| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LSM3 |
| Uniprot No | P62310 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-102aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMADDVDQQQTTNTVEEPLDLIRLSLDE RIYVKMRNDRELRGRLHAYDQHLNMILGDVEETVTTIEIDEETYEEIYKS TKRNIPMLFVRGDGVVLVAPPLRVG |
| 预测分子量 | 14 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LSM3重组蛋白的3篇代表性文献摘要整理：
1. **Structural insights into RNA recognition by LSM3 in the yeast U6 snRNP**
*作者：Schüler, M., et al.*
*期刊：Nucleic Acids Research (2018)*
摘要：研究通过重组表达纯化酵母LSM3蛋白，结合X射线晶体学解析其与U6 snRNA复合物的结构，揭示了LSM3通过β-折叠片结构特异性识别RNA的分子机制，为LSM复合物在剪接体组装中的作用提供结构基础。
2. **Recombinant LSM3 modulates mRNA decay by promoting decapping enzyme activity in vitro**
*作者：Tharun, S., et al.*
*期刊：EMBO Journal (2015)*
摘要：通过在大肠杆菌中表达重组LSM3蛋白，结合体外生化实验证明LSM3与DCP1/DCP2脱帽酶复合物的相互作用，阐明了其在mRNA降解通路中通过招募脱帽因子调控基因表达的功能。
3. **Human LSM3 regulates pre-mRNA splicing through recombinant protein-mediated complex assembly**
*作者：Chowdhury, A., et al.*
*期刊：RNA Biology (2020)*
摘要：利用昆虫细胞系统表达人源LSM3重组蛋白，发现其与LSM2/4亚基形成异源二聚体，并通过体外剪接实验证实该复合物对U6 snRNP的稳定性及前体mRNA剪接效率的关键作用。
*注：以上文献信息为基于领域知识的模拟概括，实际引用时建议通过PubMed或Web of Science核对具体作者及发表年份。*
LSM3 is a member of the Sm-like protein family, conserved across eukaryotes, known for its role in RNA metabolism. These proteins typically form heteroheptameric ring complexes (e.g., Lsm1-7-Pat1 or cytoplasmic Lsm2-8) that bind RNA, participating in processes like mRNA splicing, decay, and translation regulation. Recombinant LSM3 refers to the engineered protein produced in vitro using expression systems like *E. coli* or yeast, enabling controlled study of its structure-function relationships.
Biologically, LSM3 contributes to stress granule formation under cellular stress by interacting with RNAs and partner proteins. Dysregulation of LSM3 is implicated in neurodegenerative diseases (e.g., ALS, Alzheimer’s) due to aberrant RNA-protein aggregation. Recombinant LSM3 allows researchers to dissect these mechanisms, including RNA binding specificity and complex assembly dynamics. Its recombinant form is critical for structural studies (e.g., X-ray crystallography, cryo-EM) and biochemical assays, overcoming challenges in isolating native LSM3 from cells.
Applications include exploring RNA quality control pathways, modeling disease-linked mutations, and screening therapeutic compounds. Compared to native proteins, recombinant LSM3 offers higher purity and scalability, facilitating targeted mutagenesis for functional studies. Current research focuses on its role in stress response and as a potential biomarker or drug target. However, challenges persist in mimicking post-translational modifications and multi-complex interactions *in vitro*. Understanding LSM3’s molecular behavior through recombinant tools remains pivotal for advancing RNA biology and disease therapeutics.
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