| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ENPEP |
| Uniprot No | Q07075 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 719-949aa |
| 氨基酸序列 | YFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREW |
| 预测分子量 | 31.0kDa |
| 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ENPEP重组蛋白的3篇参考文献及其摘要概括(文献信息为模拟示例，实际需根据真实文献调整)：
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1. **文献名称**: *"Expression and Functional Characterization of Recombinant Human Glutamyl Aminopeptidase (ENPEP) in Mammalian Cells"*
**作者**: Smith J, et al.
**摘要**: 研究报道了通过哺乳动物表达系统(如HEK293细胞)重组表达人源ENPEP蛋白的方法，验证了其酶活性和在血管生成中的作用，证实重组ENPEP可促进内皮细胞迁移，为靶向治疗提供实验基础。
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2. **文献名称**: *"Purification and Structural Analysis of ENPEP Recombinant Protein for Cancer Biomarker Studies"*
**作者**: Lee H, et al.
**摘要**: 描述了从大肠杆菌中高效纯化重组ENPEP蛋白的工艺，通过X射线晶体学解析其三维结构，并发现其在多种肿瘤细胞表面过表达，提示其作为癌症诊断标志物的潜力。
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3. **文献名称**: *"Role of Recombinant ENPEP in Regulating Immune Cell Infiltration in Solid Tumors"*
**作者**: Garcia R, et al.
**摘要**: 利用重组ENPEP蛋白研究其在肿瘤微环境中的作用，发现其通过调控趋化因子活性影响巨噬细胞和T细胞的浸润，为免疫治疗靶点开发提供新方向。
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**备注**：以上文献为示例，实际引用需通过PubMed、Web of Science等平台检索关键词(如“ENPEP recombinant protein”“CD13 expression”)获取真实文献。如需进一步协助定位具体论文，请提供更多研究背景。
**Background of ENPEP Recombinant Protein**
ENPEP (glutamyl aminopeptidase), also known as aminopeptidase A, is a membrane-bound metalloprotease that plays a critical role in regulating bioactive peptides, particularly in the renin-angiotensin system (RAS). It catalyzes the hydrolysis of angiotensin II to angiotensin III, influencing blood pressure regulation, vascular tone, and fluid balance. ENPEP is also implicated in cellular processes such as angiogenesis, inflammation, and cancer progression, where its expression correlates with tumor invasiveness and metastasis.
Recombinant ENPEP protein is produced using biotechnological methods, typically through expression in mammalian or insect cell systems to ensure proper post-translational modifications and enzymatic activity. This engineered protein retains the functional domains necessary for substrate binding and catalysis, making it a valuable tool for studying ENPEP's biochemical mechanisms, substrate specificity, and interactions with inhibitors.
Research applications of ENPEP recombinant protein include elucidating its role in cardiovascular diseases, cancer biology, and immune regulation. It is also used in drug discovery to screen and validate potential therapeutic inhibitors targeting hypertension or malignancies. Additionally, ENPEP serves as an antigen in immunoassays and antibody development for diagnostic or therapeutic purposes.
The availability of recombinant ENPEP has advanced mechanistic studies and therapeutic exploration, highlighting its dual significance as a physiological regulator and a biomarker in pathological conditions. Ongoing research aims to leverage its enzymatic activity for innovative treatments in precision medicine.
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