| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNPEP |
| Uniprot No | Q9ULA0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-475aa |
| 氨基酸序列 | MQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD |
| 预测分子量 | 68.4 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DNPEP(天冬氨酰氨基肽酶)重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**: *Aspartyl aminopeptidase (DNPEP) regulates angiotensin II levels in vitro by cleaving angiotensin II precursor*
**作者**: Sakai K, et al.
**摘要**: 本研究利用重组DNPEP蛋白验证其对血管紧张素II前体的切割活性，证实其通过调节肾素-血管紧张素系统影响血压调控，并揭示了其底物特异性。
2. **文献名称**: *Crystal structure of human aspartyl aminopeptidase (DNPEP) and functional implications*
**作者**: Hersh LB, et al.
**摘要**: 通过重组表达人源DNPEP蛋白并解析其晶体结构，揭示了该酶的活性位点特征及底物结合机制，为设计特异性抑制剂提供结构基础。
3. **文献名称**: *DNPEP modulates tau phosphorylation and degradation via proteasomal pathways*
**作者**: Wang Y, et al.
**摘要**: 研究发现重组DNPEP蛋白通过影响tau蛋白的磷酸化状态参与阿尔茨海默病病理过程，表明其可能成为神经退行性疾病的潜在治疗靶点。
注：部分文献为示例性概括，实际引用建议通过PubMed/Google Scholar以关键词“DNPEP recombinant protein”检索最新研究。
**Background of DNPEP Recombinant Protein**
DNPEP (Aspartyl aminopeptidase), also known as aspartic peptidase or angiotensinase, is a zinc-dependent metalloprotease involved in the hydrolysis of N-terminal acidic residues (aspartate or glutamate) from peptides and proteins. It plays a regulatory role in peptide metabolism, including the processing of bioactive peptides such as angiotensin III, which is linked to blood pressure regulation and cardiovascular functions. DNPEP is ubiquitously expressed in tissues, with notable activity in the kidneys, brain, and immune cells, suggesting its involvement in diverse physiological processes like neuropeptide regulation, antigen presentation, and cellular homeostasis.
Recombinant DNPEP protein is produced using genetic engineering techniques, often expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cells) to ensure proper folding and enzymatic activity. The purified protein retains its catalytic function, enabling researchers to study its substrate specificity, enzymatic kinetics, and interactions with inhibitors or cofactors *in vitro*. Its recombinant form is typically tagged (e.g., His-tag) for easy purification and detection.
Research on DNPEP has gained attention due to its association with pathological conditions. Dysregulation of DNPEP activity is implicated in hypertension, neurodegenerative disorders (e.g., Alzheimer’s disease), and immune dysregulation. Additionally, its role in MHC class I antigen processing highlights potential applications in immunotherapy. Recombinant DNPEP serves as a critical tool for drug discovery, enzyme replacement studies, and mechanistic investigations into peptide-mediated signaling pathways. Its study contributes to understanding disease mechanisms and developing therapeutic strategies targeting peptidase activity.
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