纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | RNASE1 |
Uniprot No | P07998 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 29-156aa |
氨基酸序列 | KE SRAKKFQRQH MDSDSSPSSS STYCNQMMRR RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC YKSNSSMHIT DCRLTNGSRY PNCAYRTSPK ERHIIVACEG SPYVPVHFDA SVEDST |
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3篇关于RNASE1重组蛋白的典型文献示例(注:文献标题及作者为模拟,供参考):
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1. **标题**:Recombinant human RNASE1 inhibits tumor angiogenesis through ribonucleolytic activity
**作者**:Smith J, et al.
**摘要**:研究证明重组人RNASE1蛋白通过降解肿瘤微环境中的RNA,抑制内皮细胞迁移和血管生成,显著降低小鼠模型中肿瘤的生长速率。
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2. **标题**:Expression and purification of functional RNASE1 in E. coli for antimicrobial applications
**作者**:Chen L, et al.
**摘要**:开发了利用大肠杆菌高效表达重组RNASE1的方法,纯化后的蛋白展现出对革兰氏阴性菌的选择性抗菌活性,提示其在抗感染治疗中的潜力。
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3. **标题**:Structural analysis of RNASE1 variants reveals key residues for RNA-binding specificity
**作者**:Wang Y, et al.
**摘要**:通过晶体学解析重组RNASE1突变体的结构,发现特定氨基酸残基(如His12、Lys41)对RNA底物识别及催化活性具有关键作用,为工程化改造提供依据。
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(注:以上文献为示例性质,实际文献需通过PubMed/Google Scholar检索关键词如"recombinant RNASE1 protein"、"human ribonuclease 1 expression"等获取。)
**Background of RNASE1 Recombinant Protein**
RNASE1 (Ribonuclease A family member 1) is a secretory enzyme belonging to the pancreatic-type ribonuclease superfamily, renowned for its ability to catalyze RNA hydrolysis. Naturally expressed in the pancreas, it plays a key role in digesting dietary RNA. Beyond digestion, RNASE1 is detected in blood vessels, immune cells, and other tissues, suggesting roles in angiogenesis, host defense, and cellular homeostasis. Its structure features a compact globular fold stabilized by four disulfide bonds, contributing to remarkable thermal stability and enzymatic activity under diverse physiological conditions.
Recombinant RNASE1 is produced via genetic engineering, typically using *E. coli* or eukaryotic expression systems, enabling large-scale, high-purity production. Advanced purification techniques, such as affinity chromatography, ensure homogeneity and bioactivity. The recombinant protein retains the catalytic properties of its native counterpart, cleaving RNA at specific pyrimidine sites, making it invaluable for molecular biology applications, including RNA degradation studies, nucleic acid purification, and quality control in RNA-based therapeutics.
Research highlights RNASE1's therapeutic potential. Its ability to degrade extracellular RNA—a mediator of inflammation and thrombosis—positions it as a candidate for treating cardiovascular diseases, sepsis, or COVID-19-related complications. Additionally, engineered variants with enhanced cytotoxicity or targeting motifs are explored for anticancer therapies, leveraging RNA degradation to induce selective tumor cell death. Challenges remain in optimizing stability, minimizing immunogenicity, and improving tissue-specific delivery.
As a tool, recombinant RNASE1 aids in studying RNA-protein interactions, enzymatic mechanisms, and disease pathways. Its versatility and evolutionary conservation across species underscore its broad relevance in both basic research and translational medicine.
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