| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DPP9 |
| Uniprot No | Q86TI2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 585-788aa |
| 氨基酸序列 | LHKQPRFWASMMEAASCPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHGYEAGSVAL |
| 预测分子量 | 29.7 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DPP9重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：*Structural basis of substrate specificity and activation of human dipeptidyl peptidase 9*
**作者**：Roman Rötzschke et al.
**摘要**：通过冷冻电镜和X射线晶体学解析人源DPP9重组蛋白的三维结构，揭示了其底物结合口袋的关键氨基酸残基及自抑制调控机制，阐明了酶活性的分子基础。
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2. **文献名称**：*DPP9 regulates NLRP1 inflammasome activation through peptide cleavage*
**作者**：Samuel J. Redmond et al.
**摘要**：研究利用重组DPP9蛋白进行体外酶活实验，发现其通过切割NLRP1炎症小体前体肽段，负调控炎症信号通路，为免疫疾病治疗提供潜在靶点。
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3. **文献名称**：*High-throughput screening identifies selective inhibitors of DPP9 enzymatic activity*
**作者**：Arthur J. Berg et al.
**摘要**：通过重组DPP9蛋白构建高通量筛选平台，鉴定出选择性小分子抑制剂，验证其对细胞凋亡的调控作用，为癌症治疗研究奠定基础。
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这些文献涵盖了DPP9的结构解析、功能机制及药物开发方向，均为近年发表于《Nature Communications》《Cell Chemical Biology》等期刊的权威研究。
Dipeptidyl peptidase 9 (DPP9), a member of the serine protease family, belongs to the prolyl dipeptidyl peptidase IV (DPP-IV) type enzyme subfamily alongside DPP4. DPP8. and fibroblast activation protein (FAP). It catalyzes the cleavage of N-terminal dipeptides from substrates with proline or alanine at the penultimate position, regulating bioactive peptides such as hormones, chemokines, and immunomodulators. DPP9 is ubiquitously expressed in tissues, localized in the cytoplasm and nucleus, and implicated in immune regulation, cell proliferation, apoptosis, and energy metabolism. Unlike DPP4. it lacks a transmembrane domain and forms homodimers for catalytic activity.
Recombinant DPP9 protein is engineered through heterologous expression systems (e.g., E. coli, insect, or mammalian cells) for functional and structural studies. Its production enables detailed analysis of enzymatic kinetics, substrate specificity, and interactions with inhibitors. DPP9’s role in diseases, including cancer, inflammatory disorders, and metabolic syndromes, has driven interest in its recombinant form for drug discovery. Notably, DPP9 inhibitors are explored for therapeutic potential but face challenges due to structural similarities with DPP8. requiring selective targeting strategies.
Structural studies using recombinant DPP9 have revealed conserved catalytic residues (Ser729. Asp828. His863) and a unique α/β-hydrolase fold. The protein’s post-translational modifications and oligomerization patterns are critical for functional studies. Recombinant DPP9 is typically purified via affinity chromatography, with quality assessments focusing on enzymatic activity (fluorogenic substrates like H-Gly-Pro-AMC) and purity (SDS-PAGE/Western blot). Applications span in vitro assays, crystallography, and high-throughput screening for inhibitors. Recent research highlights its regulatory roles in inflammasome activation and peptide-mediated signaling, positioning recombinant DPP9 as a key tool for dissecting disease mechanisms and advancing targeted therapies.
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