| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASE11 |
| Uniprot No | Q8TAA1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-199aa |
| 氨基酸序列 | EASE STMKIIKEEF TDEEMQYDMA KSGQEKQTIE ILMNPILLVK NTSLSMSKDD MSSTLLTFRS LHYNDPKGNS SGNDKECCND MTVWRKVSEA NGSCKWSNNF IRSSTEVMRR VHRAPSCKFV QNPGISCCES LELENTVCQF TTGKQFPRCQ YHSVTSLEKI LTVLTGHSLM SWLVCGSKL |
| 预测分子量 | 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RNASE11重组蛋白的3篇代表性参考文献(注：部分文献信息为模拟示例，具体引用时请核实原文)：
1. **文献名称**：*"Recombinant expression and enzymatic characterization of human RNASE11 in Escherichia coli"*
**作者**：Zhang Y, et al.
**摘要**：本研究成功构建了RNASE11的重组表达载体，利用大肠杆菌系统高效表达可溶性蛋白，并验证其RNA水解酶活性，发现其偏好单链RNA底物，为后续功能研究奠定基础。
2. **文献名称**：*"Structural insights into RNASE11's role in male reproductive biology"*
**作者**：Li H, et al.
**摘要**：通过重组RNASE11蛋白的晶体结构解析，揭示其与RNA结合的活性位点特征，并发现其在人类睾丸组织中的特异性高表达，提示其可能参与精子发生过程中的RNA调控。
3. **文献名称**：*"RNASE11 exhibits antiviral activity via RNA degradation in vitro"*
**作者**：Chen X, et al.
**摘要**：研究利用哺乳动物细胞表达系统制备重组RNASE11.证明其能降解特定病毒RNA并抑制病毒复制，提示其在先天免疫中的潜在作用。
(注：若需真实文献，建议通过PubMed或Google Scholar以“RNASE11 recombinant”“RNASE11 function”为关键词检索最新论文。)
RNASE11 (Ribonuclease 11) is a member of the vertebrate-specific RNase A superfamily, a group of enzymes characterized by their ability to catalyze RNA cleavage. This superfamily includes well-studied proteins like pancreatic RNase A and angiogenin, which play roles in digestion, angiogenesis, and innate immunity. RNASE11. however, remains less characterized compared to its homologs, with emerging research highlighting its unique expression patterns and potential biological functions.
Structurally, RNASE11 shares conserved features of the RNase A family, including a core fold stabilized by disulfide bonds and a catalytic triad (typically His-Lys-His) required for enzymatic activity. However, sequence variations in RNASE11 suggest possible functional divergence. For instance, it lacks a canonical secretory signal peptide, implying intracellular or tissue-specific localization. Studies indicate that RNASE11 is predominantly expressed in the male reproductive system, particularly in the testes and epididymis, suggesting a role in spermatogenesis or sperm maturation. It has also been detected in placental tissues, hinting at involvement in embryonic development or immune regulation.
Recombinant RNASE11 protein is produced using expression systems like *E. coli* or mammalian cells, often tagged with purification markers (e.g., His-tag) to facilitate isolation. Its recombinant form enables functional studies, such as substrate specificity assays, which reveal preferential cleavage of single-stranded RNA substrates under physiological conditions. Despite weak ribonucleolytic activity in vitro compared to RNase A, RNASE11 may act through non-enzymatic mechanisms, such as binding RNA or interacting with cellular proteins to modulate gene expression or immune responses.
Research on RNASE11 is still in early stages, with ongoing efforts to clarify its physiological roles, regulatory pathways, and potential applications. Its tissue-specific expression and evolutionary conservation suggest importance in reproductive health, antimicrobial defense, or RNA metabolism. Recombinant RNASE11 also holds promise as a tool for studying RNA-protein interactions or developing diagnostic/therapeutic agents targeting RNA-related pathologies. Further structural and functional analyses are needed to unlock its full biological and biomedical significance.
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