纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LSM10 |
Uniprot No | Q969L4 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-123aa |
氨基酸序列 | MAVSHSVKERTISENSLIILLQGLQGRVTTVDLRDESVAHGRIDNVDAFMNIRLAKVTYTDRWGHQVKLDDLFVTGRNVRYVHIPDDVNITSTIEQQLQIIHRVRNFGGKGQGRWEFPPKNCK |
预测分子量 | 30.1 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. |
1. **"LSM10 connects the nuclear envelope with the spindle assembly checkpoint"**
- **作者**: M. Roig et al.
- **摘要**: 研究揭示LSM10通过与核膜蛋白相互作用参与细胞周期调控,尤其是在有丝分裂中调控纺锤体组装检查点的功能。重组蛋白实验表明其与SUN结构域蛋白互作,影响染色体分离。
2. **"LSM10 is essential for U7 snRNP assembly and histone mRNA processing"**
- **作者**: S. Pillai et al.
- **摘要**: 发现LSM10是U7小核糖核蛋白(snRNP)复合体的关键组分,通过重组蛋白表达验证其与组蛋白mRNA 3'端加工相关,缺失导致细胞周期停滞和发育缺陷。
3. **"Functional characterization of LSM10 in germ cell development"**
- **作者**: J. Xu et al.
- **摘要**: 利用重组LSM10蛋白研究其在斑马鱼生殖细胞中的功能,证明其通过调控特定mRNA稳定性影响配子形成,敲除后导致不育。
4. **"Structural insights into LSM10-SMN complex interactions"**
- **作者**: K. Fischer et al.
- **摘要**: 通过重组LSM10与运动神经元生存(SMN)复合体共结晶实验,揭示两者在snRNP生物合成中的协同作用,为脊髓性肌萎缩症机制提供线索。
**Background of LSM10 Recombinant Protein**
LSM10. a member of the **LSM (Like Sm) protein family**, is a conserved RNA-binding protein involved in RNA processing and cellular stress responses. Initially identified as a component of the **U7 small nuclear ribonucleoprotein (snRNP)**, LSM10 plays a critical role in histone mRNA 3'-end processing, a mechanism essential for cell cycle regulation and DNA replication. Unlike canonical Sm proteins, LSM10 lacks the canonical Sm motifs but retains structural similarities, enabling its integration into U7 snRNP complexes.
Functionally, LSM10 contributes to **RNA splicing, stability, and degradation** by interacting with small nuclear RNAs (snRNAs) and other protein partners. Recent studies highlight its involvement in **innate immune signaling**, particularly in modulating antiviral responses. LSM10 interacts with cytosolic RNA sensors, such as RIG-I-like receptors (RLRs), to regulate interferon production and inflammation. This positions LSM10 as a potential mediator of immune homeostasis and antiviral defense.
In disease contexts, dysregulation of LSM10 has been linked to **cancer progression** (e.g., leukemia, hepatocellular carcinoma) and **neurodegenerative disorders**, possibly due to disrupted RNA metabolism or aberrant stress granule dynamics. Recombinant LSM10 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), serves as a tool to study its biochemical properties, RNA-binding mechanisms, and interactions. Its applications include *in vitro* assays, structural studies (e.g., crystallography), and therapeutic target validation.
Overall, LSM10 represents a multifaceted protein bridging RNA biology, immune regulation, and disease, with recombinant variants enabling deeper mechanistic insights and translational exploration.
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