| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LSM1 |
| Uniprot No | O15116 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-133aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMNYMPGTASLIEDIDKKHLVLLRDGRTLIG FLRSIDQFANLVLHQTVERIHVGKKYGDIPRGIFVVRGENVVLLGEIDLE KESDTPLQQVSIEEILEEQRVEQQTKLEAEKLKVQALKDRGLSIPRADTL DEY |
| 预测分子量 | 17 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3篇与LSM1重组蛋白相关的虚构参考文献示例(实际文献需根据具体研究补充)：
1. **文献名称**: *"LSM1重组蛋白的克隆表达及其在细胞应激颗粒形成中的作用"*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过基因工程技术在大肠杆菌中表达并纯化了LSM1重组蛋白，验证了其与mRNA的结合活性。实验发现LSM1重组蛋白在细胞应激条件下促进应激颗粒(stress granules)的组装，揭示了其在RNA代谢中的调控机制。
2. **文献名称**: *"LSM1与SM蛋白复合物的体外重组及功能分析"*
**作者**: Lee S, Kim H.
**摘要**: 作者通过体外重组技术构建了LSM1-SM蛋白复合物，并利用pull-down实验证实其与DCP1-DCP2脱帽酶的相互作用。研究证明该复合物通过调控mRNA脱帽过程影响基因表达稳定性。
3. **文献名称**: *"LSM1重组蛋白在癌症细胞中的异常表达及靶向抑制研究"*
**作者**: Wang X, et al.
**摘要**: 通过Western blot和免疫荧光技术，发现LSM1在多种癌症细胞中高表达。利用重组LSM1蛋白进行功能抑制实验，结果显示其缺失可显著降低癌细胞增殖能力，提示其作为潜在治疗靶点。
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注：以上文献为示例性质，实际文献需通过PubMed、Google Scholar等平台检索关键词"LSM1 recombinant protein"或结合具体研究方向补充。真实文献可能涉及LSM1在RNA降解、剪接或病毒免疫应答等领域的功能研究。
LSM1 (Like Sm 1) is a conserved eukaryotic protein belonging to the Sm-like superfamily, characterized by the presence of Sm motifs that facilitate RNA binding. It plays a critical role in RNA metabolism, particularly in mRNA decay and stress granule dynamics. LSM1 functions as part of a heteroheptameric complex (LSM1-7) in the cytoplasm, where it interacts with co-factors like Pat1 and DCP1/2 to promote deadenylation-dependent mRNA decapping, a key step in 5'→3' mRNA degradation. This process is essential for regulating gene expression, eliminating aberrant transcripts, and responding to cellular stress.
Structurally, LSM1 contains two Sm-like domains that mediate interactions with RNA and protein partners. Unlike canonical Sm proteins involved in splicing, LSM1 specializes in cytoplasmic mRNA turnover. Studies link LSM1 to cellular stress responses, as it localizes to stress granules—transient aggregates of stalled translation complexes formed during environmental challenges like heat shock or nutrient deprivation.
Recombinant LSM1 proteins are engineered to study its molecular functions, often expressed in bacterial (e.g., E. coli) or eukaryotic systems for in vitro assays. These tools enable researchers to dissect its RNA-binding specificity, complex assembly, and enzymatic interactions. Notably, LSM1 dysregulation has been implicated in neurodegenerative diseases and cancer, where altered mRNA stability contributes to pathological protein aggregation or uncontrolled proliferation.
Recent research explores LSM1's role in antiviral immunity, as some viruses exploit host mRNA decay machinery. Recombinant LSM1 variants with mutations in RNA-binding sites or interaction domains help map functional regions, informing therapeutic strategies targeting RNA-protein interactions. Its conserved nature across eukaryotes also makes LSM1 a model for studying evolution of RNA surveillance pathways.
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