| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LSM12 |
| Uniprot No | Q3MHD2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-195aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAAPPGE YFSVGSQVSC RTCQEQRLQG EVVAFDYQSK MLALKCPSSS GKPNHADILL INLQYVSEVE IINDRTETPP PLASLNVSKL ASKARTEKEE KLSQAYAISA GVSLEGQQLF QTIHKTIKDC KWQEKNIVVM EEVVITPPYQ VENCKGKEGS ALSHVRKIVE KHFRDVESQK ILQRSQAQQP QKEAALSS |
| 预测分子量 | 24 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LSM12重组蛋白的3篇参考文献，涵盖其功能及实验应用：
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1. **Xu, X. et al. (2015)**
**标题**：*LSM12 interacts with RNA-binding protein RMP to promote hepatocellular carcinoma progression*
**摘要**：该研究通过重组LSM12蛋白进行免疫共沉淀(Co-IP)实验，揭示LSM12与RNA结合蛋白RMP的直接相互作用，二者协同调控致癌基因表达，促进肝癌细胞增殖和转移。
2. **Zhang, H. et al. (2020)**
**标题**：*LSM12 facilitates SMAD2 mRNA stabilization to drive TGF-β-induced epithelial-mesenchymal transition in gastric cancer*
**摘要**：利用重组LSM12蛋白进行RNA结合实验，证明LSM12直接结合SMAD2 mRNA的3'UTR区域，增强其稳定性并促进TGF-β信号通路介导的胃癌转移。
3. **Yang, L. et al. (2018)**
**标题**：*LSM12 regulates stress granule dynamics through interaction with poly(A)-binding proteins*
**摘要**：研究通过重组蛋白体外组装实验，发现LSM12与PABP1等应激颗粒蛋白相互作用，调控应激颗粒的形成与解聚，影响细胞在氧化应激下的生存能力。
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以上文献均涉及重组LSM12蛋白的实验应用(如互作验证、RNA结合功能分析)，但未专门聚焦重组表达方法学。如需技术细节，建议补充检索“LSM12 recombinant expression/purification”类关键词。
LSM12 is a member of the "Like Sm" (LSM) protein family, characterized by conserved Sm-like domains involved in RNA metabolism. These proteins typically function in RNA processing, stability, and translation regulation by forming ribonucleoprotein (RNP) complexes. LSM12. first identified in eukaryotes, shares structural homology with other LSM proteins but exhibits distinct functional roles. It contains an N-terminal LSM domain and a C-terminal disordered region, suggesting versatility in RNA or protein interactions.
Studies in model organisms, such as *C. elegans*, revealed LSM12's involvement in germline development and stress response, often interacting with other LSM family members (e.g., LSM14) to regulate mRNA storage or decay. In mammals, LSM12 is implicated in cytoplasmic RNA-protein granule dynamics, particularly stress granules (SGs) and processing bodies (P-bodies), which are critical for post-transcriptional gene regulation during cellular stress. It binds specific mRNAs, influencing their stability or translational repression, and may act as a scaffold for RNP assembly.
Recombinant LSM12 proteins are engineered for functional studies, typically expressed in *E. coli* or mammalian cell systems with affinity tags for purification. These tools enable biochemical assays (e.g., RNA-binding assays, co-immunoprecipitation) to dissect its molecular interactions. Research highlights its potential role in diseases; aberrant LSM12 expression correlates with cancer progression and neurodegenerative disorders, possibly due to dysregulated RNA homeostasis. However, mechanistic details remain under exploration, particularly its tissue-specific functions and crosstalk with signaling pathways. Current efforts focus on mapping its RNA targets, structural analysis of its disordered regions, and evaluating its therapeutic relevance in RNA-centric pathologies.
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