| 纯度 | >= 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | Arg2 |
| Uniprot No | P78540 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-354aa |
| 氨基酸序列 | SVHSVAVIGA PFSQGQKRKG VEHGPAAIRE AGLMKRLSSL GCHLKDFGDL SFTPVPKDDL YNNLIVNPRS VGLANQELAE VVSRAVSDGY SCVTLGGDHS LAIGTISGHA RHCPDLCVVW VDAHADINTP LTTSSGNLHG QPVSFLLREL QDKVPQLPGF SWIKPCISSA SIVYIGLRDV DPPEHFILKN YDIQYFSMRD IDRLGIQKVM ERTFDLLIGK RQRPIHLSFD IDAFDPTLAP ATGTPVVGGL TYREGMYIAE EIHNTGLLSA LDLVEVNPQL ATSEEEAKTT ANLAVDVIAS SFGQTREGGH IVYDQLPTPS SPDESENQAR VRI |
| 预测分子量 | 38 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Arg2重组蛋白的参考文献及其摘要概括：
1. **《Expression and purification of recombinant human arginase 2 in Escherichia coli》**
- 作者：Kim et al. (2015)
- 摘要：研究报道了通过大肠杆菌表达系统高效表达人源Arg2重组蛋白，并优化了镍柱亲和层析纯化方法，验证了其酶活性和热稳定性。
2. **《Crystal structure of arginase 2 from Homo sapiens》**
- 作者：Dowling et al. (2010)
- 摘要：首次解析了人源Arg2重组蛋白的X射线晶体结构(分辨率2.1Å)，揭示了其锰离子结合位点和底物识别机制，为药物设计提供结构基础。
3. **《Recombinant arginase 2 modulates T cell metabolism and inhibits autoimmune inflammation》**
- 作者：Munder et al. (2020)
- 摘要：通过哺乳动物细胞表达Arg2重组蛋白，证明其通过消耗微环境中的精氨酸抑制T细胞增殖，在实验性自身免疫性脑脊髓炎模型中减轻炎症反应。
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注：以上文献为示例性内容，实际引用时建议通过PubMed或Web of Science核对原文信息。
**Background of Arg2 Recombinant Protein**
Arginase 2 (Arg2), a mitochondrial enzyme encoded by the *ARG2* gene, is a key player in the urea cycle and L-arginine metabolism. It catalyzes the hydrolysis of L-arginine to urea and L-ornithine, regulating cellular polyamine synthesis, nitric oxide (NO) production, and immune responses. Unlike its cytosolic isoform Arg1. Arg2 is expressed ubiquitously, with high activity in the kidney, brain, and immune cells, and is induced under stress conditions such as hypoxia or inflammation.
Recombinant Arg2 protein is engineered through heterologous expression systems (e.g., *E. coli* or mammalian cells*) to study its biochemical properties, structural dynamics, and pathophysiological roles. Structural studies reveal Arg2 functions as a manganese-dependent homodimer, with active sites critical for substrate binding. Its dysregulation is linked to cardiovascular diseases, neurodegenerative disorders, cancer, and immune dysfunctions. For example, in tumors, Arg2 overexpression depletes arginine, impairing T-cell function and promoting immune evasion.
Recombinant Arg2 serves as a tool for drug screening, mechanistic studies, and therapeutic development. Inhibitors targeting Arg2 are explored for cancer immunotherapy and metabolic disorders. Additionally, recombinant Arg2 aids in elucidating cross-talk between arginine metabolism, NO signaling, and mitochondrial function, offering insights into disease mechanisms and precision medicine strategies. Its role in balancing immune activation and suppression further highlights its therapeutic potential in autoimmune diseases and infections.
In summary, Arg2 recombinant protein bridges basic research and clinical translation, advancing our understanding of arginine metabolism in health and disease.
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