| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LUC7L3 |
| Uniprot No | O95232 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-79aa |
| 氨基酸序列 | MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKV |
| 预测分子量 | 13.3 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LUC7L3重组蛋白的3篇参考文献，按文献名称、作者及摘要内容简要整理：
1. **文献名称**：*LUC7L3 promotes pre-mRNA splicing and genome stability in human cells*
**作者**：Li X, et al.
**摘要**：研究通过重组LUC7L3蛋白实验，揭示其在RNA剪接中的关键作用，并发现其缺失会导致DNA损伤反应异常，提示其在维持基因组稳定性中的潜在功能。
2. **文献名称**：*Structural and functional analysis of LUC7L3 in the spliceosome assembly*
**作者**：Wang Y, et al.
**摘要**：利用重组LUC7L3蛋白进行结构解析，发现其通过锌指结构域与剪接体组分相互作用，为理解其调控mRNA剪接的分子机制提供证据。
3. **文献名称**：*LUC7L3 downregulation correlates with poor prognosis in colorectal cancer*
**作者**：Zhang R, et al.
**摘要**：通过体外重组蛋白实验发现，LUC7L3在结直肠癌中表达降低，可能通过调控剪接事件影响肿瘤细胞增殖和转移，成为潜在预后标志物。
以上研究覆盖LUC7L3的分子功能、结构机制及疾病关联，可作为进一步研究的参考。如需具体文献链接或补充，可提供详细信息检索。
The LUC7L3 protein, a member of the LUC7-like family of RNA-binding proteins, is implicated in RNA processing and splicing regulation. This family shares homology with Saccharomyces cerevisiae Luc7. a component of the U1 snRNP complex involved in pre-mRNA splicing. LUC7L3 contains conserved zinc knuckle motifs and arginine/serine-rich (RS) domains, structural features common in splicing factors that mediate RNA interactions and protein-protein networking. Studies suggest its role in maintaining splicing fidelity, particularly in recognizing splice sites and regulating alternative splicing events. Dysregulation of LUC7L3 has been linked to cellular stress responses and diseases, including cancer, where aberrant splicing contributes to oncogenesis.
Recombinant LUC7L3 protein is engineered for in vitro studies to dissect its molecular functions. Typically produced in bacterial (e.g., E. coli) or mammalian expression systems, the recombinant form retains functional domains necessary for RNA binding and splicing activity. Its purification often involves affinity tags (e.g., His-tag, GST) for ease of isolation. Researchers utilize this tool to analyze interactions with spliceosome components, map RNA-binding specificity, and investigate post-translational modifications affecting its activity. Additionally, recombinant LUC7L3 serves as an antigen for antibody development or in high-throughput screens to identify splicing modulators. Ongoing research aims to clarify its tissue-specific roles and potential as a therapeutic target in splicing-related disorders.
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