| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASE7 |
| Uniprot No | Q9H1E1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-156aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSKPKGMTS SQWFKIQHMQ PSPQACNSAM KNINKHTKRC KDLNTFLHEP FSSVAATCQT PKIACKNGDK NCHQSHGPVS LTMCKLTSGK YPNCRYKEKR QNKSYVVACK PPQKKDSQQF HLVPVHLDRV L |
| 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. |
以下是关于RNASE7重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: *RNase 7. a novel innate immune defense antimicrobial protein of healthy human skin*
**作者**: Harder J, et al.
**摘要**: 该研究首次克隆并表达了重组RNASE7蛋白，发现其在人类皮肤中高表达，对多种病原菌(如大肠杆菌和白色念珠菌)具有强效抗菌活性，揭示了其在皮肤先天免疫中的关键作用。
2. **文献名称**: *Ribonuclease 7 functions as an antimicrobial peptide in the human urinary tract by targeting Escherichia coli and Proteus mirabilis*
**作者**: Becknell B, et al.
**摘要**: 研究利用重组RNASE7蛋白进行体外实验，证明其能有效抑制尿路感染常见病原体(如大肠杆菌和奇异变形杆菌)，并发现其抗菌活性依赖于其核糖核酸酶结构域。
3. **文献名称**: *Ribonuclease 7 downregulates TH17 cytokines and promotes wound healing in bacterial infections*
**作者**: Koczera P, et al.
**摘要**: 通过重组RNASE7蛋白实验，发现其不仅直接杀菌，还可调节宿主免疫反应，抑制IL-17等促炎因子分泌，加速金黄色葡萄球菌感染伤口的愈合过程。
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*注：以上文献为领域内代表性研究，实际引用时建议通过PubMed/Google Scholar核对具体信息。*
RNASE7. a member of the ribonuclease A (RNASE) superfamily, is a cationic peptide with broad-spectrum antimicrobial activity that plays a critical role in innate immunity. First identified in human skin, it is constitutively expressed by epithelial cells at mucosal surfaces (respiratory, urinary, and gastrointestinal tracts) and barrier tissues, serving as a first-line defense against pathogens. Unlike other RNASE family members primarily involved in RNA metabolism, RNASE7 demonstrates potent microbicidal effects through both enzymatic and non-enzymatic mechanisms. Its conserved ribonuclease domain, stabilized by disulfide bonds, enables selective cleavage of microbial RNA while remaining relatively non-toxic to host cells.
Recombinant RNASE7 proteins are engineered using expression systems like E. coli or mammalian cells to study its structure-function relationships and therapeutic potential. Studies reveal its effectiveness against clinically relevant bacteria (e.g., Pseudomonas aeruginosa, Staphylococcus aureus), fungi (Candida spp.), and enveloped viruses. The antimicrobial action involves membrane disruption via electrostatic interactions between its positively charged surface and negatively charged microbial membranes, coupled with RNA degradation activity. Interestingly, some antimicrobial effects persist even when enzymatic activity is inhibited, suggesting additional mechanisms like biofilm disruption.
Research highlights RNASE7's dual role in infection control and immune modulation, with upregulated expression during inflammation. Recombinant variants are being explored as topical antimicrobials, particularly for antibiotic-resistant infections and wound healing. Challenges include optimizing stability and delivery while minimizing cytotoxicity. Current investigations focus on engineering RNASE7 derivatives with enhanced selectivity and exploring synergistic effects with conventional antibiotics, positioning it as a promising candidate for novel anti-infective strategies.
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