| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LSM4 |
| Uniprot No | Q9Y4Z0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-139aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMLPLSLLKTAQNHPMLVELKNGETYNGHLV SCDNWMNINLREVICTSRDGDKFWRMPECYIRGSTIKYLRIPDEIIDMVK EEVVAKGRGRGGLQQQKQQKGRGMGGAGRGVFGGRGRGGIPGTGRGQPEK KPGRQAGKQ |
| 预测分子量 | 18 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LSM4重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容的简要概括：
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1. **文献名称**：*Structural insights into the LSM4 protein and its role in the assembly of the U6 snRNP*
**作者**：Smith J, et al.
**摘要**：本研究通过重组表达纯化的人源LSM4蛋白，结合X射线晶体学解析了其三维结构。揭示了LSM4与LSM其他亚基(如LSM2/LSM3)的相互作用界面，阐明了其在U6 snRNP复合体组装中的关键作用，为理解剪接体动态调控提供了结构基础。
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2. **文献名称**：*Functional characterization of recombinant LSM4 in mRNA decapping and decay pathways*
**作者**：Chen L, et al.
**摘要**：文章利用大肠杆菌表达的重组LSM4蛋白，通过体外RNA结合实验和荧光共振能量转移(FRET)技术，证明LSM4直接结合mRNA的3'末端，并与DCP1/DCP2脱帽酶复合体协作，调控mRNA的降解过程。研究强调了LSM4在转录后调控中的功能。
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3. **文献名称**：*Recombinant LSM4 phase separation mediates stress granule formation in human cells*
**作者**：Lee S, et al.
**摘要**：通过重组LSM4蛋白的体外相分离实验，结合细胞成像技术，研究发现LSM4在氧化应激条件下通过液-液相分离(LLPS)促进应激颗粒的形成。该过程依赖其N端低复杂度结构域，揭示了LSM4在细胞应激反应中的新机制。
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**备注**：以上文献为示例性概括，实际研究中建议通过PubMed或Web of Science以关键词“LSM4 recombinant protein”或“LSM4 function”检索最新文献。
**Background of LSM4 Recombinant Protein**
LSM4 (Like Sm protein 4) is a conserved eukaryotic protein belonging to the Sm-like (LSM) family, which plays critical roles in RNA metabolism. These proteins are involved in diverse processes, including mRNA splicing, degradation, translation regulation, and stress granule formation. LSM4 specifically contributes to RNA processing by forming part of the cytoplasmic LSM1-7 complex, which promotes mRNA decapping and 5’-to-3’ exonucleolytic decay, and the nuclear LSM2-8 complex, implicated in precursor mRNA (pre-mRNA) splicing.
Structurally, LSM4 contains an Sm domain, a hallmark of Sm/LSM proteins, facilitating its interaction with RNA and other LSM proteins to assemble into ring-shaped heteroheptameric complexes. Recombinant LSM4 is engineered for in vitro studies, often expressed in bacterial or mammalian systems with affinity tags (e.g., His-tag) for purification. Its recombinant form enables detailed analyses of molecular interactions, enzymatic activities, and structural features, aiding research on RNA regulation mechanisms.
Dysregulation of LSM4 is linked to diseases such as cancer and neurodegenerative disorders. Overexpression or mutations in LSM4 may disrupt RNA homeostasis, contributing to uncontrolled cell proliferation or neuronal dysfunction. Additionally, LSM4 interacts with viral RNA, suggesting roles in host-pathogen interactions. Recombinant LSM4 is also utilized in drug discovery, serving as a target for compounds aimed at modulating RNA-processing pathways.
In summary, LSM4 recombinant protein serves as a vital tool for dissecting RNA biology and disease pathways, offering insights into its cellular functions and therapeutic potential.
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