| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ARG |
| Uniprot No | Q8N6T3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-406aa |
| 氨基酸序列 | MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLSFVRSVTMDKWKDIELEKMKAGGNAKFREFLESQEDYDPCWSLQEKYNSRAAALFRDKVVALAEGREWSLESSPAQNWTPPQPRTLPSMVHRVSGQPQSVTASSDKAFEDWLNDDLGSYQGAQGNRYVGFGNTPPPQKKEDDFLNNAMSSLYSGWSSFTTGASRFASAAKEGATKFGSQASQKASELGHSLNENVLKPAQEKVKEGKIFDDVSSGVSQLASKVQGVGSKGWRDVTTFFSGKAEGPLDSPSEGHSYQNSGLDHFQNSNIDQSFWETFGSAEPTKTRKSPSSDSWTCADTSTERRSSDSWEVWGSASTNRNSNSDGGEGGEGTKKAVPPAVPTDDGWDNQNW |
| 预测分子量 | 45.5 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. |
以下是关于重组ARG(精氨酸酶)蛋白的3篇示例参考文献(内容为模拟生成，实际文献请通过学术数据库查询)：
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1. **文献名称**：重组人精氨酸酶I的高效表达与纯化
**作者**：Zhang L., Wang Y., et al.
**摘要**：本研究通过在大肠杆菌表达系统中克隆并优化人精氨酸酶I(rhARG I)基因，利用亲和层析技术纯化获得高活性重组蛋白。实验表明，重组rhARG I在体外具有与天然酶相似的催化效率，为后续肿瘤治疗研究奠定基础。
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2. **文献名称**：精氨酸酶的结构解析及其重组蛋白的酶学特性
**作者**：Smith J., Tanaka K., et al.
**摘要**：通过X射线晶体学解析了重组精氨酸酶的三维结构，揭示了其活性中心的关键氨基酸残基。进一步酶动力学实验表明，重组蛋白在pH 7.4时活性最高，且对精氨酸的Km值为2.1 mM，提示其在代谢疾病模型中的应用潜力。
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3. **文献名称**：重组精氨酸酶在肿瘤微环境中的抗增殖效应
**作者**：Kim S., Chen R., et al.
**摘要**：利用哺乳动物细胞表达系统制备重组精氨酸酶，并验证其在体外降低肿瘤细胞精氨酸浓度的能力。实验证明，该蛋白可通过诱导精氨酸耗竭抑制黑色素瘤细胞增殖，且在小鼠模型中表现出低免疫原性。
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**提示**：实际研究中请通过PubMed、Web of Science或Google Scholar等平台，以关键词“recombinant arginase”、“ARG1 protein expression”等检索最新文献，并核实作者与期刊信息。
**Background of ARG Recombinant Proteins**
Arginase (ARG) is a metalloenzyme that plays a critical role in the urea cycle, catalyzing the hydrolysis of L-arginine into L-ornithine and urea. This reaction is essential in nitrogen metabolism, particularly in the liver, where it aids in detoxifying ammonia. Beyond its metabolic functions, arginase has gained attention in immunology and disease research due to its regulatory roles in immune responses, cellular proliferation, and pathogen defense.
Recombinant ARG proteins are engineered versions of the enzyme produced via genetic engineering techniques. By cloning the ARG gene into expression systems such as *E. coli*, yeast, or mammalian cells, researchers can produce large quantities of purified, bioactive arginase. This approach allows for precise control over protein properties, including isoform specificity (ARG1 vs. ARG2), post-translational modifications, and stability, which are crucial for both research and therapeutic applications.
ARG recombinant proteins are widely used to study conditions linked to dysregulated arginine metabolism, such as cancer, cardiovascular diseases, and immune disorders. For example, certain tumors overexpress arginase to deplete local arginine, suppressing T-cell activity and evading immune surveillance. Recombinant ARG tools help unravel these mechanisms and test therapeutic strategies, including enzyme inhibitors or arginase-based therapies.
In biotechnology, recombinant ARG enzymes are explored for industrial applications, such as biosensors for arginine detection or biocatalysts in chemical synthesis. Additionally, microbial arginases are studied for their role in pathogenicity, offering targets for antimicrobial drug development.
Despite their utility, challenges remain, such as optimizing enzyme activity under physiological conditions or minimizing off-target effects in therapeutic contexts. Ongoing research focuses on engineering arginase variants with enhanced catalytic efficiency, stability, and tissue-specific targeting. Overall, recombinant ARG proteins serve as versatile tools bridging basic science, medicine, and industrial innovation.
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