| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NHP2 |
| Uniprot No | Q9NX24 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-153aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMTKIKADPDGPEAQAEACSGERTYQELLVN QNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFVNKGEKGIMV LAGDTLPIEVYCHLPVMCEDRNLPYVYIPSKTDLGAAAGSKRPTCVIMVK PHEEYQEAYDECLEEVQSLPLPL |
| 预测分子量 | 19 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NHP2重组蛋白的3篇参考文献及其摘要概述：
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1. **文献名称**：*Reconstitution of human telomerase with recombinant components*
**作者**：Collins, K. et al.
**摘要**：该研究通过重组蛋白技术表达了人端粒酶复合体的核心组分(包括NHP2、NOP10、dyskerin和端粒酶RNA)，验证了它们在体外重组活性端粒酶的能力，并揭示了NHP2在复合体组装和RNA结合中的关键作用。
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2. **文献名称**：*Structural basis for the function of the Saccharomyces cerevisiae Gfd1 protein in mRNA nuclear export*
**作者**：Walbott, H. et al.
**摘要**：研究利用重组表达的酵母Nhp2蛋白(人NHP2同源物)，结合X射线晶体学分析其与RNA及复合体蛋白的相互作用，阐明了Nhp2在mRNA核输出中的结构功能，强调了其保守的RNA结合域的重要性。
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3. **文献名称**：*Mutations in the telomerase-associated protein NHP2 cause dyskeratosis congenita*
**作者**：Vulliamy, T. et al.
**摘要**：文章报道了先天性角化不良患者的NHP2基因突变，通过重组野生型和突变型NHP2蛋白的功能实验，证明突变导致端粒酶活性丧失，揭示了NHP2在维持端粒稳态中的病理机制。
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**备注**：若需扩展检索，可结合关键词“NHP2 recombinant expression”或“H/ACA RNP assembly”查找近年研究，部分文献可能涉及重组蛋白在疾病模型或药物筛选中的应用。
**Background of NHP2 Recombinant Protein**
NHP2 (non-histone protein 2) is a conserved nucleolar protein belonging to the H/ACA ribonucleoprotein (RNP) complex family, which plays a critical role in RNA metabolism, including rRNA processing, modification, and telomerase stabilization. It is structurally homologous to the yeast protein Nhp2p and functions as a core component of H/ACA RNPs, guiding site-specific pseudouridylation of RNA through its association with small nucleolar RNAs (snoRNAs) or small Cajal body RNAs (scaRNAs). This post-transcriptional modification is essential for RNA stability, ribosome biogenesis, and proper cellular function.
Recombinant NHP2 protein is engineered for research applications, typically produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*) to ensure high purity and activity. Its recombinant form allows detailed study of H/ACA RNP assembly, RNA-protein interactions, and pseudouridylation mechanisms. Dysregulation of NHP2 is linked to human diseases, particularly dyskeratosis congenita (DC), a rare genetic disorder characterized by telomere maintenance defects and bone marrow failure. Mutations in *NHP2* disrupt telomerase RNA (TERC) stability, accelerating telomere shortening and cellular aging.
Research on recombinant NHP2 also aids in understanding ribosomopathies, cancer biology, and aging-related pathologies. Its role in telomerase activity underscores its relevance in oncology, as telomerase reactivation is a hallmark of many cancers. Structural and functional studies using recombinant NHP2 contribute to therapeutic development, including small-molecule inhibitors targeting telomerase or RNA-modifying complexes. Overall, NHP2 recombinant protein serves as a vital tool for dissecting molecular pathways in RNA biology and disease mechanisms.
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