g., U3 snoRNA or proteins like DIM2), and explore its enzymatic or scaffolding roles in rRNA processing. Additionally, it serves as a tool to study mutations linked to developmental disorders or cancer, providing insights into how altered ribosome biogenesis contributes to disease.
Recent studies also utilize recombinant UTP23 in high-resolution cryo-EM analyses to map its position within the SSU processome, advancing our understanding of ribosome assembly dynamics. Its applications extend to drug discovery, particularly in targeting ribosome biosynthesis pathways for cancer therapy. Despite progress, questions remain about its precise molecular functions, post-translational modifications, and regulatory mechanisms, making recombinant UTP23 a continued focus in cell biology and translational research.
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