| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASE8 |
| Uniprot No | Q8TDE3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-154aa |
| 氨基酸序列 | KPK DMTSSQWFKT QHVQPSPQAC NSAMSIINKY TERCKDLNTF LHEPFSSVAI TCQTPNIACK NSCKNCHQSH GPMSLTMGEL TSGKYPNCRY KEKHLNTPYI VACDPPQQGD PGYPLVPVHL DKVV |
| 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RNASE8重组蛋白的参考文献示例(注：以下内容为假设性示例，实际文献需根据具体数据库检索)：
1. **文献名称**：*Recombinant Expression and Antimicrobial Characterization of Human RNASE8 in Escherichia coli*
**作者**：Zhang L, Wang Y, Liu X
**摘要**：本研究成功在大肠杆菌系统中表达了重组人RNASE8蛋白，并对其进行了纯化和功能分析。实验表明，重组RNASE8对多种革兰氏阴性菌表现出显著的抗菌活性，提示其在先天免疫防御中的潜在作用。
2. **文献名称**：*Structural and Functional Insights into RNASE8 via Recombinant Protein Crystallography*
**作者**：Chen H, Li J, Xu M
**摘要**：通过重组RNASE8蛋白的晶体结构解析，揭示了其与RNASE A家族其他成员的结构差异。功能实验表明，其独特的活性位点可能与其在黏膜免疫中的特异性功能相关。
3. **文献名称**：*Role of Recombinant RNASE8 in Host Defense Against Fungal Pathogens*
**作者**：Kim S, Park T, Lee K
**摘要**：本研究利用重组RNASE8蛋白，证实其通过破坏真菌细胞壁发挥抗白色念珠菌活性，为开发新型抗真菌药物提供了理论依据。
4. **文献名称**：*Expression Optimization and Biophysical Characterization of Recombinant RNASE8 for Therapeutic Applications*
**作者**：Gupta R, Sharma A, Patel S
**摘要**：通过优化表达条件提高了重组RNASE8的产量，并对其稳定性、折叠及生物物理特性进行了系统分析，为其作为抗菌疗法的临床应用奠定基础。
建议通过PubMed、Google Scholar等平台以“RNASE8 recombinant protein”、“RNASE8 expression and function”等关键词检索真实文献。
**Background of RNASE8 Recombinant Protein**
RNASE8 (Ribonuclease 8) is a member of the ribonuclease A (RNASE A) superfamily, a group of secreted enzymes characterized by their ability to cleave RNA. This superfamily plays diverse roles in vertebrate biology, including RNA metabolism, host defense, and angiogenesis. RNASE8. initially identified through genomic analyses, shares structural homology with other family members, such as RNASE1 and RNASE3 (eosinophil-derived neurotoxin), but exhibits distinct tissue-specific expression patterns. It is primarily expressed in the male and female reproductive systems, as well as the placenta, suggesting potential roles in reproductive biology and innate immunity.
Functionally, RNASE8 is hypothesized to contribute to microbial defense in mucosal surfaces, leveraging its ribonucleolytic activity to degrade viral or bacterial RNA. Unlike some RNASE A members (e.g., RNASE2/3), RNASE8 lacks pronounced cytotoxic or angiogenic properties, but its enzymatic activity and tissue localization imply specialized roles in protecting reproductive and gestational tissues from pathogens. Studies also suggest its involvement in modulating immune responses, though detailed mechanisms remain under investigation.
Recombinant RNASE8 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, bioactive protein for functional studies. Its recombinant form enables researchers to explore its enzymatic kinetics, substrate specificity, and interactions with microbial or host molecules. Structural analyses reveal conserved catalytic residues (e.g., His-Lys-His motifs) critical for RNA cleavage, alongside unique sequence features that may influence substrate binding or tissue targeting.
Research on RNASE8 recombinant protein holds promise for understanding its physiological roles, particularly in reproductive immunity, and may inform therapeutic strategies targeting infections or inflammatory conditions in urogenital and placental contexts. Further studies are needed to clarify its regulatory mechanisms and potential clinical applications.
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