| 纯度 | >90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ARG1 |
| Uniprot No | P05089 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-322aa |
| 氨基酸序列 | MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT LACFGLAREG NHKPIDYLNP PK |
| 预测分子量 | 36 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ARG1重组蛋白的3篇参考文献及其摘要概括(文献为示例性描述，非真实存在)：
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1. **标题**: *"High-Yield Expression and Purification of Recombinant Human Arginase 1 in E. coli for Therapeutic Applications"*
**作者**: Zhang, L. et al.
**摘要**: 研究报道了在大肠杆菌系统中高效表达人源ARG1重组蛋白的优化方法，通过亲和层析纯化获得高纯度蛋白，并验证其酶活性和稳定性，为肿瘤免疫治疗提供候选药物。
2. **标题**: *"Structural Insights into Recombinant Arginase 1: Implications for Substrate Binding and Catalytic Mechanism"*
**作者**: Thompson, R. & Kumar, S.
**摘要**: 利用X射线晶体学解析了重组ARG1的三维结构，揭示了其锰离子结合位点及底物识别机制，为设计靶向ARG1的抑制剂奠定基础。
3. **标题**: *"Recombinant Arginase 1 Attenuates T-cell Activation in Autoimmune Disease Models"*
**作者**: Chen, Y. et al.
**摘要**: 评估了重组ARG1在体外和小鼠自身免疫模型中的免疫抑制功能，证明其通过耗竭局部精氨酸抑制T细胞增殖，缓解炎症反应。
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如需真实文献，建议在PubMed或Web of Science中检索关键词“recombinant arginase 1”或“ARG1 protein expression”。
**ARG1 Recombinant Protein Background**
Arginase-1 (ARG1) is a manganese-dependent enzyme that plays a critical role in the urea cycle, primarily expressed in the liver. It catalyzes the hydrolysis of L-arginine into L-ornithine and urea, a key step in detoxifying ammonia, a byproduct of nitrogen metabolism. Beyond its metabolic function, ARG1 is implicated in immune regulation, cell proliferation, and tissue repair, with emerging roles in pathologies such as cancer, cardiovascular diseases, and immune disorders.
Recombinant ARG1 protein is produced using biotechnological methods, often through expression in bacterial (e.g., *E. coli*) or mammalian cell systems. This engineered protein retains the enzymatic activity and structural features of native ARG1. enabling its use in biochemical and clinical research. Purification typically involves affinity chromatography, followed by refolding or post-translational modifications to ensure functionality.
In research, recombinant ARG1 serves as a tool to study urea cycle disorders, such as ARG1 deficiency—a rare genetic disease causing hyperargininemia. It also aids in exploring arginine metabolism's impact on immune cells (e.g., macrophages, T cells) and tumor microenvironments, where ARG1-mediated arginine depletion can suppress anti-tumor responses. Therapeutically, recombinant ARG1 is investigated for enzyme replacement therapy and as a potential modulator in diseases linked to dysregulated arginine pathways.
Quality assessments include activity assays, SDS-PAGE for purity, and mass spectrometry to confirm molecular weight (~35 kDa). Its applications span drug development, diagnostic studies, and mechanistic investigations into metabolic or immune-related conditions. By providing a controlled and scalable source of functional ARG1. recombinant protein technology advances both basic science and translational medicine.
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